ID PLPL3_HUMAN Reviewed; 481 AA. AC Q9NST1; B0QYI0; B2RCL3; B3KW00; Q6P1A1; Q96CB4; DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 2. DT 11-NOV-2015, entry version 122. DE RecName: Full=Patatin-like phospholipase domain-containing protein 3; DE EC=3.1.1.3; DE AltName: Full=Acylglycerol O-acyltransferase; DE EC=2.3.1.-; DE AltName: Full=Adiponutrin; DE AltName: Full=Calcium-independent phospholipase A2-epsilon; DE Short=iPLA2-epsilon; GN Name=PNPLA3; Synonyms=ADPN, C22orf20; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12529303; DOI=10.1101/gr.695703; RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., RA Knowles S., Bye J.M., Beare D.M., Dunham I.; RT "Reevaluating human gene annotation: a second-generation analysis of RT chromosome 22."; RL Genome Res. 13:27-36(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP GLU-434. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND RP VARIANTS CYS-115; MET-148 AND GLU-434. RC TISSUE=Brain, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-434. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS RP GLY-99; MET-148 AND GLU-434. RC TISSUE=Brain, and Skin; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15364929; DOI=10.1074/jbc.M407841200; RA Jenkins C.M., Mancuso D.J., Yan W., Sims H.F., Gibson B., Gross R.W.; RT "Identification, cloning, expression, and purification of three novel RT human calcium-independent phospholipase A2 family members possessing RT triacylglycerol lipase and acylglycerol transacylase activities."; RL J. Biol. Chem. 279:48968-48975(2004). RN [8] RP INDUCTION. RX PubMed=15181042; DOI=10.1210/jc.2003-031978; RA Liu Y.-M., Moldes M., Bastard J.-P., Bruckert E., Viguerie N., RA Hainque B., Basdevant A., Langin D., Pairault J., Clement K.; RT "Adiponutrin: A new gene regulated by energy balance in human adipose RT tissue."; RL J. Clin. Endocrinol. Metab. 89:2684-2689(2004). RN [9] RP VARIANT MET-148, AND POLYMORPHISM. RX PubMed=18728122; DOI=10.1530/EJE-08-0426; RA Johansson L.E., Lindblad U., Larsson C.A., Raastam L., RA Ridderstraale M.; RT "Polymorphisms in the adiponutrin gene are associated with increased RT insulin secretion and obesity."; RL Eur. J. Endocrinol. 159:577-583(2008). RN [10] RP VARIANTS MET-148 AND ILE-453, AND INVOLVEMENT IN SUSCEPTIBILITY TO RP NAFLD1. RX PubMed=18820647; DOI=10.1038/ng.257; RA Romeo S., Kozlitina J., Xing C., Pertsemlidis A., Cox D., RA Pennacchio L.A., Boerwinkle E., Cohen J.C., Hobbs H.H.; RT "Genetic variation in PNPLA3 confers susceptibility to nonalcoholic RT fatty liver disease."; RL Nat. Genet. 40:1461-1465(2008). RN [11] RP VARIANT MET-148, AND INVOLVEMENT IN SUSCEPTIBILITY TO NAFLD1. RX PubMed=19224197; DOI=10.1007/s00125-009-1285-z; RA Kotronen A., Johansson L.E., Johansson L.M., Roos C., Westerbacka J., RA Hamsten A., Bergholm R., Arkkila P., Arola J., Kiviluoto T., RA Fisher R.M., Ehrenborg E., Orho-Melander M., Ridderstrale M., RA Groop L., Yki-Jarvinen H.; RT "A common variant in PNPLA3, which encodes adiponutrin, is associated RT with liver fat content in humans."; RL Diabetologia 52:1056-1060(2009). RN [12] RP CHARACTERIZATION OF VARIANT MET-148. RX PubMed=20034933; DOI=10.1074/jbc.M109.064501; RA He S., McPhaul C., Li J.Z., Garuti R., Kinch L., Grishin N.V., RA Cohen J.C., Hobbs H.H.; RT "A sequence variation (I148M) in PNPLA3 associated with nonalcoholic RT fatty liver disease disrupts triglyceride hydrolysis."; RL J. Biol. Chem. 285:6706-6715(2010). RN [13] RP VARIANT MET-148, AND INVOLVEMENT IN SUSCEPTIBILITY TO NAFLD1. RX PubMed=19738004; DOI=10.1194/jlr.P900013-JLR200; RA Sookoian S., Castano G.O., Burgueno A.L., Gianotti T.F., RA Rosselli M.S., Pirola C.J.; RT "A nonsynonymous gene variant in the adiponutrin gene is associated RT with nonalcoholic fatty liver disease severity."; RL J. Lipid Res. 50:2111-2116(2009). CC -!