CLUL1_RAT
ID CLUL1_RAT Reviewed; 464 AA.
AC Q3ZRW7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Clusterin-like protein 1;
DE Flags: Precursor;
GN Name=Clul1 {ECO:0000312|EMBL:AAT81476.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAT81476.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAT81476.1};
RC TISSUE=Retina {ECO:0000312|EMBL:AAT81476.1};
RA Zhang Q., Anderson R.E.;
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; AY655707; AAT81476.1; -; mRNA.
DR RefSeq; NP_001028243.1; NM_001033071.1.
DR AlphaFoldDB; Q3ZRW7; -.
DR SMR; Q3ZRW7; -.
DR GlyGen; Q3ZRW7; 6 sites.
DR PhosphoSitePlus; Q3ZRW7; -.
DR GeneID; 367345; -.
DR KEGG; rno:367345; -.
DR UCSC; RGD:1306852; rat.
DR CTD; 27098; -.
DR RGD; 1306852; Clul1.
DR InParanoid; Q3ZRW7; -.
DR OrthoDB; 567684at2759; -.
DR PhylomeDB; Q3ZRW7; -.
DR PRO; PR:Q3ZRW7; -.
DR Proteomes; UP000002494; 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..464
FT /note="Clusterin-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000270979"
FT COILED 56..109
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..331
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT DISULFID 116..323
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT DISULFID 119..320
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT DISULFID 124..313
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT DISULFID 131..303
FT /evidence="ECO:0000250|UniProtKB:P10909"
SQ SEQUENCE 464 AA; 53706 MW; 0276A46E5FF7616D CRC64;
MQPPLFVISV YLLWLKYCDS APTWKETDAT DGNLKSLPEV GEADVEGEVK KALIGIKQMK
IMMERREEEH AKLMKALKKC KEEKQEAQKL MNEVQERLEE EEKLCQASSI GSWDGCRPCL
ESNCIRFYTA CQPGWSSVKS MMKQFLKKIY RFLSSQSEDV KDPPAIEQLT KEDLQVVHIE
NLFSQLAVDA KSLFNMSFYI FKQMQQEFDQ AFQLYFMSDV DLMEPYPPAL SKEITKKEEL
GQRWGIPNVF QLFHNFSLSV YGRVQQIIMK TLNAIEDSWE PHKELDQRGM TSEMLPEQNG
EMCEEFVKNL SGCLKFRKRC QKCHNYLSEE CPDVPELHIE FLEALKLVNV SNQQYDQIVQ
MTQYHLEDTI YLMEKMQEQF GWVSQLASHN PVTEDIFNST KAVPKIHGGD SSKQDEIMVD
SSSILPSSNF TVQNPPEEGA ESSNVIYYMA AKVLQHLKGC FETW