ID   ZPLD1_MACFA             Reviewed;         415 AA.
AC   Q95JJ6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 62.
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; ORFNames=QtsA-16765;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
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}.
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DR   EMBL; AB070185; BAB63130.1; -; mRNA.
DR   RefSeq; NP_001270109.1; NM_001283180.1.
DR   AlphaFoldDB; Q95JJ6; -.
DR   SMR; Q95JJ6; -.
DR   STRING; 9541.XP_005548307.1; -.
DR   GeneID; 102118928; -.
DR   CTD; 131368; -.
DR   eggNOG; ENOG502QQQ1; Eukaryota.
DR   OrthoDB; 692009at2759; -.
DR   Proteomes; UP000233100; Unplaced.
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; Glycoprotein;
KW   Membrane; Reference proteome; Secreted; Signal; Transmembrane;
KW   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_0000307285"
FT   CHAIN           20..319
FT                   /note="Zona pellucida-like domain-containing protein 1,
FT                   secreted form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000441815"
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   REGION          323..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            319..320
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P10761"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  45488 MW;  9281DA2B3DBDE8ED CRC64;
     MEQIRLLLLL TIRVLSGSAQ FNGYNCDANL HSRFPAERDI SVYCGVQAIT MKINFCTVLF
     SGYSETDLAL NGRHGDSHCR GFINNNTFPA VVIFIINLST LEGCGNNLVV STIPGVSAYG
     NATSVQIGNI SGYIDTPDPP TIISYLPGLL YKFSCSYPLE YLVNNTQLAS SSAAISVREN
     NGTFVSTLNL LLYNDSTYNQ QLIIPSIGLP LKTKVFAAVQ ATNLDGRWNV LMDYCYTTPS
     GNPNDDIRYD LFLSCDKDPQ TTVIENGRSQ RGRFSFEVFR FVKHKNQKMS TVFLHCVTKL
     CRADDCPFLM PICSHRERRD AGRRTTWSSQ SSSGSAVLSA GPIITRSDET PTNNSQLGSP
     SVPPFQLNAI TSALISGMVI LGVMSFSLLV CPLALLHRKG PTSLVLNGIR NPVFD