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Pancreatic lipase-related protein 2 (PL-RP2) (EC 3.1.1.26) (EC 3.1.1.3) (Galactolipase) (Secretory glycoprotein GP-3)

 LIPR2_RAT               Reviewed;         468 AA.
P54318;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
12-SEP-2018, entry version 128.
RecName: Full=Pancreatic lipase-related protein 2 {ECO:0000250|UniProtKB:P54317};
Short=PL-RP2 {ECO:0000250|UniProtKB:P54317};
EC=3.1.1.26;
EC=3.1.1.3;
AltName: Full=Galactolipase;
AltName: Full=Secretory glycoprotein GP-3 {ECO:0000303|PubMed:8486693};
Flags: Precursor;
Name=Pnliprp2 {ECO:0000312|RGD:620793};
Synonyms=Plrp2 {ECO:0000250|UniProtKB:P54317};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-46.
STRAIN=Sprague-Dawley; TISSUE=Pancreas;
PubMed=8486693;
Wishart M.J., Andrews P.C., Nichols R., Blevins G.T. Jr.,
Logsdon C.D., Williams J.A.;
"Identification and cloning of GP-3 from rat pancreatic acinar zymogen
granules as a glycosylated membrane-associated lipase.";
J. Biol. Chem. 268:10303-10311(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8203536;
Payne R.M., Sims H.F., Jennens M.L., Lowe M.E.;
"Rat pancreatic lipase and two related proteins: enzymatic properties
and mRNA expression during development.";
Am. J. Physiol. 266:G914-G921(1994).
[3]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 17-468, DISULFIDE BONDS,
GLYCOSYLATION AT ASN-352, CATALYTIC ACTIVITY, ACTIVE SITE, AND
FUNCTION.
TISSUE=Pancreas;
PubMed=9822688; DOI=10.1074/jbc.273.48.32121;
Roussel A., Yang Y., Ferrato F., Verger R., Cambillau C., Lowe M.;
"Structure and activity of rat pancreatic lipase-related protein 2.";
J. Biol. Chem. 273:32121-32128(1998).
-!- FUNCTION: Lipase with broad substrate specificity. Can hydrolyze
both phospholipids and galactolipids. Shows a preference for 1,2-
didodecanoylphosphatidylethanolamine and 1,2-
didodecanoylphosphatidylglycerol, and has low activity towards
1,2-didodecanoylphosphatidylcholine (in vitro).
{ECO:0000250|UniProtKB:P17892, ECO:0000250|UniProtKB:P54317,
ECO:0000269|PubMed:9822688}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate. {ECO:0000269|PubMed:9822688}.
-!- CATALYTIC ACTIVITY: 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2
H(2)O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates.
{ECO:0000269|PubMed:9822688}.
-!- ACTIVITY REGULATION: CLPS stimulates triacylglycerol lipase
activity. Triacylglycerol lipase activity is not inhibited by
increasing bile salt concentration.
{ECO:0000250|UniProtKB:P17892}.
-!- SUBCELLULAR LOCATION: Secreted. Membrane.
-!- TISSUE SPECIFICITY: Pancreatic secretory (zymogen) granule.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA41250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; L09216; AAA41250.1; ALT_INIT; mRNA.
PIR; A46696; A46696.
RefSeq; NP_476554.1; NM_057206.1.
UniGene; Rn.87688; -.
PDB; 1BU8; X-ray; 1.80 A; A=17-468.
PDBsum; 1BU8; -.
ProteinModelPortal; P54318; -.
SMR; P54318; -.
ESTHER; ratno-4plip; Pancreatic_lipase.
iPTMnet; P54318; -.
PRIDE; P54318; -.
GeneID; 117554; -.
KEGG; rno:117554; -.
CTD; 5408; -.
RGD; 620793; Pnliprp2.
HOVERGEN; HBG003243; -.
InParanoid; P54318; -.
KO; K14075; -.
BRENDA; 3.1.1.26; 5301.
EvolutionaryTrace; P54318; -.
PRO; PR:P54318; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0042589; C:zymogen granule membrane; IDA:RGD.
GO; GO:0102549; F:1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity; IEA:UniProtKB-EC.
GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0047714; F:galactolipase activity; IDA:RGD.
GO; GO:0016298; F:lipase activity; IDA:RGD.
GO; GO:0004620; F:phospholipase activity; IDA:RGD.
GO; GO:0004806; F:triglyceride lipase activity; IDA:RGD.
GO; GO:0019376; P:galactolipid catabolic process; IDA:RGD.
GO; GO:0009395; P:phospholipid catabolic process; ISS:UniProtKB.
GO; GO:0009791; P:post-embryonic development; IEP:RGD.
GO; GO:0032094; P:response to food; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0033993; P:response to lipid; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
CDD; cd00707; Pancreat_lipase_like; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013818; Lipase/vitellogenin.
InterPro; IPR016272; Lipase_LIPH.
InterPro; IPR033906; Lipase_N.
InterPro; IPR002331; Lipase_panc.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
InterPro; IPR000734; TAG_lipase.
PANTHER; PTHR11610; PTHR11610; 1.
Pfam; PF00151; Lipase; 1.
Pfam; PF01477; PLAT; 1.
PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
PRINTS; PR00823; PANCLIPASE.