- FUNCTION: Multifunctional enzyme which has both triacylglycerol CC lipase and acylglycerol O-acyltransferase activities. CC {ECO:0000269|PubMed:15364929}. CC -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a CC carboxylate. CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15364929}; CC Single-pass type II membrane protein CC {ECO:0000269|PubMed:15364929}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NST1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NST1-2; Sequence=VSP_036222; CC Note=No experimental confirmation available.; CC -!- INDUCTION: By changes in energy balance: down-regulated following CC very low-calorie diet, whereas refeeding elevates the mRNA level. CC {ECO:0000269|PubMed:15181042}. CC -!- POLYMORPHISM: Polymorphic variation at position 148 influences CC insulin secretion levels and obesity. In obese subjects the body CC mass index and waist are higher in carriers of the Ile-148 allele. CC The Ile-148 carriers also display decreased insulin secretion in CC response to oral glucose tolerance test. Met-148 allele carriers CC are seemingly more insulin resistant at a lower body mass index. CC -!- DISEASE: Non-alcoholic fatty liver disease 1 (NAFLD1) CC [MIM:613282]: A condition characterized by accumulation of CC triglycerides in the liver. It is associated with adverse CC metabolic consequences, including insulin resistance and CC dyslipidemia. In a subset of individuals, hepatic steatosis CC promotes an inflammatory response in the liver, referred to as CC steatohepatitis, which can progress to cirrhosis and liver cancer. CC NAFLD is the most common form of liver disease in Western CC countries. {ECO:0000269|PubMed:18820647, CC ECO:0000269|PubMed:19224197, ECO:0000269|PubMed:19738004}. CC Note=Disease susceptibility is associated with variations CC affecting the gene represented in this entry. CC -!- SIMILARITY: Contains 1 patatin domain. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL138578; CAB71238.2; -; mRNA. DR EMBL; CR456476; CAG30362.1; -; mRNA. DR EMBL; AK123806; BAG53962.1; -; mRNA. DR EMBL; AK315166; BAG37610.1; -; mRNA. DR EMBL; AL023654; CAI21791.1; -; Genomic_DNA. DR EMBL; AL035398; CAI21791.1; JOINED; Genomic_DNA. DR EMBL; AL035398; CAI22840.1; -; Genomic_DNA. DR EMBL; AL023654; CAI22840.1; JOINED; Genomic_DNA. DR EMBL; AL023654; CAQ07959.1; -; Genomic_DNA. DR EMBL; AL035398; CAQ07959.1; JOINED; Genomic_DNA. DR EMBL; AL035398; CAQ09484.1; -; Genomic_DNA. DR EMBL; AL023654; CAQ09484.1; JOINED; Genomic_DNA. DR EMBL; CH471138; EAW73324.1; -; Genomic_DNA. DR EMBL; BC014449; AAH14449.2; -; mRNA. DR EMBL; BC065195; AAH65195.1; -; mRNA. DR CCDS; CCDS14054.1; -. [Q9NST1-1] DR RefSeq; NP_079501.2; NM_025225.2. [Q9NST1-1] DR UniGene; Hs.654800; -. DR ProteinModelPortal; Q9NST1; -. DR BioGrid; 123247; 4. DR IntAct; Q9NST1; 2. DR STRING; 9606.ENSP00000216180; -. DR PhosphoSite; Q9NST1; -. DR BioMuta; PNPLA3; -. DR DMDM; 32469599; -. DR MaxQB; Q9NST1; -. DR PaxDb; Q9NST1; -. DR PRIDE; Q9NST1; -. DR DNASU; 80339; -. DR Ensembl; ENST00000216180; ENSP00000216180; ENSG00000100344. [Q9NST1-1] DR Ensembl; ENST00000423180; ENSP00000397987; ENSG00000100344. [Q9NST1-2] DR GeneID; 80339; -. DR KEGG; hsa:80339; -. DR UCSC; uc003bei.1; human. [Q9NST1-1] DR CTD; 80339; -. DR GeneCards; PNPLA3; -. DR H-InvDB; HIX0159175; -. DR HGNC; HGNC:18590; PNPLA3. DR HPA; HPA058058; -. DR MIM; 609567; gene. DR MIM; 613282; phenotype. DR neXtProt; NX_Q9NST1; -. DR Orphanet; 33271; Non-alcoholic fatty liver disease. DR PharmGKB; PA38592; -. DR eggNOG; KOG3773; Eukaryota. DR eggNOG; ENOG410XSQS; LUCA. DR GeneTree; ENSGT00390000005295; -. DR HOGENOM; HOG000007467; -. DR HOVERGEN; HBG007046; -. DR InParanoid; Q9NST1; -. DR KO; K13534; -. DR OMA; FDAKTTI; -. DR OrthoDB; EOG7J9VQR; -. DR PhylomeDB; Q9NST1; -. DR TreeFam; TF314272; -. DR Reactome; R-HSA-1482883; Acyl chain remodeling of DAG and TAG. DR UniPathway; UPA00256; -. DR GeneWiki; PNPLA3; -. DR GenomeRNAi; 80339; -. DR NextBio; 70910; -. DR PRO; PR:Q9NST1; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; Q9NST1; -. DR CleanEx; HS_PNPLA3; -. DR ExpressionAtlas; Q9NST1; baseline and differential. DR Genevisible; Q9NST1; HS. