ID   ZPLD1_XENLA             Reviewed;         415 AA.
AC   Q66IR0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Zona pellucida-like domain-containing protein 1;
DE            Short=ZP domain-containing protein 1;
DE   AltName: Full=Cupulin {ECO:0000250|UniProtKB:C0H9B6};
DE   Contains:
DE     RecName: Full=Zona pellucida-like domain-containing protein 1, secreted form {ECO:0000250|UniProtKB:C0H9B6};
DE   Flags: Precursor;
GN   Name=zpld1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Glycoprotein which is a component of the gelatinous
CC       extracellular matrix in the cupulae of the vestibular organ.
CC       {ECO:0000250|UniProtKB:C0H9B6}.
CC   -!- SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein
CC       1]: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:C0H9B6};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein 1,
CC       secreted form]: Secreted, extracellular space, extracellular matrix
CC       {ECO:0000250|UniProtKB:C0H9B6}.
CC   -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC       the secreted form found in the extracellular matrix of the cupula.
CC       {ECO:0000250|UniProtKB:C0H9B6}.
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; BC081237; AAH81237.1; -; mRNA.
DR   RefSeq; NP_001087796.1; NM_001094327.1.
DR   AlphaFoldDB; Q66IR0; -.
DR   SMR; Q66IR0; -.
DR   DNASU; 447620; -.
DR   GeneID; 447620; -.
DR   KEGG; xla:447620; -.
DR   CTD; 447620; -.
DR   Xenbase; XB-GENE-5829959; zpld1.S.
DR   OrthoDB; 692009at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 447620; Expressed in internal ear.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.4100; -; 1.
DR   InterPro; IPR042235; ZP-C.
DR   InterPro; IPR001507; ZP_dom.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   SMART; SM00241; ZP; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Disulfide bond; Extracellular matrix; Membrane;
KW   Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..415
FT                   /note="Zona pellucida-like domain-containing protein 1"
FT                   /id="PRO_0000307287"
FT   CHAIN           20..319
FT                   /note="Zona pellucida-like domain-containing protein 1,
FT                   secreted form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000441817"
FT   TOPO_DOM        20..372
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394..415
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..320
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   SITE            319..320
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P10761"
FT   DISULFID        44..155
FT                   /evidence="ECO:0000250|UniProtKB:P10761"
FT   DISULFID        79..104
FT                   /evidence="ECO:0000250|UniProtKB:P10761"
FT   DISULFID        235..296
FT                   /evidence="ECO:0000250|UniProtKB:P10761"
FT   DISULFID        255..313
FT                   /evidence="ECO:0000250|UniProtKB:P10761"
SQ   SEQUENCE   415 AA;  45730 MW;  3787133B98507169 CRC64;
     MEPIWLLLLL AIFTVSVSAQ FNGYNCDANQ HSRFPAERDI TVYCGVQTIT MKINFCTVLF
     SGYSESDLSL NGKHGDAHCR GFINNNTFPA VVIFTINLST LESCENSLVV STVPGVNAYG
     IASMVQIGNI SGYIDTPDPP TIISYLPGLL YKFSCSYPLE YLVNNTQLAS SSAAISVREG
     NGTFISTLNL LLYNDSTYSQ QLLIPSAGLP LKTKIYAAVR ATNLDGRWNV LMDYCYTTPS
     GNPSDDIRYD LFLSCDKDPQ TTIFENGKSQ MGRFSFEVFR FVKHKNQKMS TVFLHCITKL
     CRSDDCHYLT PTCHNRDRRD AVIRTTLTPY SLSGNAVVSA GPIITRSDET PANNSQLAHP
     GNQQFQINSV TSALISGVVI LGATSLSFFI IALTLLNRKK QNSLVLCGIR NPVFN