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LIPR3_HUMAN
ID   LIPR3_HUMAN             Reviewed;         467 AA.
AC   Q17RR3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Pancreatic lipase-related protein 3;
DE            Short=PL-RP3;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=PNLIPRP3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-381 AND GLY-382.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=19640199;
RA   Saelee P., Wongkham S., Puapairoj A., Khuntikeo N., Petmitr S.,
RA   Chariyalertsak S., Sumethchotimaytha W., Karalak A.;
RT   "Novel PNLIPRP3 and DOCK8 gene expression and prognostic implications of
RT   DNA loss on chromosome 10q25.3 in hepatocellular carcinoma.";
RL   Asian Pac. J. Cancer Prev. 10:501-506(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Overexpressed in hepatocellular carcinoma.
CC       {ECO:0000269|PubMed:19640199}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AC011328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC117224; AAI17225.1; -; mRNA.
DR   CCDS; CCDS31292.1; -.
DR   RefSeq; NP_001011709.2; NM_001011709.2.
DR   AlphaFoldDB; Q17RR3; -.
DR   SMR; Q17RR3; -.
DR   STRING; 9606.ENSP00000358232; -.
DR   ESTHER; human-PNLIPRP3; Pancreatic_lipase.
DR   GlyGen; Q17RR3; 3 sites.
DR   iPTMnet; Q17RR3; -.
DR   PhosphoSitePlus; Q17RR3; -.
DR   BioMuta; PNLIPRP3; -.
DR   DMDM; 269849614; -.
DR   EPD; Q17RR3; -.
DR   jPOST; Q17RR3; -.
DR   MassIVE; Q17RR3; -.
DR   PaxDb; Q17RR3; -.
DR   PeptideAtlas; Q17RR3; -.
DR   PRIDE; Q17RR3; -.
DR   Antibodypedia; 52438; 113 antibodies from 15 providers.
DR   DNASU; 119548; -.
DR   Ensembl; ENST00000369230.4; ENSP00000358232.3; ENSG00000203837.5.
DR   GeneID; 119548; -.
DR   KEGG; hsa:119548; -.
DR   MANE-Select; ENST00000369230.4; ENSP00000358232.3; NM_001011709.3; NP_001011709.2.
DR   UCSC; uc001lcl.5; human.
DR   CTD; 119548; -.
DR   DisGeNET; 119548; -.
DR   GeneCards; PNLIPRP3; -.
DR   HGNC; HGNC:23492; PNLIPRP3.
DR   HPA; ENSG00000203837; Tissue enhanced (breast, skin).
DR   neXtProt; NX_Q17RR3; -.
DR   OpenTargets; ENSG00000203837; -.
DR   PharmGKB; PA134954941; -.
DR   VEuPathDB; HostDB:ENSG00000203837; -.
DR   eggNOG; ENOG502SHK7; Eukaryota.
DR   GeneTree; ENSGT00940000163197; -.
DR   HOGENOM; CLU_027171_0_2_1; -.
DR   InParanoid; Q17RR3; -.
DR   OMA; NRSYYFL; -.
DR   OrthoDB; 534956at2759; -.
DR   PhylomeDB; Q17RR3; -.
DR   TreeFam; TF324997; -.
DR   PathwayCommons; Q17RR3; -.
DR   Reactome; R-HSA-192456; Digestion of dietary lipid.
DR   SignaLink; Q17RR3; -.
DR   BioGRID-ORCS; 119548; 6 hits in 1064 CRISPR screens.
DR   ChiTaRS; PNLIPRP3; human.
DR   GenomeRNAi; 119548; -.
DR   Pharos; Q17RR3; Tdark.
DR   PRO; PR:Q17RR3; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q17RR3; protein.
DR   Bgee; ENSG00000203837; Expressed in upper leg skin and 66 other tissues.
DR   Genevisible; Q17RR3; HS.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR   GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
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   SUPFAM; SSF49723; SSF49723; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..467
FT                   /note="Pancreatic lipase-related protein 3"
FT                   /id="PRO_0000286602"
FT   DOMAIN          355..467
FT                   /note="PLAT"
FT   ACT_SITE        168
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        191
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        279
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        21..27
FT                   /evidence="ECO:0000250"
FT   DISULFID        107..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        252..277
FT                   /evidence="ECO:0000250"
FT   DISULFID        301..312
FT                   /evidence="ECO:0000250"
FT   DISULFID        315..320
FT                   /evidence="ECO:0000250"
FT   DISULFID        451..467
FT                   /evidence="ECO:0000250"
FT   VARIANT         2
FT                   /note="L -> F (in dbSNP:rs10885929)"
FT                   /id="VAR_032141"
FT   VARIANT         332
FT                   /note="F -> L (in dbSNP:rs7077408)"
FT                   /id="VAR_032142"
FT   VARIANT         381
FT                   /note="V -> I (in dbSNP:rs10736251)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_060285"
FT   VARIANT         382
FT                   /note="R -> G (in dbSNP:rs1897519)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_060286"
FT   VARIANT         450
FT                   /note="F -> Y (in dbSNP:rs2116286)"
FT                   /id="VAR_032143"
SQ   SEQUENCE   467 AA;  52254 MW;  F383E516278D1FC2 CRC64;
     MLGIWIVAFL FFGTSRGKEV CYERLGCFKD GLPWTRTFST ELVGLPWSPE KINTRFLLYT
     IHNPNAYQEI SAVNSSTIQA SYFGTDKITR INIAGWKTDG KWQRDMCNVL LQLEDINCIN
     LDWINGSREY IHAVNNLRVV GAEVAYFIDV LMKKFEYSPS KVHLIGHSLG AHLAGEAGSR
     IPGLGRITGL DPAGPFFHNT PKEVRLDPSD ANFVDVIHTN AARILFELGV GTIDACGHLD
     FYPNGGKHMP GCEDLITPLL KFNFNAYKKE MASFFDCNHA RSYQFYAESI LNPDAFIAYP
     CRSYTSFKAG NCFFCSKEGC PTMGHFADRF HFKNMKTNGS HYFLNTGSLS PFARWRHKLS
     VKLSGSEVTQ GTVFLRVGGA VRKTGEFAIV SGKLEPGMTY TKLIDADVNV GNITSVQFIW
     KKHLFEDSQN KLGAEMVINT SGKYGYKSTF CSQDIMGPNI LQNLKPC
 
 
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