ZP3R_CAVPO
ID ZP3R_CAVPO Reviewed; 533 AA.
AC O08569;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Zona pellucida sperm-binding protein 3 receptor;
DE AltName: Full=Acrosomal matrix component 67;
DE Short=Protein AM67;
DE Short=p67;
DE Flags: Precursor;
GN Name=ZP3R;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000312|EMBL:AAC13888.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 298-309; 334-338; 361-390
RP AND 457-474, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Hartley {ECO:0000312|EMBL:AAC13888.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAC13888.1};
RX PubMed=9139729; DOI=10.1074/jbc.272.19.12714;
RA Foster J.A., Friday B.B., Maulit M.T., Blobel C., Winfrey V.P., Olson G.E.,
RA Kim K.-S., Gerton G.L.;
RT "AM67, a secretory component of the guinea pig sperm acrosomal matrix, is
RT related to mouse sperm protein sp56 and the complement component 4-binding
RT proteins.";
RL J. Biol. Chem. 272:12714-12722(1997).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 494-513.
RC TISSUE=Sperm {ECO:0000269|PubMed:7798265};
RX PubMed=7798265; DOI=10.1016/s0021-9258(18)31677-6;
RA Noland T.D., Friday B.B., Maulit M.T., Gerton G.L.;
RT "The sperm acrosomal matrix contains a novel member of the pentaxin family
RT of calcium-dependent binding proteins.";
RL J. Biol. Chem. 269:32607-32614(1994).
CC -!- FUNCTION: Probably involved in the formation of the dense core and M1
CC domain of the acrosome. May also regulate the release of certain
CC secretory proteins following the acrosomal reaction.
CC {ECO:0000303|PubMed:9139729}.
CC -!- SUBUNIT: Homooligomer; disulfide-linked. May contain 6-8 monomers per
CC oligomer. {ECO:0000269|PubMed:9139729, ECO:0000303|PubMed:9139729}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC lumen {ECO:0000269|PubMed:9139729}. Note=Sperm acrosomal matrix.
CC Restricted to the M1 domain of the apical segment of the acrosome.
CC -!- TISSUE SPECIFICITY: Testis. Not expressed in heart, brain, liver or
CC kidney. {ECO:0000269|PubMed:9139729}.
CC -!- PTM: The N-terminus may be blocked. {ECO:0000303|PubMed:7798265}.
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DR EMBL; U75654; AAC13888.1; -; mRNA.
DR RefSeq; NP_001166498.1; NM_001173027.1.
DR AlphaFoldDB; O08569; -.
DR SMR; O08569; -.
DR STRING; 10141.ENSCPOP00000005657; -.
DR Ensembl; ENSCPOT00000006339; ENSCPOP00000005657; ENSCPOG00000006274.
DR GeneID; 100135632; -.
DR KEGG; cpoc:100135632; -.
DR CTD; 22789; -.
DR eggNOG; ENOG502SHRK; Eukaryota.
DR GeneTree; ENSGT00940000154640; -.
DR HOGENOM; CLU_020107_5_2_1; -.
DR InParanoid; O08569; -.
DR OMA; CDAKGSW; -.
DR OrthoDB; 1058295at2759; -.
DR TreeFam; TF334137; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000006274; Expressed in testis and 2 other tissues.
DR GO; GO:0043160; C:acrosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0043159; C:acrosomal matrix; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0007340; P:acrosome reaction; NAS:UniProtKB.
DR GO; GO:0006996; P:organelle organization; NAS:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Fertilization; Glycoprotein; Reference proteome; Repeat; Signal; Sushi.
FT SIGNAL 1..28
FT /evidence="ECO:0000255, ECO:0000312|EMBL:AAC13888.1"
FT CHAIN 29..533
FT /note="Zona pellucida sperm-binding protein 3 receptor"
FT /id="PRO_0000006012"
FT DOMAIN 29..88
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 89..150
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 151..215
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 216..275
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 276..342
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 343..408
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 409..467
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 30..74
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 60..86
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 91..132
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 118..148
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 153..196
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 182..213
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 218..260
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 246..273
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 278..328
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 312..340
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 345..393
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 378..406
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 411..452
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 438..465
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 533 AA; 59773 MW; EDBDDED487A45389 CRC64;
MFPRLQAVSA PALLQITLMA VLLAPVLGDC GPPPILPFAS PVIQSYETNF RTGTALKYNC
HRGYWRVNSS HVICDINGSW IYNVFCAKKR CRNPGELANG KVEIITDLLF GSTIEFSCSK
GYSLIGSTTS QCESQGKTVD WSDPLPECVI VKCDSPPDIS NGKHSGTDED LYTYGSLVTY
VCDPNYSLLG NASISCLVAN KTVGVWSSNP PTCEKVICRQ PHIPKGIFLS GFGFYYTYKD
TLVISCKKGY ILRGSSIIHC EANSKWYPSI PTCEPNGCID LPEVPYISWE RNVLSLKNQE
IFEIGSLLKY DCKTGYRPTP NEPRTVTCQE NLKWAISKGC ERVCCPTPNM EKMRIINERR
DFTGVCVYAY EDYIFYMCDE GYYPISADGR SSCQADGMWN PKMPACESAV CLKPDILNGK
LSVEKDHYTE TENVTIHCDS GYEVVGPQNI ICSENRTWTP EIPKCEWEVP EECKQVAAGR
KLLECLPNPS DVKMALEVYK LSLEIEQLEK EKYVKIQEKF SKKEMKQLTS ALH