PRINTS; PR00821; TAGLIPASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF49723; SSF49723; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00120; LIPASE_SER; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
Lipid metabolism; Membrane; Metal-binding; Reference proteome;
Secreted; Signal.
SIGNAL 1 16 {ECO:0000269|PubMed:8486693}.
CHAIN 17 468 Pancreatic lipase-related protein 2.
/FTId=PRO_0000017796.
DOMAIN 356 468 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
ACT_SITE 170 170 Nucleophile.
{ECO:0000269|PubMed:9822688}.
ACT_SITE 194 194 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10037,
ECO:0000269|PubMed:9822688}.
ACT_SITE 281 281 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10037,
ECO:0000269|PubMed:9822688}.
METAL 205 205 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 208 208 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 210 210 Calcium. {ECO:0000250}.
METAL 213 213 Calcium. {ECO:0000250}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9822688}.
DISULFID 20 26 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:9822688}.
DISULFID 108 119 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:9822688}.
DISULFID 255 279 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:9822688}.
DISULFID 303 314 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:9822688}.
DISULFID 317 322 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:9822688}.
DISULFID 452 468 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:9822688}.
STRAND 18 20 {ECO:0000244|PDB:1BU8}.
HELIX 22 24 {ECO:0000244|PDB:1BU8}.
STRAND 26 28 {ECO:0000244|PDB:1BU8}.
STRAND 33 36 {ECO:0000244|PDB:1BU8}.
HELIX 48 51 {ECO:0000244|PDB:1BU8}.
STRAND 54 59 {ECO:0000244|PDB:1BU8}.
STRAND 62 69 {ECO:0000244|PDB:1BU8}.
STRAND 71 73 {ECO:0000244|PDB:1BU8}.
HELIX 75 78 {ECO:0000244|PDB:1BU8}.
STRAND 86 92 {ECO:0000244|PDB:1BU8}.
HELIX 103 112 {ECO:0000244|PDB:1BU8}.
STRAND 117 123 {ECO:0000244|PDB:1BU8}.
HELIX 125 128 {ECO:0000244|PDB:1BU8}.
HELIX 132 157 {ECO:0000244|PDB:1BU8}.
HELIX 161 163 {ECO:0000244|PDB:1BU8}.
STRAND 164 169 {ECO:0000244|PDB:1BU8}.
HELIX 172 182 {ECO:0000244|PDB:1BU8}.
TURN 183 185 {ECO:0000244|PDB:1BU8}.
STRAND 187 194 {ECO:0000244|PDB:1BU8}.
TURN 198 202 {ECO:0000244|PDB:1BU8}.
HELIX 205 207 {ECO:0000244|PDB:1BU8}.
HELIX 211 213 {ECO:0000244|PDB:1BU8}.
STRAND 214 220 {ECO:0000244|PDB:1BU8}.
HELIX 227 230 {ECO:0000244|PDB:1BU8}.
STRAND 240 246 {ECO:0000244|PDB:1BU8}.
HELIX 266 270 {ECO:0000244|PDB:1BU8}.
HELIX 279 293 {ECO:0000244|PDB:1BU8}.
HELIX 295 297 {ECO:0000244|PDB:1BU8}.
HELIX 306 310 {ECO:0000244|PDB:1BU8}.
STRAND 324 326 {ECO:0000244|PDB:1BU8}.
HELIX 327 331 {ECO:0000244|PDB:1BU8}.
TURN 333 336 {ECO:0000244|PDB:1BU8}.
STRAND 337 345 {ECO:0000244|PDB:1BU8}.
STRAND 356 365 {ECO:0000244|PDB:1BU8}.
STRAND 370 380 {ECO:0000244|PDB:1BU8}.
STRAND 388 395 {ECO:0000244|PDB:1BU8}.
STRAND 400 409 {ECO:0000244|PDB:1BU8}.
STRAND 413 422 {ECO:0000244|PDB:1BU8}.
STRAND 433 442 {ECO:0000244|PDB:1BU8}.
TURN 443 445 {ECO:0000244|PDB:1BU8}.
STRAND 448 452 {ECO:0000244|PDB:1BU8}.
STRAND 463 467 {ECO:0000244|PDB:1BU8}.
SEQUENCE 468 AA; 52535 MW; B41FB0B339BA9A6F CRC64;
MLLCWIVSLL LATVGGKEVC YGHLGCFSND KPWAGMLQRP LKIFPWSPED IDTRFLLYTN
ENPNNYQKIS ATEPDTIKFS NFQLDRKTRF IVHGFIDKGE DGWLLDMCKK MFQVEKVNCI
CVDWRRGSRT EYTQASYNTR VVGAEIAFLV QVLSTEMGYS PENVHLIGHS LGAHVVGEAG
RRLEGHVGRI TGLDPAEPCF QGLPEEVRLD PSDAMFVDVI HTDSAPIIPY LGFGMSQKVG
HLDFFPNGGK EMPGCQKNIL STIVDINGIW EGTQNFVACN HLRSYKYYAS SILNPDGFLG
YPCSSYEKFQ QNDCFPCPEE GCPKMGHYAD QFEGKTATVE QTVYLNTGDS GNFTRWRYKV
SVTLSGAKKL SGYILVALYG NNGNSKQYEI FKGSLKPEAR HVRDIDVDIN VGEIQKVKFL
WNNKVINLFR PTLGASQITV QSGVDGKEYN FCSSDTVRED VLQSLYPC


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