ID A0A3B4YKH4_SERLL Unreviewed; 424 AA.
AC A0A3B4YKH4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:ENSSLDP00000031070.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000031070.1}
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 -!- SIMILARITY: Belongs to the ZP domain family. ZPB subfamily.
CC {ECO:0000256|ARBA:ARBA00010863}.
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; A0A3B4YKH4; -.
DR STRING; 1841481.ENSSLDP00000031070; -.
DR Ensembl; ENSSLDT00000031962.1; ENSSLDP00000031070.1; ENSSLDG00000023801.1.
DR GeneTree; ENSGT00940000163253; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0035805; C:egg coat; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
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; IPR017957; P_trefoil_CS.
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 SMART; SM00018; PD; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57492; Trefoil; 1.
DR PROSITE; PS00025; P_TREFOIL_1; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 3: Inferred from homology;
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..424
FT /note="Zona pellucida sperm-binding protein 4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017269861"
FT DOMAIN 58..96
FT /note="P-type"
FT /evidence="ECO:0000259|PROSITE:PS51448"
FT DOMAIN 101..384
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT DISULFID 60..86
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
FT DISULFID 70..85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 424 AA; 46937 MW; DE9001B705CC3B31 CRC64;
MELFKCLFGV VVVVVVVSVC DVTAQHYWTM PLQKHQPPLP SQLPQQRLKV PPPSVPFDKC
QVAETEKIQC GTRDITAEQC ENINCCFDGR QCYYGKAVTV QCTRDGQFVV VVARDATMPH
IDVDSVSLLE TNNPSCTPAG VTAAFAIFQF PVTACGTTIK EEEGYVVYEN HMSSSYEVGI
GPRGSITRDS HFELLFQCRY SGTAVEALVL EVNALPPPVP VAAAGPLRVE LRLGNGQCLS
KGCVEEEVAY SSFYTREDYP VTKVLREPVH VEVRLLERSD PNIVLNLEHC WATSTPNPHS
LPQWDLLVDG CPYHDDRYTT TVVPVDGSSG LQYPSHHKRF IIKMFTFVDQ NTFTTQQDTV
FIHCATAVCY PSSTNSCAQP CHRQRRAVAA VRKASSNQRA VVSSGEVILT EERTTSAPDT
KSNR
//
