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Entry version 35 (18 Sep 2019)
Sequence version 2 (23 Mar 2010)
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Protein

Hapless 2

Gene

HAP2

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

During fertilization, required on male (minus) gametes for their fusion with female (plus) gametes (PubMed:18367645, PubMed:20335357, PubMed:25655701, PubMed:28235200). Required for membrane fusion, but not for the initial adhesion between gametes (PubMed:18367645, PubMed:25655701, PubMed:28235200). Inserts (via its extracellular domain) into lipid membranes (in vitro) (PubMed:28235200). Probably initiates the fusion of gamete cell membranes by inserting its extracellular domain into the cell membrane of a female gamete (PubMed:28235200).4 Publications

Miscellaneous

HAP2/GCS1 family members mediate membrane fusion between gametes in a broad range of eukaryotes, ranging from algae and higher plants to protozoans and cnidaria, suggesting they are derived from an ancestral gamete fusogen (PubMed:20080406). They function similar to viral fusogens, by inserting part of their extracellular domain into the lipid bilayer of an adjoining cell (PubMed:28235200).1 Publication1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processFertilization
LigandLipid-binding

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.N.3.1.6 the hapless2 male gamete fusion factor (fusexin) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Hapless 2
Short name:
HAP21 Publication
Alternative name(s):
Generative cell specific-11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HAP22 PublicationsImported
Synonyms:GCS11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3055 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini23 – 630ExtracellularCuratedAdd BLAST608
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei631 – 651HelicalSequence analysisAdd BLAST21
Topological domaini652 – 1139CytoplasmicCuratedAdd BLAST488

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasmic vesicle, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

No effect on normal adhesion of male (minus) gametes and female (plus) gametes, but the gametes fail to fuse and to give rise to quadriflagellated zygotes.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi184 – 186Missing : No effect on expression at the cell surface. Abolishes ability to mediate gamete fusion. 1 Publication3
Mutagenesisi185 – 186RA → AR: No effect on expression at the cell surface. Abolishes ability to mediate gamete fusion. 1 Publication2
Mutagenesisi185R → A or Q: No effect on expression at the cell surface. Impairs ability to bind to lipid membranes. Abolishes ability to mediate gamete fusion. 1 Publication1
Mutagenesisi185R → K: No effect on expression at the cell surface. No effect on binding to lipid membranes and on ability to mediate gamete fusion. 1 Publication1
Mutagenesisi192 – 193FW → AA: No effect on expression at the cell surface. Nearly abolishes ability to bind lipid membranes. Decreases ability to mediate gamete fusion. 1 Publication2
Mutagenesisi366C → A: Decreases expression at the cell surface. Decreases ability to mediate gamete fusion. 1 Publication1
Mutagenesisi367D → A: No effect on expression at the cell surface. No effect on ability to mediate gamete fusion. 1 Publication1
Mutagenesisi368K → A, M or R: No effect on expression at the cell surface. No effect on ability to mediate gamete fusion. 1 Publication1
Mutagenesisi372G → A: No effect on expression at the cell surface. No effect on ability to mediate gamete fusion. 1 Publication1
Mutagenesisi391L → G: Abolishes expression at the cell surface. Abolishes ability to mediate gamete fusion; when associated with P-394. 1 Publication1
Mutagenesisi394Q → P: Abolishes expression at the cell surface. Abolishes ability to mediate gamete fusion; when associated with G-391. 1 Publication1
Mutagenesisi661 – 662CC → SS: No effect on expression at the cell surface mating structure. Abolishes ability to mediate gamete fusion. 1 Publication2
Mutagenesisi661C → S: No effect on expression at the cell surface mating structure. Slightly decreases ability to mediate gamete fusion. 1 Publication1
Mutagenesisi662C → S: No effect on expression at the cell surface mating structure. No effect on ability to mediate gamete fusion. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22Sequence analysisAdd BLAST22
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500266863223 – 1139Hapless 2Add BLAST1117

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi33 ↔ 44Combined sources1 Publication
Disulfide bondi136 ↔ 164Combined sources1 Publication
Disulfide bondi147 ↔ 210Combined sources1 Publication
Disulfide bondi165 ↔ 383Combined sources1 Publication
Disulfide bondi167 ↔ 190Combined sources1 Publication
Disulfide bondi366 ↔ 390Combined sources1 Publication
Disulfide bondi475 ↔ 482Combined sources1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi497N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi515 ↔ 556Combined sources1 Publication
Glycosylationi577O-linked (GlcNAc...) threonineCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The protein present at the cell membrane is rapidly degraded after fusion between male (minus) and female (plus) gametes, contrary to the protein present in intracellular pools (PubMed:20335357). This may represent a mechanism to avoid fusion of several male gametes with a single female gamete (Probable).Curated1 Publication
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
A4GRC6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Detected on male (minus) gametes (at protein level) (PubMed:20335357, PubMed:25655701, PubMed:28235200). Detected at low levels in vegetative cells. Highly expressed in male (minus) gametes, with low expression in female (plus) gametes (PubMed:16378100).4 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Homotrimer. Membrane contact and insertion (via its extracellular domain) into a lipid membrane probably triggers trimerization.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
3055.EDP01230

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11139
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A4GRC6

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi588 – 1124Gly-richPROSITE-ProRule annotationAdd BLAST537
Compositional biasi888 – 905Pro-richPROSITE-ProRule annotationAdd BLAST18
Compositional biasi976 – 990Pro-richPROSITE-ProRule annotationAdd BLAST15

