ZPLD1_SALSA
ID ZPLD1_SALSA Reviewed; 413 AA.
AC C0H9B6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Zona pellucida-like domain-containing protein 1 {ECO:0000250|UniProtKB:Q8TCW7};
DE Short=ZP domain-containing protein 1 {ECO:0000250|UniProtKB:Q8TCW7};
DE AltName: Full=Cupulin {ECO:0000303|PubMed:25369234};
DE Contains:
DE RecName: Full=Zona pellucida-like domain-containing protein 1, secreted form {ECO:0000305};
DE Flags: Precursor;
GN Name=zpld1 {ECO:0000250|UniProtKB:Q8TCW7};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000312|EMBL:ACN10635.1};
RN [1] {ECO:0000312|EMBL:ACN10635.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:ACN10635.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 20-32; 34-52; 74-80; 228-248; 274-280 AND 289-299,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION,
RP PYROGLUTAMATE FORMATION AT GLN-20, PROTEOLYTIC CLEAVAGE, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=25369234; DOI=10.1371/journal.pone.0111917;
RA Dernedde J., Weise C., Mueller E.C., Hagiwara A., Bachmann S., Suzuki M.,
RA Reutter W., Tauber R., Scherer H.;
RT "Cupulin is a zona pellucida-like domain protein and major component of the
RT cupula from the inner ear.";
RL PLoS ONE 9:E111917-E111917(2014).
CC -!- FUNCTION: Glycoprotein which is a component of the gelatinous
CC extracellular matrix in the cupulae of the vestibular organ.
CC {ECO:0000269|PubMed:25369234}.
CC -!- SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein
CC 1]: Cytoplasmic vesicle membrane {ECO:0000305|PubMed:25369234}; Single-
CC 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:0000305|PubMed:25369234}.
CC -!- TISSUE SPECIFICITY: Detected in the acellular cupulae of the vestibular
CC organ, and also in support cells adjacent to the cupula (at protein
CC level). {ECO:0000269|PubMed:25369234}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted form found in the extracellular matrix of the cupula.
CC {ECO:0000305|PubMed:25369234}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:25369234}.
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DR EMBL; BT058922; ACN10635.1; -; mRNA.
DR RefSeq; NP_001158864.1; NM_001165392.1.
DR AlphaFoldDB; C0H9B6; -.
DR SMR; C0H9B6; -.
DR STRING; 8030.ENSSSAP00000033267; -.
DR GeneID; 100306853; -.
DR KEGG; sasa:100306853; -.
DR CTD; 560177; -.
DR Proteomes; UP000087266; Chromosome ssa04.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Membrane; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:25369234"
FT CHAIN 20..413
FT /note="Zona pellucida-like domain-containing protein 1"
FT /id="PRO_5009732475"
FT CHAIN 20..319
FT /note="Zona pellucida-like domain-containing protein 1,
FT secreted form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441818"
FT TOPO_DOM 20..370
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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 MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:25369234"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
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"
FT CONFLICT 22
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 45203 MW; 18C7EE6BE3C28E5F CRC64;
MEQICLIILL ISKALSVGAQ FNGYNCDANF HSRFPAERDI SVYCGVQTIT LKINFCPVLF
SGYTDTDLAL NGRHGDAHCR GFINNNTFPT VVLFSISLAT LETCGNALVV STAQGPNAYG
NLSLVQIGNI SGYIDTPDPP TIISYLPGLL YKFSCSYPLE YLVNNTQLAS SAAAISVKDS
NGTFVSTLSL LLYNDSSYVQ QLSIPMAGLT LKTRVFAAVK ATNLDRRWNV LMDYCYTTAS
GNPNDELRYD LFFSCDKDPQ TTVFENGKSQ MGRFAFEVFR FVKHKNQKMS TVFLHCVTKL
CRADDCPMLM PICGSRKKRD VSERTESNSA SGNAIITAGP IITRSDDTPM NNSQLAQLNS
PVFRMNTVTS ALISGIIILG VMSLCFFILS LTLLKGKRAP PTILSGARNP AFN
