ID A0A3Q0RV06_AMPCI Unreviewed; 440 AA.
AC A0A3Q0RV06;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-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 Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000014257.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000014257.1}
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; A0A3Q0RV06; -.
DR Ensembl; ENSACIT00000014638.1; ENSACIP00000014257.1; ENSACIG00000011044.1.
DR GeneTree; ENSGT01030000234567; -.
DR Proteomes; UP000261340; Unplaced.
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; 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 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|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|RuleBase:RU367066};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367066};
KW Signal {ECO:0000256|RuleBase:RU367066}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT CHAIN 22..440
FT /note="Zona pellucida sperm-binding protein 3"
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT /id="PRO_5025704556"
FT DOMAIN 110..376
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT REGION 37..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 48205 MW; 31BCDABD869CAE17 CRC64;
MGSMQLIVFS FVLAYVRLSD AWFHSVGAPT RLGINAQRPA VTEAEPTGRP DGEHSSQSAQ
QVAKLQSKQN QLAAEPLSWK FPEDPVDLVT KPPFKFELRQ PVVADPVAVR CGESKIFVEV
SQDLLGLGKL IKPEEITLGG CSATEIDDLS HVLVFESELH GCGSTLVLTE STFIYAFMLV
YNPKEFGRNG ITRSQSAVIG VECHYQRQHS ASSHPEPPAW TFNKDTGKAG AQHYFSLKLM
TDDWRFERTS NKYASVDVIN MEAAVLLQTQ PPLRVLVDSC VATTEPNSAS EPREALIKNN
GCLGGQHTIS RFMPQSQPDK LQLLVAVYIS CLLKAISAST PVTIENKACS FYEGIWRAVD
GKDQFCTCCE STCGMRKIRD LHANISVGGS QWCQILHPPG TACILLPHEA EHCGATGGTP
DQRSKLLINR DSSVALMLED
//