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Both the cytoplasmic and the extracellular domain are required for normal trafficking to the cell surface, and thus for fertilization (PubMed:25655701). The extracellular domain can insert itself into lipid membranes, probably as a trimer (PubMed:28235200). The extracellular domain has structural similarity to class II viral fusion proteins.2 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the HAP2/GCS1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IX3U Eukaryota
ENOG4111J3I LUCA

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR040326 HAP2/GCS1
IPR018928 HAP2/GCS1_dom

The PANTHER Classification System

More...
PANTHERi
PTHR31764 PTHR31764, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF10699 HAP2-GCS1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

A4GRC6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MCRAIAVALI VYLAQHYILA HAEVIASGRL EKCVVDGVTE ELDCQEKVVV
60 70 80 90 100
TLTVGNGQSL QTEALEFSLS CLNSPDGRCP CSCSAADPTC ACRDLAAPLR
110 120 130 140 150
VSLTKSPLWA SYPLQYLSSF NWKPLEVILR PSNKVCKDGD WEDSPTCGWF
160 170 180 190 200
SQGGVRVADS QGFCCECSSS QVWDDTFGSS KERTRANLDC DFWSDPLDIL
210 220 230 240 250
IGRKPVSAHC LTFDPQWYSG YELGAASLQF EIAITVEVPT APSPTTATTS
260 270 280 290 300
ATPRTNNSSS ANSTNSTNSP APQFLSPPAP STREVLHLGP SVPLASSASR
310 320 330 340 350
LLSAKLLGDL AMYTQLPAIS NQVLMVPQPP AAAAATGSPL DATLATNRSA
360 370 380 390 400
WMLLDKTMLS MDGLACDKVG TGFSAFRYQP SGCGRAPQAC LSGQLKDLWE
410 420 430 440 450
ADLARIADGR VPLYMITRFT GGSDTTLQSF SGGPLSFALP VTSHSQSLVT
460 470 480 490 500
LSVAADGVRL VTNRSPGKIT GAAVCRFAGT SCGGFEAVAA RGYIYVNITN
510 520 530 540 550
TGRLDSDYTL TVSNCSSNVR PIEARTLAVR AGSAASLDPP MELYVEDQAA
560 570 580 590 600
AAARTCTVSL YDSVGAVTDS LTLSFYTNAT QLVVKPSGGY NGTGDGAGVK
610 620 630 640 650
RNGTDCSTAC TNPIDVLCFV TKKCWSKFGR LLGIIGGALV GLGLLAVALK
660 670 680 690 700
FGWLASLAAS CCGGGGGAAA GGAGGGMGLG TGGGGGCFGG GQQQQQLPPA
710 720 730 740 750
ASHAMSPPQQ QQRSHAEVAA GAAVAGAGAA GAAAAVLGAK HGGGGGGARG
760 770 780 790 800
KQQHADTRHL QDRDSRAIDG GASIGSSSAG GSSSLSSYSQ PREAGGRLLQ
810 820 830 840 850
PPAAAVFVPE GGGGGAAGDE GARAQSSDWD ARGRSPRVAD EHGSPRQRYD
860 870 880 890 900
GVRQSPYMVS ANPYDGWYDG GSGGGGGGGG GGYGREAPPP QGPPPHPVGA
910 920 930 940 950
PPPPPRRRSL WERMWLQRPG GGGGGGGGGG GGGGGGSGGG VDQHGGRSCA
960 970 980 990 1000
DAARRGGGGP GGMRGVEGLM SNGGRPNGPH PHAPPPPPPP QQQQQQQRQR
1010 1020 1030 1040 1050
RSFLESLTAM MTLPWGGGRE EEAGGDRRGG GRGGAAAAHG GRGAGGGRGH
1060 1070 1080 1090 1100
PPSIGSPPPG PLQPPEYGPQ GGQARRWGAG GGRGGVGGDG GGGGVGAAAY
1110 1120 1130
VQLSTGGRGG GGGGGRGRGG GREGPTWHNP VYDWQAPPK
Length:1,139
Mass (Da):115,204
Last modified:March 23, 2010 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i10686ACC371BBE93
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti697L → Q in BAE71145 (PubMed:16378100).Curated1
Sequence conflicti708P → PQ in BAE71145 (PubMed:16378100).Curated1
Sequence conflicti731G → V in BAE71145 (PubMed:16378100).Curated1
Sequence conflicti747G → A in BAE71145 (PubMed:16378100).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
EF397563 mRNA Translation: ABO29824.2
DS496135 Genomic DNA No translation available.
AB206813 mRNA Translation: BAE71145.2

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

Becoming one - Issue 193 of July 2017

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF397563 mRNA Translation: ABO29824.2
DS496135 Genomic DNA No translation available.
AB206813 mRNA Translation: BAE71145.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5MF1X-ray3.30A/B/C23-592[»]
6DBSX-ray2.60A/B/C23-582[»]
6E18X-ray2.60A23-591[»]
SMRiA4GRC6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi3055.EDP01230

Protein family/group databases

TCDBi1.N.3.1.6 the hapless2 male gamete fusion factor (fusexin) family

PTM databases

iPTMnetiA4GRC6

Phylogenomic databases

eggNOGiENOG410IX3U Eukaryota
ENOG4111J3I LUCA

Family and domain databases

InterProiView protein in InterPro
IPR040326 HAP2/GCS1
IPR018928 HAP2/GCS1_dom
PANTHERiPTHR31764 PTHR31764, 1 hit
PfamiView protein in Pfam
PF10699 HAP2-GCS1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHAP2_CHLRE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A4GRC6
Secondary accession number(s): Q2PGG4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
Last sequence update: March 23, 2010
Last modified: September 18, 2019
This is version 35 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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