CLUL1_BOVIN
ID CLUL1_BOVIN Reviewed; 465 AA.
AC Q3ZRW9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Clusterin-like protein 1;
DE Flags: Precursor;
GN Name=CLUL1 {ECO:0000312|EMBL:AAT81475.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAT81475.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retinal cone cell {ECO:0000312|EMBL:AAT81475.1};
RA Zhang Q., Tomita H., Anderson R.E.;
RT "Further evidence showing CLUL1 as a conserved cone photoreceptor-specific
RT gene.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the clusterin family. {ECO:0000255}.
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DR EMBL; AY643094; AAT81475.1; -; mRNA.
DR RefSeq; NP_001029692.1; NM_001034520.1.
DR AlphaFoldDB; Q3ZRW9; -.
DR SMR; Q3ZRW9; -.
DR STRING; 9913.ENSBTAP00000018616; -.
DR PaxDb; Q3ZRW9; -.
DR PRIDE; Q3ZRW9; -.
DR GeneID; 516801; -.
DR KEGG; bta:516801; -.
DR CTD; 27098; -.
DR eggNOG; ENOG502QQ44; Eukaryota.
DR InParanoid; Q3ZRW9; -.
DR OrthoDB; 567684at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR InterPro; IPR000753; Clusterin-like.
DR InterPro; IPR016015; Clusterin_C.
DR InterPro; IPR016014; Clusterin_N.
DR PANTHER; PTHR10970; PTHR10970; 1.
DR Pfam; PF01093; Clusterin; 1.
DR SMART; SM00035; CLa; 1.
DR SMART; SM00030; CLb; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..465
FT /note="Clusterin-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000270977"
FT REGION 280..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 62..107
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..333
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT DISULFID 116..325
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT DISULFID 119..322
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT DISULFID 124..315
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT DISULFID 131..305
FT /evidence="ECO:0000250|UniProtKB:P10909"
SQ SEQUENCE 465 AA; 53950 MW; 9048047F34C086F3 CRC64;
MKPPILVFIV YLLQLRDCQC APTGKDRTSI REDPKGFSKA GEIDVDEEVK KALIGMKQMK
ILMERREEEH SKLMRTLKKC REEKQEALKL MNEVQEHLEE EERLCQVSLM DSWDECKSCL
ESDCMRFYTT CQSSWSSMKS TIERVFRKIY QFLFPFHEDD EKELPVGEKF TEEDVQLMQI
ENVFSQLTVD VGFLYNMSFH VFKQMQQEFD LAFQSYFMSD TDSMEPYFFP AFSKEPAKKA
HPMQSWDIPS FFQLFCNFSL SVYQSVSATV TEMLKATEDL SKQDKDSAHG GPSSTTWPVR
GRGLCGEPGQ NSSECLQFHA RCQKCQDYLW ADCPAVPELY TKADEALELV NISNQQYAQV
LQMTQHHLED TTYLMEKMRE QFGWVTELAS QTPGSENIFS FIKVVPGVHE GNFSKQDEKM
IDISILPSSN FTLTIPLEES AESSDFISYM LAKAVQHFKE HFKSW