LIPR1_CANLF
ID LIPR1_CANLF Reviewed; 467 AA.
AC P06857; Q28287;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Inactive pancreatic lipase-related protein 1;
DE Short=PL-RP1;
DE Flags: Precursor;
GN Name=PNLIPRP1; Synonyms=PLRP1;
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].
RX PubMed=3562437; DOI=10.1097/00006676-198609000-00007;
RA Kerfelec B., Laforge K.S., Puigserver A., Scheele G.A.;
RT "Primary structures of canine pancreatic lipase and phospholipase A2
RT messenger RNAs.";
RL Pancreas 1:430-437(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2502543; DOI=10.1016/s0021-9258(18)51572-6;
RA Mickel F.S., Weidenbach F., Swarovsky B., Laforge K.S., Scheele G.A.;
RT "Structure of the canine pancreatic lipase gene.";
RL J. Biol. Chem. 264:12895-12901(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
RP GLYCOSYLATION AT ASN-157, PROTEIN SEQUENCE OF 18-33, ABSENCE OF LIPASE
RP ACTIVITY, DISULFIDE BONDS, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, MUTAGENESIS OF VAL-196 AND ALA-198, AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=9726421;
RX DOI=10.1002/(sici)1097-0134(19980901)32:4<523::aid-prot10>3.0.co;2-e;
RA Roussel A., de Caro J., Bezzine S., Gastinel L., de Caro A., Carriere F.,
RA Leydier S., Verger R., Cambillau C.;
RT "Reactivation of the totally inactive pancreatic lipase RP1 by structure-
RT predicted point mutations.";
RL Proteins 32:523-531(1998).
CC -!- FUNCTION: May function as inhibitor of dietary triglyceride digestion.
CC Lacks detectable lipase activity towards triglycerides, diglycerides,
CC phosphatidylcholine, galactolipids or cholesterol esters (in vitro).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9726421}.
CC -!- TISSUE SPECIFICITY: Detected in pancreas (at protein level).
CC {ECO:0000269|PubMed:9726421}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:3562437 and PubMed:2502543) thought to
CC be the pancreatic lipase, but has been shown to lack lipase activity.
CC {ECO:0000305|PubMed:9726421}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30840.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M35302; AAA30885.1; -; mRNA.
DR EMBL; M28151; AAA30840.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M28141; AAA30840.1; JOINED; Genomic_DNA.
DR EMBL; M28142; AAA30840.1; JOINED; Genomic_DNA.
DR EMBL; M28143; AAA30840.1; JOINED; Genomic_DNA.
DR EMBL; M28145; AAA30840.1; JOINED; Genomic_DNA.
DR EMBL; M28148; AAA30840.1; JOINED; Genomic_DNA.
DR EMBL; M28147; AAA30840.1; JOINED; Genomic_DNA.
DR EMBL; M28146; AAA30840.1; JOINED; Genomic_DNA.
DR EMBL; M28144; AAA30840.1; JOINED; Genomic_DNA.
DR EMBL; M28149; AAA30840.1; JOINED; Genomic_DNA.
DR EMBL; M28150; AAA30840.1; JOINED; Genomic_DNA.
DR PIR; B24392; LIDG.
DR RefSeq; NP_001003319.2; NM_001003319.2.
DR PDB; 1RP1; X-ray; 2.10 A; A=18-467.
DR PDBsum; 1RP1; -.
DR AlphaFoldDB; P06857; -.
DR SMR; P06857; -.
DR STRING; 9612.ENSCAFP00000017453; -.
DR ESTHER; canfa-1plip; Pancreatic_lipase.
DR iPTMnet; P06857; -.
DR PaxDb; P06857; -.
DR Ensembl; ENSCAFT00000018834; ENSCAFP00000017453; ENSCAFG00000011815.
DR Ensembl; ENSCAFT00030046588; ENSCAFP00030040719; ENSCAFG00030025195.
