ID A0A3Q1HG72_9TELE Unreviewed; 404 AA.
AC A0A3Q1HG72;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Zona pellucida sperm-binding protein 3 {ECO:0000256|RuleBase:RU367066};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000027545.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000027545.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|RuleBase:RU367066}.
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DR AlphaFoldDB; A0A3Q1HG72; -.
DR Ensembl; ENSAPOT00000000964.1; ENSAPOP00000027545.1; ENSAPOG00000012355.1.
DR GeneTree; ENSGT01030000234567; -.
DR Proteomes; UP000257200; Unplaced.
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 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; 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|RuleBase:RU367066};
KW Extracellular matrix {ECO:0000256|RuleBase:RU367066};
KW Membrane {ECO:0000256|RuleBase:RU367066};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Secreted {ECO:0000256|RuleBase:RU367066};
KW Signal {ECO:0000256|RuleBase:RU367066}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT CHAIN 17..404
FT /note="Zona pellucida sperm-binding protein 3"
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT /id="PRO_5041488998"
FT DOMAIN 72..322
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
SQ SEQUENCE 404 AA; 45117 MW; 6A818A20851414BE CRC64;
MSLLSVCFVF VLYVLSVLVT VKCYTDQTSP VFLSSPDLAA LDATSHANKP RFEDPVGITA
AGEDGVKTFV LKCHEENMEV VMKAQLFDPG LSAEPMRLRL GPVGAAGDHC VAKVTGNGEY
IIRAPLAECG NKVMVDSAVL YSNLLLYYPP SSPVVVLTCR RYTVSSRELR PTWSPFTLFQ
SAHLDLDFHL RLMTDDWSSE RTSSVYFLGE TVNMEASVDH HHHLPLRLYV SSCVATLTSD
VNSSPRYPFI DHQGCFTDSQ LSGSKSRFLS RVHNNHLQIQ LEPFLFHRDR RHSIYITCYL
EAEPISKSDP VKKACSFINN RWRSVDGDDH VCESCAEKAS SISSAGSSHK RVHRSRREGN
GESCTIFRAK SIKQAECKSK HQQKINSAAQ KQNHLDILTF SLDP
//
