GenomeNet

Database: UniProt
Entry: A0A3B4YWW1_SERLL
LinkDB: A0A3B4YWW1_SERLL
Original site: A0A3B4YWW1_SERLL 
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
//
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