ID A0A3B4YWW1_SERLL Unreviewed; 565 AA.
AC A0A3B4YWW1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Zona pellucida sperm-binding protein 4 {ECO:0000256|ARBA:ARBA00040238};
DE AltName: Full=Zona pellucida glycoprotein 4 {ECO:0000256|ARBA:ARBA00042573};
DE AltName: Full=Zona pellucida protein B {ECO:0000256|ARBA:ARBA00042273};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000032716.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000032716.1}
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 ZP4 may act as a sperm receptor. {ECO:0000256|ARBA:ARBA00037545}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}. Zona pellucida
CC {ECO:0000256|ARBA:ARBA00024183}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00779}.
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DR AlphaFoldDB; A0A3B4YWW1; -.
DR Ensembl; ENSSLDT00000033638.1; ENSSLDP00000032716.1; ENSSLDG00000024811.1.
DR GeneTree; ENSGT00940000163253; -.
DR Proteomes; UP000261360; Unplaced.
DR CDD; cd00111; Trefoil; 1.
DR Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 1.
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; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR PANTHER; PTHR23343; ZONA PELLUCIDA SPERM-BINDING PROTEIN; 1.
DR PANTHER; PTHR23343:SF31; ZONA PELLUCIDA SPERM-BINDING PROTEIN 4; 1.
DR Pfam; PF00088; Trefoil; 1.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00018; PD; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57492; Trefoil; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 4: Predicted;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00779}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Fertilization {ECO:0000256|ARBA:ARBA00023279};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 231..269
FT /note="P-type"
FT /evidence="ECO:0000259|PROSITE:PS51448"
FT DOMAIN 274..555
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT REGION 1..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 233..259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
FT DISULFID 243..258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 565 AA; 62657 MW; 00F8971D9C7BDCD8 CRC64;
MWQNAGAKGA PPPQAPQTHQ PAPPPKDPQY QQIPQFQPSP PQRSPPYGQL PPIVPYRDQQ
YVPSPPKAVP RPQVHQVSPP SPPKAVPRPQ IHQVSPPSPP KAVPRPQVPQ VSPPSPPKAV
PRPQVPQVSP PSPQFPHYPK IQPPPPQKVP QYFDVPQIQP PPPQKVPQYS HERAQYPQAP
KFQPRGVSNY KSDPDVLLPQ KPYDPQQPKQ HTSPQDPSIY PSTGSKQPIF QSCEVAPNVR
VPCGGPDISA AACEAISCCF DGRQCYFGKA VTVQCTKDAQ FIVVVARDAT LPHIDLESVA
LLGGGQGCTH VDSNSDFAIY QFPVTACGSV IMEEPGVIIY ENRMSSSYEV GIGDRGAITR
DSYYELLFQC RYIGTSVETV VVEVLPLQDP PLPAAALGPI QVHLWLANGQ CHTKGCNELD
VAYNSFYTDA DYPVTKVLRD PVYVEVQLLD KTDPNLVLTL GRCWTTTSSN PHNANETIYH
SFLFCRNVHH KRAVGFLSAL TVLTWPESLK LTIFTQDSCH RTNVYLQFIL YSGGRPFICS
KLKKIQLCRN MKTQIRVLHL TFYFC
//