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Inactive pancreatic lipase-related protein 1 (PL-RP1)

 LIPR1_HUMAN             Reviewed;         467 AA.
P54315; Q68D83; Q68DR6; Q8TAU2; Q9BS82;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-OCT-2018, entry version 163.
RecName: Full=Inactive pancreatic lipase-related protein 1;
Short=PL-RP1;
Flags: Precursor;
Name=PNLIPRP1; Synonyms=PLRP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ABSENCE OF LIPASE ACTIVITY,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Pancreas;
PubMed=1379598;
Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.;
"Two novel human pancreatic lipase related proteins, hPLRP1 and
hPLRP2. Differences in colipase dependence and in lipase activity.";
J. Biol. Chem. 267:16509-16516(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Liver;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ASP-414.
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND ABSENCE OF CATALYTIC ACTIVITY.
PubMed=19824014; DOI=10.1002/mnfr.200800563;
Berton A., Sebban-Kreuzer C., Rouvellac S., Lopez C., Crenon I.;
"Individual and combined action of pancreatic lipase and pancreatic
lipase-related proteins 1 and 2 on native versus homogenized milk fat
globules.";
Mol. Nutr. Food Res. 53:1592-1602(2009).
[5]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-467 IN COMPLEX WITH
CALCIUM IONS, AND DISULFIDE BONDS.
Structural genomics consortium (SGC);
"Structure of the human pancreatic lipase-related protein 1.";
Submitted (FEB-2009) to the PDB data bank.
[6]
VARIANT [LARGE SCALE ANALYSIS] CYS-129.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: May function as inhibitor of dietary triglyceride
digestion. Lacks detectable lipase activity towards triglycerides,
diglycerides, phosphatidylcholine, galactolipids or cholesterol
esters (in vitro) (By similarity). {ECO:0000250,
ECO:0000269|PubMed:19824014}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1379598,
ECO:0000269|PubMed:19824014}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P54315-1; Sequence=Displayed;
Name=2;
IsoId=P54315-2; Sequence=VSP_014097, VSP_014100;
Name=3;
IsoId=P54315-3; Sequence=VSP_014098, VSP_014099;
-!- TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:1379598}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M93283; AAA59532.1; -; mRNA.
EMBL; CR749299; CAH18154.1; -; mRNA.
EMBL; CR749524; CAH18337.1; -; mRNA.
EMBL; BC005233; AAH05233.1; -; mRNA.
EMBL; BC025784; AAH25784.1; -; mRNA.
CCDS; CCDS7595.1; -. [P54315-1]
PIR; A43357; A43357.
RefSeq; NP_001290064.1; NM_001303135.1. [P54315-1]
RefSeq; NP_006220.1; NM_006229.3. [P54315-1]
RefSeq; XP_011538170.1; XM_011539868.1.
UniGene; Hs.73923; -.
PDB; 2PPL; X-ray; 2.20 A; A=18-467.
PDBsum; 2PPL; -.
ProteinModelPortal; P54315; -.
SMR; P54315; -.
BioGrid; 111408; 10.
IntAct; P54315; 34.
MINT; P54315; -.
STRING; 9606.ENSP00000351695; -.
ESTHER; human-PNLIPRP1; Pancreatic_lipase.
BioMuta; PNLIPRP1; -.
DMDM; 1708837; -.
PaxDb; P54315; -.
PeptideAtlas; P54315; -.
PRIDE; P54315; -.
ProteomicsDB; 56681; -.
ProteomicsDB; 56682; -. [P54315-2]
ProteomicsDB; 56683; -. [P54315-3]
Ensembl; ENST00000358834; ENSP00000351695; ENSG00000187021. [P54315-1]
Ensembl; ENST00000528052; ENSP00000433933; ENSG00000187021. [P54315-1]
GeneID; 5407; -.
KEGG; hsa:5407; -.
UCSC; uc001lco.2; human. [P54315-1]
CTD; 5407; -.
EuPathDB; HostDB:ENSG00000187021.14; -.
GeneCards; PNLIPRP1; -.
HGNC; HGNC:9156; PNLIPRP1.
MIM; 604422; gene.
neXtProt; NX_P54315; -.
OpenTargets; ENSG00000187021; -.
PharmGKB; PA33479; -.
eggNOG; ENOG410IHRX; Eukaryota.
eggNOG; ENOG410Y92X; LUCA.
GeneTree; ENSGT00760000119069; -.
HOGENOM; HOG000038552; -.
HOVERGEN; HBG003243; -.
InParanoid; P54315; -.
KO; K14074; -.
OMA; DQGCPQM; -.
PhylomeDB; P54315; -.
TreeFam; TF324997; -.
BRENDA; 3.1.1.26; 2681.
Reactome; R-HSA-192456; Digestion of dietary lipid.
EvolutionaryTrace; P54315; -.
GenomeRNAi; 5407; -.
PRO; PR:P54315; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000187021; Expressed in 80 organ(s), highest expression level in body of pancreas.
CleanEx; HS_PNLIPRP1; -.
ExpressionAtlas; P54315; baseline and differential.
Genevisible; P54315; HS.
GO; GO:0005576; C:extracellular region; TAS:ProtInc.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0004806; F:triglyceride lipase activity; TAS:ProtInc.
GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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; Alternative splicing; Calcium; Complete proteome;
Disulfide bond; Metal-binding; Polymorphism; Reference proteome;
Secreted; Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 467 Inactive pancreatic lipase-related
protein 1.
/FTId=PRO_0000017790.
DOMAIN 356 467 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
ACT_SITE 171 171 Nucleophile.
ACT_SITE 194 194 Charge relay system.
ACT_SITE 281 281 Charge relay system.
METAL 205 205 Calcium; via carbonyl oxygen.
