ID A0A452I535_9SAUR Unreviewed; 404 AA.
AC A0A452I535;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Zona pellucida sperm-binding protein 3 {ECO:0000256|ARBA:ARBA00017980, ECO:0000256|RuleBase:RU367066};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000022682.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000022682.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Component of the zona pellucida, an extracellular matrix
CC surrounding oocytes which mediates sperm binding, induction of the
CC acrosome reaction and prevents post-fertilization polyspermy. The zona
CC pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4.
CC ZP3 is essential for sperm binding and zona matrix formation.
CC {ECO:0000256|RuleBase:RU367066}.
CC -!- SUBCELLULAR LOCATION: Zona pellucida {ECO:0000256|RuleBase:RU367066}.
CC Cell membrane {ECO:0000256|RuleBase:RU367066}; Single-pass type I
CC membrane protein {ECO:0000256|RuleBase:RU367066}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida. {ECO:0000256|RuleBase:RU367066}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000256|RuleBase:RU367066}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
CC {ECO:0000256|ARBA:ARBA00006735, ECO:0000256|RuleBase:RU367066}.
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DR AlphaFoldDB; A0A452I535; -.
DR STRING; 38772.ENSGAGP00000022682; -.
DR Ensembl; ENSGAGT00000025838.1; ENSGAGP00000022682.1; ENSGAGG00000016630.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0035805; C:egg coat; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035804; F:structural constituent of egg coat; IEA:UniProtKB-UniRule.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:UniProtKB-UniRule.
DR GO; GO:0035803; P:egg coat formation; IEA:UniProtKB-UniRule.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR048290; ZP_chr.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR11576; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR11576:SF2; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 1.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00241; ZP; 1.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367066};
KW Cleavage on pair of basic residues {ECO:0000256|RuleBase:RU367066};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU367066};
KW Extracellular matrix {ECO:0000256|RuleBase:RU367066};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367066};
KW Signal {ECO:0000256|RuleBase:RU367066}.
FT DOMAIN 58..317
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
SQ SEQUENCE 404 AA; 44301 MW; 38B863AEDA2D16E6 CRC64;
MCVFELVTVA TGSGPCNVFI FSRVLQMWFD FVTQFMLLVI STSIPLRAVS LLQPVTVQCE
EAQLVITVHR DLFGTGQLIK AADLSLGPAA CQYTSLNAAE NTVTFTAGLH ECGSTLQMTP
DSLIYSTSLN YNPTPASNPV ILRTNPAVIP IECHYPRKDN VSSKAIKPTW VPFSSTLSAE
ERLAFSLRLM NDDWSAERPS NGFQLGEVMH IQADVSTGNH VALRLFVDSC VATLTPDRDS
YPRYAVIAFN GCLVDGRSDD TTSVFISPRS RQDTLQFMVD VFRFAGDIYI TCHLKVTAVE
QAPDPLNKAC SFNKAGNIWA PVEGTRDICR CCETRNCALL GGQSGRGSHL DRWPRRRFQR
DVASRHGEAD VVVGPLIILD AYQESTDVVE DRVEAGKAAA PGIL
//
