LIPR1_RAT
ID LIPR1_RAT Reviewed; 473 AA.
AC P54316;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Inactive pancreatic lipase-related protein 1;
DE Short=PL-RP1;
DE Flags: Precursor;
GN Name=Pnliprp1; Synonyms=Plrp1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Pancreas;
RX PubMed=1730292; DOI=10.1016/0014-5793(92)80403-4;
RA Wicker-Planquart C., Puigserver A.;
RT "Primary structure of rat pancreatic lipase mRNA.";
RL FEBS Lett. 296:61-66(1992).
CC -!- FUNCTION: May function as inhibitor of dietary triglyceride digestion.
CC Lacks detectable lipase activity (in vitro) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the pancreatic lipase.
CC {ECO:0000305|PubMed:1730292}.
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DR EMBL; X61925; CAA43927.1; -; mRNA.
DR PIR; S20612; S20612.
DR RefSeq; NP_114470.1; NM_032081.1.
DR AlphaFoldDB; P54316; -.
DR SMR; P54316; -.
DR STRING; 10116.ENSRNOP00000024164; -.
DR ESTHER; ratno-3plip; Pancreatic_lipase.
DR GlyGen; P54316; 1 site.
DR PaxDb; P54316; -.
DR GeneID; 84028; -.
DR KEGG; rno:84028; -.
DR CTD; 5407; -.
DR RGD; 620792; Pnliprp1.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR InParanoid; P54316; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; P54316; -.
DR BRENDA; 3.1.1.26; 5301.
DR Reactome; R-RNO-192456; Digestion of dietary lipid.
DR PRO; PR:P54316; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0016298; F:lipase activity; IDA:RGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0031016; P:pancreas development; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..473
FT /note="Inactive pancreatic lipase-related protein 1"
FT /id="PRO_0000017792"
FT DOMAIN 356..470
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 109..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 255..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 303..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 317..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 451..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
SQ SEQUENCE 473 AA; 52378 MW; CE03D1E021F30723 CRC64;
MLTLWTVSLF LLGAAQGKEV CYDNLGCFSD AEPWAGTAIR PLKLLPWSPE KINTRFLLYT
NENPTAFQTL QLSDPLTIGA SNFQVARKTR FIIHGFIDKG EENWVVDMCK NMFQVEEVNC
ICVDWKKGSQ TTYTQAANNV RVVGAQVAQM IDILVKNYSY SPSKVHLIGH SLGAHVAGEA
GSRTPGLGRI TGLDPVEANF EGTPEEVRLD PSDADFVDVI HTDAAPLIPF LGFGTNQMSG
HLDFFPNGGQ SMPGCKKNAL SQIVDIDGIW SGTRDFVACN HLRSYKYYLE SILNPDGFAA
YPCASYKDFE SNKCFPCPDQ GCPQMGHYAD KFAGKSGDEP QKFFLNTGEA KNFARWRYRV
SLILSGRMVT GQVKVALFGS KGNTRQYDIF RGIIKPGATH SSEFDAKLDV GTIEKVKFLW
NNQVINPSFP KVGAAKITVQ KGEERTEYNF CSEETVREDT LLTLLPCETS DTV