METAL 208 208 Calcium; via carbonyl oxygen.
METAL 210 210 Calcium.
METAL 213 213 Calcium.
DISULFID 21 27 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|Ref.5}.
DISULFID 109 120 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|Ref.5}.
DISULFID 255 279 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|Ref.5}.
DISULFID 303 314 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|Ref.5}.
DISULFID 317 322 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|Ref.5}.
DISULFID 451 467 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|Ref.5}.
VAR_SEQ 111 186 KLFEVEEVNCICVDWKKGSQATYTQAANNVRVVGAQVAQML
DILLTEYSYPPSKVHLIGHSLGAHVAGEAGSKTPG -> VG
ASSDPCGQLRPTLLLTSLHHFMHSRNLYILGNFMQLKCFSS
QKLKCLSMFPHYICTLKQPHLLLEKYSYYLISG (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014097.
VAR_SEQ 111 117 KLFEVEE -> PGASPRA (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_014098.
VAR_SEQ 118 467 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_014099.
VAR_SEQ 187 467 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014100.
VARIANT 61 61 N -> D (in dbSNP:rs11197744).
/FTId=VAR_049820.
VARIANT 129 129 S -> C (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036379.
VARIANT 271 271 A -> V (in dbSNP:rs2305205).
/FTId=VAR_022082.
VARIANT 414 414 E -> D (in dbSNP:rs2305204).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_022659.
VARIANT 461 461 L -> P (in dbSNP:rs1049125).
/FTId=VAR_014915.
STRAND 19 22 {ECO:0000244|PDB:2PPL}.
TURN 23 25 {ECO:0000244|PDB:2PPL}.
STRAND 26 30 {ECO:0000244|PDB:2PPL}.
TURN 32 34 {ECO:0000244|PDB:2PPL}.
STRAND 35 40 {ECO:0000244|PDB:2PPL}.
HELIX 49 52 {ECO:0000244|PDB:2PPL}.
STRAND 55 63 {ECO:0000244|PDB:2PPL}.
STRAND 68 71 {ECO:0000244|PDB:2PPL}.
HELIX 76 80 {ECO:0000244|PDB:2PPL}.
STRAND 87 93 {ECO:0000244|PDB:2PPL}.
HELIX 104 115 {ECO:0000244|PDB:2PPL}.
STRAND 118 124 {ECO:0000244|PDB:2PPL}.
HELIX 126 129 {ECO:0000244|PDB:2PPL}.
HELIX 133 158 {ECO:0000244|PDB:2PPL}.
HELIX 162 164 {ECO:0000244|PDB:2PPL}.
STRAND 165 170 {ECO:0000244|PDB:2PPL}.
HELIX 173 182 {ECO:0000244|PDB:2PPL}.
STRAND 189 194 {ECO:0000244|PDB:2PPL}.
TURN 198 202 {ECO:0000244|PDB:2PPL}.
TURN 205 207 {ECO:0000244|PDB:2PPL}.
HELIX 211 213 {ECO:0000244|PDB:2PPL}.
STRAND 214 220 {ECO:0000244|PDB:2PPL}.
HELIX 227 230 {ECO:0000244|PDB:2PPL}.
STRAND 240 246 {ECO:0000244|PDB:2PPL}.
STRAND 249 251 {ECO:0000244|PDB:2PPL}.
HELIX 266 270 {ECO:0000244|PDB:2PPL}.
HELIX 279 293 {ECO:0000244|PDB:2PPL}.
TURN 295 298 {ECO:0000244|PDB:2PPL}.
HELIX 306 310 {ECO:0000244|PDB:2PPL}.
STRAND 324 326 {ECO:0000244|PDB:2PPL}.
HELIX 327 331 {ECO:0000244|PDB:2PPL}.
STRAND 341 345 {ECO:0000244|PDB:2PPL}.
STRAND 349 352 {ECO:0000244|PDB:2PPL}.
STRAND 356 367 {ECO:0000244|PDB:2PPL}.
STRAND 369 379 {ECO:0000244|PDB:2PPL}.
STRAND 387 394 {ECO:0000244|PDB:2PPL}.
STRAND 399 408 {ECO:0000244|PDB:2PPL}.
STRAND 412 421 {ECO:0000244|PDB:2PPL}.
STRAND 432 441 {ECO:0000244|PDB:2PPL}.
STRAND 447 451 {ECO:0000244|PDB:2PPL}.
STRAND 462 466 {ECO:0000244|PDB:2PPL}.
SEQUENCE 467 AA; 51848 MW; 2781EA1E22E39E78 CRC64;
MLIFWTITLF LLGAAKGKEV CYEDLGCFSD TEPWGGTAIR PLKILPWSPE KIGTRFLLYT
NENPNNFQIL LLSDPSTIEA SNFQMDRKTR FIIHGFIDKG DESWVTDMCK KLFEVEEVNC
ICVDWKKGSQ ATYTQAANNV RVVGAQVAQM LDILLTEYSY PPSKVHLIGH SLGAHVAGEA
GSKTPGLSRI TGLDPVEASF ESTPEEVRLD PSDADFVDVI HTDAAPLIPF LGFGTNQQMG
HLDFFPNGGE SMPGCKKNAL SQIVDLDGIW AGTRDFVACN HLRSYKYYLE SILNPDGFAA
YPCTSYKSFE SDKCFPCPDQ GCPQMGHYAD KFAGRTSEEQ QKFFLNTGEA SNFARWRYGV
SITLSGRTAT GQIKVALFGN KGNTHQYSIF RGILKPGSTH SYEFDAKLDV GTIEKVKFLW
NNNVINPTLP KVGATKITVQ KGEEKTVYNF CSEDTVREDT LLTLTPC


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