ZP3R_RAT
ID ZP3R_RAT Reviewed; 577 AA.
AC Q7TSY4; Q7TSY3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Zona pellucida sperm-binding protein 3 receptor;
DE AltName: Full=Sperm fertilization protein 56;
DE Short=sp56;
DE Flags: Precursor;
GN Name=Zp3r; Synonyms=Sp56;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAP37007.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar {ECO:0000312|EMBL:AAP37007.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAP37007.1};
RX PubMed=12737520; DOI=10.1038/sj.cr.7290156;
RA He X.B., Yan Y.C., Li Y.P., Koide S.S.;
RT "Cloning of rat sp56, the homologue of mouse sperm ZP3 receptor-sp56.";
RL Cell Res. 13:121-129(2003).
CC -!- FUNCTION: Binds to ZP3 glycoprotein in egg zona pellucida. Probably
CC involved in interactions between sperm acrosome and egg zona pellucida
CC during and immediately following the acrosome reaction (By similarity).
CC {ECO:0000250|UniProtKB:Q60736}.
CC -!- SUBUNIT: Homomultimer; disulfide-linked.
CC {ECO:0000250|UniProtKB:Q60736}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC lumen {ECO:0000269|PubMed:12737520}. Note=Sperm acrosomal matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12737520}; Synonyms=L
CC {ECO:0000303|PubMed:12737520};
CC IsoId=Q7TSY4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12737520}; Synonyms=S
CC {ECO:0000303|PubMed:12737520};
CC IsoId=Q7TSY4-2; Sequence=VSP_050758;
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12737520}.
CC -!- DEVELOPMENTAL STAGE: Detected from early pachytene spermatocytes and
CC throughout spermatogenesis. {ECO:0000269|PubMed:12737520}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q60736}.
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DR EMBL; AY278363; AAP37007.1; -; mRNA.
DR EMBL; AY278364; AAP37008.1; -; mRNA.
DR AlphaFoldDB; Q7TSY4; -.
DR SMR; Q7TSY4; -.
DR STRING; 10116.ENSRNOP00000031964; -.
DR GlyGen; Q7TSY4; 13 sites.
DR PaxDb; Q7TSY4; -.
DR UCSC; RGD:727846; rat. [Q7TSY4-1]
DR RGD; 727846; Zp3r.
DR eggNOG; ENOG502SHRK; Eukaryota.
DR InParanoid; Q7TSY4; -.
DR PhylomeDB; Q7TSY4; -.
DR PRO; PR:Q7TSY4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043160; C:acrosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0043159; C:acrosomal matrix; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:RGD.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
DR CDD; cd00033; CCP; 7.
DR InterPro; IPR040514; C4bp_oligo.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF18453; C4bp_oligo; 1.
DR Pfam; PF00084; Sushi; 7.
DR SMART; SM00032; CCP; 7.
DR SUPFAM; SSF57535; SSF57535; 7.
DR PROSITE; PS50923; SUSHI; 7.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasmic vesicle; Disulfide bond; Fertilization;
KW Glycoprotein; Reference proteome; Repeat; Signal; Sushi.
FT SIGNAL 1..32
FT /evidence="ECO:0000250|UniProtKB:Q60736"
FT CHAIN 33..577
FT /note="Zona pellucida sperm-binding protein 3 receptor"
FT /evidence="ECO:0000250|UniProtKB:Q60736"
FT /id="PRO_0000006014"
FT DOMAIN 33..92
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 93..154
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 155..219
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 220..279
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 280..346
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 347..412
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 451..509
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 34..78
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 64..90
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 95..136
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 122..152
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 157..200
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 186..217
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 222..264
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 250..277
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 282..332
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 316..344
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 349..397
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 382..410
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 453..494
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 480..507
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 154..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12737520"
FT /id="VSP_050758"
SQ SEQUENCE 577 AA; 64373 MW; 89FD20ADF3A1FD3D CRC64;
MTAWSLHELW KTSHSTLFQV TLATVLMAPV LGDCGPPPSL PFASPISQLD EVSFPPGAVL
KYTCHHGFKR TNSSHITCDE NGSWVYTTFC ARKRCKNPGE LVNGKIEILS DLLVGLNIEF
SCSEGYLLIG SATSRCEVQG KGVNWSDSLP ECVIATCEPP PVINNGKHSG REEDLYTYGS
MVIYSCDPSY TLFGNASIVC TVVNKTVGVW SPHPPACEKI VCHQPQIPKG ELVPGFRHFH
TYKDALEIRC KKGFALRGNS VIHCEANGEW FPSVPTCEPN GCIDIPDISY ASWDGNRFPL
ENTAVFEIGT KLKYRCKPGY RANVHDVQIV TCQENLTWSS PSGCERVCCP TPNMEKIKIV
SERRDFTGTC VYAYGDYVFY ICSEGTYPMT TDGRSSCQAD GKWDPAIPSC EADPSLQNHF
ALTFPNISET NVTNRTYLLE NENATESFIK AVCPKPEIIN GNLSVEKEIY AEMENITIQC
DSGYDLVGSS NIICLENRTW YPDIPFCIME GPEDCEIVNK GRQLLQCLSS PEDVQRALEV
YKLSLEIERL EQQREKRTSV HRKAHYTKVD GPFRPFS
