ZP3R_MOUSE
ID ZP3R_MOUSE Reviewed; 579 AA.
AC Q60736;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAC52208.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-50; 231-237; 303-335 AND
RP 374-381, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=ICR {ECO:0000269|PubMed:7604284};
RC TISSUE=Testis {ECO:0000269|PubMed:7604284};
RX PubMed=7604284; DOI=10.1126/science.7604284;
RA Bookbinder L.H., Cheng A., Bleil J.D.;
RT "Tissue- and species-specific expression of sp56, a mouse sperm
RT fertilization protein.";
RL Science 269:86-89(1995).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 33-44 AND 231-237, AND SUBUNIT.
RC STRAIN=ICR {ECO:0000269|PubMed:8188752};
RC TISSUE=Sperm {ECO:0000269|PubMed:8188752};
RX PubMed=8188752; DOI=10.1083/jcb.125.4.867;
RA Cheng A., Le T., Palacios M., Bookbinder L.H., Wassarman P.M., Suzuki F.,
RA Bleil J.D.;
RT "Sperm-egg recognition in the mouse: characterization of sp56, a sperm
RT protein having specific affinity for ZP3.";
RL J. Cell Biol. 125:867-878(1994).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC STRAIN=CD-1 {ECO:0000269|PubMed:11133656};
RC TISSUE=Testis {ECO:0000269|PubMed:11133656};
RX PubMed=11133656; DOI=10.1095/biolreprod64.1.36;
RA Kim K.-S., Cha M.C., Gerton G.L.;
RT "Mouse sperm protein sp56 is a component of the acrosomal matrix.";
RL Biol. Reprod. 64:36-43(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000269|PubMed:7604284, ECO:0000303|PubMed:11133656}.
CC -!- SUBUNIT: Homomultimer; disulfide-linked. {ECO:0000269|PubMed:8188752}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC lumen {ECO:0000269|PubMed:11133656}. Note=Sperm acrosomal matrix.
CC -!- TISSUE SPECIFICITY: Testis-specific. Not expressed in heart, liver,
CC abdominal muscle, lung, brain or kidney. {ECO:0000269|PubMed:7604284}.
CC -!- DEVELOPMENTAL STAGE: Detected from late meiosis and accumulates during
CC early spermiogenesis. {ECO:0000269|PubMed:11133656}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11133656}.
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DR EMBL; U17108; AAC52208.1; -; mRNA.
DR CCDS; CCDS15257.1; -.
DR PIR; A56740; A56740.
DR AlphaFoldDB; Q60736; -.
DR SMR; Q60736; -.
DR STRING; 10090.ENSMUSP00000045443; -.
DR GlyGen; Q60736; 13 sites.
DR iPTMnet; Q60736; -.
DR PhosphoSitePlus; Q60736; -.
DR PaxDb; Q60736; -.
DR PRIDE; Q60736; -.
DR ProteomicsDB; 275049; -.
DR MGI; MGI:104965; Zp3r.
DR eggNOG; ENOG502SHRK; Eukaryota.
DR InParanoid; Q60736; -.
DR PhylomeDB; Q60736; -.
DR PRO; PR:Q60736; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60736; protein.
DR GO; GO:0043160; C:acrosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0043159; C:acrosomal matrix; IDA:UniProtKB.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0002081; C:outer acrosomal membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0002199; C:zona pellucida receptor complex; IDA:MGI.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:UniProtKB.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:1903027; P:regulation of opsonization; ISO:MGI.
DR GO; GO:0009609; P:response to symbiotic bacterium; ISO:MGI.
DR GO; GO:0007338; P:single fertilization; IDA:MGI.
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..32
FT /evidence="ECO:0000269|PubMed:8188752"
FT CHAIN 33..579
FT /note="Zona pellucida sperm-binding protein 3 receptor"
FT /evidence="ECO:0000269|PubMed:8188752"
FT /id="PRO_0000006013"
FT DOMAIN 33..93
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 94..155
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 156..220
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 221..280
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 281..347
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 348..413
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT DOMAIN 454..511
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000305"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 428
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 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 34..79
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 65..91
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 96..137
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 123..153
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 158..201
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 187..218
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 223..265
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 251..278
FT /evidence="ECO:0000250|UniProtKB:P08174,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 283..333
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 317..345
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 350..398
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 383..411
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 456..497
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 483..509
FT /evidence="ECO:0000250|UniProtKB:P04003,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 579 AA; 64950 MW; C87BD1FDB2C92C53 CRC64;
MITWSFIDLW RTSHSTLFQM TLATVLMAPV LGDCGPPPLL PFASPTNQLY ESTTFPSGTV
LKYTCHHGFK RVNSSHLSCD ENGSWVYSTF CARKRCKNPG ELVNGKVEIP SDLLVGSIIE
FSCSKGYLLI GSATSRCEVQ GKGVDWSDSL PECVIATCEP PPPISNGKHS GRDDDLYTFG
SVVIYNCDPT FTLLGNASIV CTVVNRTVGV WRPHPPACQK IVCHRPQIPK GYLAPGFRQF
YAYRDALEIR CKKGFILRGS SVIHCEANGE WFPSIPTCEP NGCTNIPDIS YASWEGYKFP
LRNFEVFEIG AKLKYQCKPG YRASLNDPQT VTCQENLTWS STNGCERICC PTPDMEKIKI
VSERRDFTGT CIYAYGDYVF YICNEGSYPM STDGRSSCQA DGKWDPAIPS CQADSGLQNR
LALFTFPNIS ETNVTNKTYL FGHEENSTEH AMKGVCLKPM VINGNLSVER VIYAELENIT
IQCDPGYTIV GSPNIICSNR TWYPEVPSCQ MEVLEDCRIV SRGAQLLHCL SSPEDVHRAL
KVYKLFLEIE RLEHQKEKWI QLHRKPQSMK INRSFRLCN
