COL_ICTTR
ID COL_ICTTR Reviewed; 111 AA.
AC Q91XL7;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Colipase;
DE Flags: Precursor;
GN Name=CLPS;
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RA Squire T.L., Bauer V.W., Lowe M.E., Andrews M.T.;
RT "Genomic organization of the pancreatic triacylglycerol lipase gene in a
RT hibernating mammal.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows the
CC lipase to anchor itself to the lipid-water interface. Without colipase
CC the enzyme is washed off by bile salts, which have an inhibitory effect
CC on the lipase. {ECO:0000250|UniProtKB:P04118}.
CC -!- FUNCTION: Enterostatin has a biological activity as a satiety signal.
CC {ECO:0000250|UniProtKB:P04118}.
CC -!- SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase.
CC {ECO:0000250|UniProtKB:P04118}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the pancreas.
CC -!- SIMILARITY: Belongs to the colipase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00674}.
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DR EMBL; AF395869; AAK72258.1; -; mRNA.
DR RefSeq; NP_001269178.1; NM_001282249.1.
DR AlphaFoldDB; Q91XL7; -.
DR SMR; Q91XL7; -.
DR STRING; 43179.ENSSTOP00000021080; -.
DR Ensembl; ENSSTOT00000026093; ENSSTOP00000021080; ENSSTOG00000027903.
DR GeneID; 101966377; -.
DR CTD; 1208; -.
DR eggNOG; ENOG502S4NY; Eukaryota.
DR GeneTree; ENSGT00390000012644; -.
DR HOGENOM; CLU_165591_0_0_1; -.
DR InParanoid; Q91XL7; -.
DR OMA; NSIQCKS; -.
DR OrthoDB; 1504784at2759; -.
DR TreeFam; TF336178; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd00039; COLIPASE; 1.
DR InterPro; IPR001981; Colipase.
DR InterPro; IPR017914; Colipase_C.
DR InterPro; IPR017915; Colipase_CS.
DR InterPro; IPR017913; Colipase_N.
DR PANTHER; PTHR10041; PTHR10041; 1.
DR Pfam; PF01114; Colipase; 1.
DR Pfam; PF02740; Colipase_C; 1.
DR PRINTS; PR00128; COLIPASE.
DR SMART; SM00023; COLIPASE; 1.
DR PROSITE; PS00121; COLIPASE_1; 1.
DR PROSITE; PS51342; COLIPASE_2; 1.
PE 2: Evidence at transcript level;
KW Digestion; Disulfide bond; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT PROPEP 17..21
FT /note="Enterostatin, activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000005708"
FT CHAIN 22..111
FT /note="Colipase"
FT /id="PRO_0000005709"
FT DISULFID 33..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 39..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 43..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 65..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 79..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
SQ SEQUENCE 111 AA; 12056 MW; 1C01F67B22F1ADAB CRC64;
MKVLVLLLVT LAVVYAAPDP RGILINLEDG EICMNSAQCK SSCCQHFSPL GVARCTRKAS
ENSECSPKTL YGIYYKCPCE RGLTCESDRT IIGAITNTNY GICLDAGRSK E