ID   CLUL1_CANLF             Reviewed;         465 AA.
AC   Q95KN1; Q9N1T8;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Clusterin-like protein 1;
DE   AltName: Full=Retinal-specific clusterin-like protein;
DE   Flags: Precursor;
GN   Name=CLUL1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Retina;
RX   PubMed=10675623; DOI=10.1016/s0378-1119(99)00542-9;
RA   Zhang Q., Ray K., Acland G.M., Czarnecki J.M., Aguirre G.D.;
RT   "Molecular cloning, characterization and expression of a novel retinal
RT   clusterin-like protein cDNA.";
RL   Gene 243:151-160(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=14507903; DOI=10.1167/iovs.02-1202;
RA   Zhang Q., Beltran W.A., Mao Z., Li K., Johnson J.L., Acland G.M.,
RA   Aguirre G.D.;
RT   "Comparative analysis and expression of CLUL1, a cone photoreceptor-
RT   specific gene.";
RL   Invest. Ophthalmol. Vis. Sci. 44:4542-4549(2003).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=CLUL1b;
CC         IsoId=Q95KN1-1; Sequence=Displayed;
CC       Name=2; Synonyms=CLUL1a;
CC         IsoId=Q95KN1-2; Sequence=VSP_013743, VSP_013744;
CC   -!- TISSUE SPECIFICITY: Retina-specific (at protein level). In the light-
CC       adapted retina, expressed in the outer segment of cone photoreceptors.
CC       In the dark-adapted retina, strongly expressed in the outer plexiform
CC       layer in the region of contact between the cone pedicles and second
CC       order neurons with little or no expression in the cone photoreceptor
CC       outer segments. {ECO:0000269|PubMed:14507903}.
CC   -!- SIMILARITY: Belongs to the clusterin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF147784; AAF36799.1; -; mRNA.
DR   EMBL; AF241221; AAK49030.1; -; mRNA.
DR   RefSeq; NP_001003135.2; NM_001003135.2. [Q95KN1-1]
DR   RefSeq; XP_013970974.1; XM_014115499.1.
DR   AlphaFoldDB; Q95KN1; -.
DR   SMR; Q95KN1; -.
DR   STRING; 9612.ENSCAFP00000027095; -.
DR   PaxDb; Q95KN1; -.
DR   GeneID; 403747; -.
DR   KEGG; cfa:403747; -.
DR   CTD; 27098; -.
DR   eggNOG; ENOG502QQ44; Eukaryota.
DR   InParanoid; Q95KN1; -.
DR   OrthoDB; 567684at2759; -.
DR   Proteomes; UP000002254; 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   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..465
FT                   /note="Clusterin-like protein 1"
FT                   /id="PRO_0000005553"
FT   COILED          62..106
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        285
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"
FT   DISULFID        116..325
FT                   /evidence="ECO:0000250"
FT   DISULFID        119..322
FT                   /evidence="ECO:0000250"
FT   DISULFID        124..315
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..127
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10675623"
FT                   /id="VSP_013743"
FT   VAR_SEQ         128..140
FT                   /note="HTTCQPSWSSMKN -> MFTRAEFGTSGTS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10675623"
FT                   /id="VSP_013744"
SQ   SEQUENCE   465 AA;  54402 MW;  BBDE1AC512D5D33F CRC64;
     MKPSLLVFTV YLLWLKDCHC APTWKDKTDM HGNLKGFSEA GDIDVDEEVK KALIGMKQMK
     IMMERREEEH TNLMKTLKKC KEEKQEALKL MNEVQEHLEE EESLCQVSLT DSWDECKSCL
     ESNCMRFHTT CQPSWSSMKN TVEQFFRNIY QYLFPFDEDN EKDLPVGEKF IEEDAQVAQI
     ENVFNQLTVD VRFLFNRSLN VFKQMQQEFD QTFQSYFMSD TDLMQPNFLP ALSKEPRKKA
     DPVQSWDIPS FFQLFYNFSL SIYHSISTTI TKTLNAIEDL PKQDNDSNHG SLSSKTLPVQ
     HRGPYGEFGQ NLSECFQFHA RCQKCQDYLW EDCPDVPELH TKVDEALELV NISHQQYAQV
     LQMTQHHLED TTYLMEKMRE EFGWVADLAN QAPGAENIFD STKMVPNIHE GNFSKQDETM
     IDLSILSSPN FTLKIPLEES AETSNFISYM LEKAVQHFKK HFKTW