ID   CLUL1_MOUSE             Reviewed;         464 AA.
AC   Q3ZRW6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Clusterin-like protein 1;
DE   Flags: Precursor;
GN   Name=Clul1 {ECO:0000312|EMBL:AAT81477.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000312|EMBL:AAT81477.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ {ECO:0000312|EMBL:AAT81477.1};
RC   TISSUE=Retina {ECO:0000312|EMBL:AAT81477.1};
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; AY655708; AAT81477.1; -; mRNA.
DR   AlphaFoldDB; Q3ZRW6; -.
DR   SMR; Q3ZRW6; -.
DR   GlyGen; Q3ZRW6; 6 sites.
DR   iPTMnet; Q3ZRW6; -.
DR   PhosphoSitePlus; Q3ZRW6; -.
DR   PeptideAtlas; Q3ZRW6; -.
DR   PRIDE; Q3ZRW6; -.
DR   InParanoid; Q3ZRW6; -.
DR   PRO; PR:Q3ZRW6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q3ZRW6; protein.
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_0000270978"
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;  53733 MW;  8D8CB4E5A47F9BB8 CRC64;
     MQPPLLVLSV YLLWLKYCDS APTWKETDAT DGNLKSLPEV GEADVEGEVK KALIGIKQMK
     IMMERREEEH AKLMKALKKC KEEKQEAQKL MNEVQERLEE EEKLCQASSI GSWDGCRPCL
     ESNCIRFYTA CQPGWSSVKS MMKQFLKKIY RFLSSQSEDV KDPPAIEQLT KEDLQVVHIE
     NLFSQLAVDA KSLFNMSFYI FKQMQHEFDQ AFQLYFMSDV DLMEPYPPAL SKEITKKEEL
     GQRWGIPNVF QLFHNFSLSV YGRVQQIIMK TLNAIEDSWE PHKELDQRGM TSEMLPEQNG
     EMCEEFVKNL SGCLKFRKRC QKCHNYLSEE CPDVPELHIE FLEALKLVNV SNQQYDQIVQ
     MTQYHLEDTI YLMEKMQEQF GWVSQLASHN PVTEDIFNST KAVPKIHGGD SSKQDEIMVD
     SSSILPSSNF TVQNPPEEGA ESSSTIYYIV AKVLQHFKGH FKTW