GenomeNet

Database: UniProt
Entry: A0A096LXN8_POEFO
LinkDB: A0A096LXN8_POEFO
Original site: A0A096LXN8_POEFO 
ID   A0A096LXN8_POEFO        Unreviewed;       415 AA.
AC   A0A096LXN8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Zona pellucida sperm-binding protein 3 {ECO:0000256|RuleBase:RU367066};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000023929.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000023929.1}
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|RuleBase:RU367066}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU367066}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AYCK01005613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A096LXN8; -.
DR   STRING; 48698.ENSPFOP00000023929; -.
DR   Ensembl; ENSPFOT00000027126.1; ENSPFOP00000023929.1; ENSPFOG00000024115.1.
DR   eggNOG; ENOG502SJK6; Eukaryota.
DR   GeneTree; ENSGT01030000234567; -.
DR   OMA; TEVSMIV; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
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; IPR048290; ZP_chr.
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   PRINTS; PR00023; ZPELLUCIDA.
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:UP000028760};
KW   Secreted {ECO:0000256|RuleBase:RU367066};
KW   Signal {ECO:0000256|RuleBase:RU367066};
KW   Transmembrane {ECO:0000256|RuleBase:RU367066};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU367066}.
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367066"
FT   TRANSMEM        35..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367066"
FT   TRANSMEM        395..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367066"
FT   DOMAIN          96..359
FT                   /note="ZP"
FT                   /evidence="ECO:0000259|PROSITE:PS51034"
SQ   SEQUENCE   415 AA;  46452 MW;  105470434EED5A22 CRC64;
     MEMPLRRRVI CIFLLTVWVQ LNVLLGVLLQ ATTTMGFAVL SVVLLLIISL VFRVSDAIRP
     LKEGPMIDAQ GREYKTVSLE DSSRPTHESK TTVRVECTEV SMIIFIQADF YNNGRLVSPQ
     ELFLGDAKYW KNKQCQALDA GDGEYVIEAD LQDCGSKLMV IGNNLIYSNN LILSPVVGSL
     GITRATGAVV PVSCHYKRVH TVSSTVQQHP PSVSISSEFA MGSSPFSLRL KTDDWSAEKY
     SNTVYLGDPL HLEVSYSGLD QRKLFIDLCV ATLTADSTSV PRYCFIENHG CFVDARDGGL
     NSVFKPRSTT SSLQFQFDAF LFQDDLRNTI FVTCEVKATR QLWKSSPTNK VCNYINSSWK
     NVDGLDGVCQ CCKGVCSKLT SKGKLYLELV YQHQLMIQYF IALHIFVFQM IFVIL
//
DBGET integrated database retrieval system