DR Ensembl; ENSCAFT00040046440; ENSCAFP00040040526; ENSCAFG00040024900.
DR Ensembl; ENSCAFT00845055120; ENSCAFP00845043344; ENSCAFG00845030995.
DR GeneID; 404010; -.
DR KEGG; cfa:404010; -.
DR CTD; 5407; -.
DR VEuPathDB; HostDB:ENSCAFG00845030995; -.
DR VGNC; VGNC:44745; PNLIP.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR GeneTree; ENSGT00940000162375; -.
DR HOGENOM; CLU_027171_0_2_1; -.
DR InParanoid; P06857; -.
DR OMA; NMFKVEE; -.
DR OrthoDB; 534956at2759; -.
DR TreeFam; TF324997; -.
DR BRENDA; 3.1.1.26; 1153.
DR EvolutionaryTrace; P06857; -.
DR Proteomes; UP000002254; Chromosome 28.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR002331; Lipase_panc.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00823; PANCLIPASE.
DR PRINTS; PR00821; TAGLIPASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lipid degradation; Lipid metabolism; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:9726421"
FT CHAIN 18..467
FT /note="Inactive pancreatic lipase-related protein 1"
FT /id="PRO_0000017789"
FT DOMAIN 356..467
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT ACT_SITE 171
FT /note="Nucleophile"
FT ACT_SITE 194
FT /note="Charge relay system"
FT ACT_SITE 281
FT /note="Charge relay system"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9726421"
FT DISULFID 21..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9726421"
FT DISULFID 109..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9726421"
FT DISULFID 255..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9726421"
FT DISULFID 303..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9726421"
FT DISULFID 317..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9726421"
FT DISULFID 451..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9726421"
FT MUTAGEN 196
FT /note="V->A: Removes steric hindrance and restores lipase
FT activity; when associated with P-198."
FT /evidence="ECO:0000269|PubMed:9726421"
FT MUTAGEN 198
FT /note="A->P: Removes steric hindrance and restores lipase
FT activity; when associated with A-196."
FT /evidence="ECO:0000269|PubMed:9726421"
FT CONFLICT 92
FT /note="I -> T (in Ref. 1; AAA30885)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="D -> N (in Ref. 1; AAA30885)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="D -> N (in Ref. 1; AAA30885)"
FT /evidence="ECO:0000305"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1RP1"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1RP1"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:1RP1"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 133..158
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:1RP1"
FT TURN 198..202
FT /evidence="ECO:0007829|PDB:1RP1"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:1RP1"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:1RP1"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 306..310
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1RP1"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 356..367
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 369..379
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 387..394
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 399..408
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 411..422
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 432..441
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:1RP1"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:1RP1"
SQ SEQUENCE 467 AA; 51482 MW; 5B186845404E5B5C CRC64;
MVSIWTIALF LLGAAKAKEV CYEQIGCFSD AEPWAGTAIR PLKVLPWSPE RIGTRFLLYT
NKNPNNFQTL LPSDPSTIEA SNFQTDKKTR FIIHGFIDKG EENWLLDMCK NMFKVEEVNC
ICVDWKKGSQ TSYTQAANNV RVVGAQVAQM LSMLSANYSY SPSQVQLIGH SLGAHVAGEA
GSRTPGLGRI TGLDPVEASF QGTPEEVRLD PTDADFVDVI HTDAAPLIPF LGFGTSQQMG
HLDFFPNGGE EMPGCKKNAL SQIVDLDGIW EGTRDFVACN HLRSYKYYSE SILNPDGFAS
YPCASYRAFE SNKCFPCPDQ GCPQMGHYAD KFAVKTSDET QKYFLNTGDS SNFARWRYGV
SITLSGKRAT GQAKVALFGS KGNTHQFNIF KGILKPGSTH SNEFDAKLDV GTIEKVKFLW
NNNVVNPTFP KVGAAKITVQ KGEEKTVHSF CSESTVREDV LLTLTPC