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0051265; F:diolein transacylation activity; IDA:UniProtKB. DR GO; GO:0051264; F:mono-olein transacylation activity; IDA:UniProtKB. DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB. DR GO; GO:0036155; P:acylglycerol acyl-chain remodeling; TAS:Reactome. DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome. DR GO; GO:0006644; P:phospholipid metabolic process; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0036153; P:triglyceride acyl-chain remodeling; IDA:CACAO. DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB. DR GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR002641; Patatin/PLipase_A2-rel. DR Pfam; PF01734; Patatin; 1. DR SUPFAM; SSF52151; SSF52151; 1. PE 1: Evidence at protein level; KW Acyltransferase; Alternative splicing; Complete proteome; KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; KW Membrane; Obesity; Polymorphism; Reference proteome; Signal-anchor; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 481 Patatin-like phospholipase domain- FT containing protein 3. FT /FTId=PRO_0000064458. FT TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 42 62 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 63 481 Lumenal. {ECO:0000255}. FT DOMAIN 10 179 Patatin. FT MOTIF 45 49 GXSXG. FT ACT_SITE 47 47 {ECO:0000250}. FT CARBOHYD 89 89 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 280 280 N-linked (GlcNAc...). {ECO:0000255}. FT VAR_SEQ 59 62 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_036222. FT VARIANT 99 99 C -> G (in dbSNP:rs2076213). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_015845. FT VARIANT 115 115 G -> C (in dbSNP:rs2076212). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_015846. FT VARIANT 148 148 I -> M (common polymorphism; fails to FT hydrolyze emulsified triglycerides; FT associated with increased hepatic fat FT content and serum aspartate FT aminotransferase concentrations; FT dbSNP:rs738409). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18728122, FT ECO:0000269|PubMed:18820647, FT ECO:0000269|PubMed:19224197, FT ECO:0000269|PubMed:19738004, FT ECO:0000269|PubMed:20034933}. FT /FTId=VAR_019961. FT VARIANT 216 216 T -> P (in dbSNP:rs35726887). FT /FTId=VAR_053814. FT VARIANT 434 434 K -> E (in dbSNP:rs2294918). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15461802, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.5}. FT /FTId=VAR_015847. FT VARIANT 453 453 S -> I (common polymorphism; associated FT with lower hepatic fat content in African FT Americans; dbSNP:rs6006460). FT {ECO:0000269|PubMed:18820647}. FT /FTId=VAR_053815. SQ SEQUENCE 481 AA; 52865 MW; 1ED0341B5AF5B6CB CRC64; MYDAERGWSL SFAGCGFLGF YHVGATRCLS EHAPHLLRDA RMLFGASAGA LHCVGVLSGI PLEQTLQVLS DLVRKARSRN IGIFHPSFNL SKFLRQGLCK CLPANVHQLI SGKIGISLTR VSDGENVLVS DFRSKDEVVD ALVCSCFIPF YSGLIPPSFR GVRYVDGGVS DNVPFIDAKT TITVSPFYGE YDICPKVKST NFLHVDITKL SLRLCTGNLY LLSRAFVPPD LKVLGEICLR GYLDAFRFLE EKGICNRPQP GLKSSSEGMD PEVAMPSWAN MSLDSSPESA ALAVRLEGDE LLDHLRLSIL PWDESILDTL SPRLATALSE EMKDKGGYMS KICNLLPIRI MSYVMLPCTL PVESAIAIVQ RLVTWLPDMP DDVLWLQWVT SQVFTRVLMC LLPASRSQMP VSSQQASPCT PEQDWPCWTP CSPKGCPAET KAEATPRSIL RSSLNFFLGN KVPAGAEGLS TFPSFSLEKS L //