HAP2_NEMVE
ID HAP2_NEMVE Reviewed; 853 AA.
AC A7SIM4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Hapless 2;
DE AltName: Full=Generative cell specific 1 {ECO:0000303|PubMed:25111819};
DE Flags: Precursor;
GN Name=HAP2; Synonyms=GCS1 {ECO:0000303|PubMed:25111819};
GN ORFNames=v1g212848 {ECO:0000312|EMBL:EDO36432.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000312|Proteomes:UP000001593};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25111819; DOI=10.1016/j.bbrc.2014.08.006;
RA Ebchuqin E., Yokota N., Yamada L., Yasuoka Y., Akasaka M., Arakawa M.,
RA Deguchi R., Mori T., Sawada H.;
RT "Evidence for participation of GCS1 in fertilization of the starlet sea
RT anemone Nematostella vectensis: implication of a common mechanism of sperm-
RT egg fusion in plants and animals.";
RL Biochem. Biophys. Res. Commun. 451:522-528(2014).
RN [2] {ECO:0000312|EMBL:EDO36432.1, ECO:0000312|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000312|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
RN [3]
RP REVIEW.
RX PubMed=20080406; DOI=10.1016/j.tcb.2009.12.007;
RA Wong J.L., Johnson M.A.;
RT "Is HAP2-GCS1 an ancestral gamete fusogen?";
RL Trends Cell Biol. 20:134-141(2010).
CC -!- FUNCTION: During fertilization, required on male gametes for their
CC fusion with female gametes (PubMed:25111819). Probably initiates the
CC fusion of gamete cell membranes by inserting part of its extracellular
CC domain into the cell membrane of a female gamete (PubMed:20080406).
CC {ECO:0000269|PubMed:25111819, ECO:0000303|PubMed:20080406}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25111819};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in sperm (at protein level). Detected in
CC testis seminal ducts. {ECO:0000269|PubMed:25111819}.
CC -!- MISCELLANEOUS: HAP2/GCS1 family members mediate membrane fusion between
CC gametes in a broad range of eukaryotes, ranging from algae and higher
CC plants to protozoans and cnidaria, suggesting they are derived from an
CC ancestral gamete fusogen. They function similar to viral fusogens, by
CC inserting part of their extracellular domain into the lipid bilayer of
CC an adjoining cell. {ECO:0000303|PubMed:20080406}.
CC -!- SIMILARITY: Belongs to the HAP2/GCS1 family. {ECO:0000305}.
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DR EMBL; DS469670; EDO36432.1; -; Genomic_DNA.
DR RefSeq; XP_001628495.1; XM_001628445.1.
DR AlphaFoldDB; A7SIM4; -.
DR SMR; A7SIM4; -.
DR EnsemblMetazoa; EDO36432; EDO36432; NEMVEDRAFT_v1g212848.
DR GeneID; 5507857; -.
DR KEGG; nve:5507857; -.
DR eggNOG; ENOG502QREH; Eukaryota.
DR HOGENOM; CLU_334718_0_0_1; -.
DR InParanoid; A7SIM4; -.
DR OMA; LERDHND; -.
DR OrthoDB; 575147at2759; -.
DR PhylomeDB; A7SIM4; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR InterPro; IPR040326; HAP2/GCS1.
DR InterPro; IPR018928; HAP2/GCS1_dom.
DR PANTHER; PTHR31764; PTHR31764; 1.
DR Pfam; PF10699; HAP2-GCS1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Fertilization; Glycoprotein; Lipid-binding;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..853
FT /note="Hapless 2"
FT /id="PRO_5002714433"
FT TOPO_DOM 23..603
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..853
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 33..51
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 151..206
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 170..352
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 172..195
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 334..359
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 475..513
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
SQ SEQUENCE 853 AA; 96468 MW; 5BF4C9A0228F917E CRC64;
MGRGQIIMIL VGLLCLANES YSDVIAKSSL QMCENTGNSD DPYNVVDQKA CEKKLIVTLS
VRSGQNGTEF LKAVTNVSKV YDQTEKEMAR LYNPFIITLA KTPVKLTYPY YYLAMVNNKP
TERVVISDSK WHASGSYHAC SDAWDDEDAL CGFYTDAEGK PIWDSQGFCC RCTEQEKWRG
SFNDKNPYSR AGINCKLFGT QAAAHCMTFD DLWYTVNEVG LWQMDFSIHV KAYDLVVEKV
GNKTQSKWVD GGEIVIGPTI RSGVGVHGRL HATFIGEFQS HKQFPVLTTK YLLIPYVSEK
VDPKTHPQFR NGPHDYMLID KHEVNYKSSG PHECDKIGVS FSAFRAQAPM GCSQKQGDCL
HNQPKDYFEE DTKRRASGKT PYYFPQKFGK LLGVNQRKDN NHFVLTYEVD EVMTSMVTLQ
ISADDVILIY NRAEGKILRA YAQDFEALSR DGNLYVIVQN IGLVTADFYV VIKECSVGIG
KLLEKAASIN PQQTHSFTFS VKAQQWKGGD NFCIVQLYDA RRKMVDSSNV TFRTTEPCVC
ASSCGCSCFK NGFKCTKRED RDFTKTKPKD SGLDLGFFPK LWNKIKNVWD TVTSVFNFME
SGWALLGTAL GLLSLGGLKA FLGFRKTGSR IARFGFGGAN KGRVRRRDGS GRMVTMEFNE
TGDRIDPETK EVIEPRNKKK ELLLNLFFFF ILPFLLIYHL VGWIRWRMRK PGSEDEEQAG
TGDEQGGASP LHNIEARAAV DQFLQPDTIV YHSYSQDDYV AQFLINPGKR FCMAGRMTSL
SGPSADQFRF DLLQAIQIYE VIDNKRRRLE SVNSLNAHYF SRLLNAEAMI DCLSLKPAFP
CLNVNRKRKP KQK
