ID ACOX2_HUMAN Reviewed; 681 AA. AC Q99424; A6NF16; B2R8U5; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 24-JAN-2024, entry version 197. DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 2 {ECO:0000303|PubMed:14702039}; DE EC=1.17.99.3 {ECO:0000269|PubMed:27884763}; DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase; DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase {ECO:0000250|UniProtKB:O02767}; DE AltName: Full=Trihydroxycoprostanoyl-CoA oxidase {ECO:0000250|UniProtKB:P97562}; DE Short=THCA-CoA oxidase {ECO:0000250|UniProtKB:O02767}; DE Short=THCCox; GN Name=ACOX2 {ECO:0000312|HGNC:HGNC:120}; 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 [MRNA], PROTEIN SEQUENCE OF 8-14; 271-282; 337-346; RP 450-468 AND 656-664, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=8943006; DOI=10.1073/pnas.93.24.13748; RA Baumgart E., Vanhooren J.C.T., Fransen M., Marynen P., Puype M., RA Vandekerckhove J., Leunissen J.A.M., Fahimi H.D., Mannaerts G.P., RA Van Veldhoven P.P.; RT "Molecular characterization of the human peroxisomal branched-chain acyl- RT CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and RT evidence for the absence of the protein in Zellweger's syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13748-13753(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Fournier B., Baumgart E., Fahimi D., Mannaerts G.P., Van Veldhoven P.P.; RT "Genomic sequence of peroxisomal human branched chain acyl-CoA oxidase."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND THR-13, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP INVOLVEMENT IN CBAS6, VARIANT CBAS6 69-TYR--LEU-682 DEL, AND RP CHARACTERIZATION OF VARIANT CBAS6 69-TYR--LEU-682 DEL. RX PubMed=27647924; DOI=10.1073/pnas.1613228113; RA Vilarinho S., Sari S., Mazzacuva F., Bilguevar K., Esendagli-Yilmaz G., RA Jain D., Akyol G., Dalgic B., Guenel M., Clayton P.T., Lifton R.P.; RT "ACOX2 deficiency: A disorder of bile acid synthesis with transaminase RT elevation, liver fibrosis, ataxia, and cognitive impairment."; RL Proc. Natl. Acad. Sci. U.S.A. 113:11289-11293(2016). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INVOLVEMENT IN CBAS6, RP VARIANT CBAS6 TRP-225, AND CHARACTERIZATION OF VARIANT CBAS6 TRP-225. RX PubMed=27884763; DOI=10.1016/j.jhep.2016.11.005; RA Monte M.J., Alonso-Pena M., Briz O., Herraez E., Berasain C., Argemi J., RA Prieto J., Marin J.J.; RT "ACOX2 deficiency: An inborn error of bile acid synthesis identified in an RT adolescent with persistent hypertransaminasemia."; RL J. Hepatol. 66:581-588(2017). CC -!- FUNCTION: Oxidizes the CoA esters of the bile acid intermediates CC di- and tri-hydroxycholestanoic acids (PubMed:27884763). Capable of CC oxidizing short as well as long chain 2-methyl branched fatty acids (By CC similarity). {ECO:0000250|UniProtKB:P07872, CC ECO:0000269|PubMed:27884763}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl- CC CoA + A + H2O = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy- CC 5beta-cholestan-26-oyl-CoA + AH2; Xref=Rhea:RHEA:15733, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:58677, ChEBI:CHEBI:59807; EC=1.17.99.3; CC Evidence={ECO:0000269|PubMed:27884763}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15734; CC Evidence={ECO:0000305|PubMed:27884763}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl- CC CoA + O2 = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24- CC en-26-oyl-CoA + H2O2; Xref=Rhea:RHEA:46728, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:59879, ChEBI:CHEBI:77251; CC Evidence={ECO:0000250|UniProtKB:O02767}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46729; CC Evidence={ECO:0000250|UniProtKB:O02767}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P07872}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07872}. CC -!- INTERACTION: CC Q99424; P63172: DYNLT1; NbExp=3; IntAct=EBI-12026476, EBI-1176455; CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:27884763, CC ECO:0000269|PubMed:8943006}. CC -!- TISSUE SPECIFICITY: Present in all tissues tested: heart, brain, CC placenta, lung, liver, skeletal muscle, kidney and pancreas. Most CC abundant in heart, liver and kidney. {ECO:0000269|PubMed:8943006}. CC -!- DISEASE: Congenital bile acid synthesis defect 6 (CBAS6) [MIM:617308]: CC An inborn error of bile acid synthesis characterized by abnormally CC increased liver enzymes, hypolipidemia and low cholesterol, vitamin D CC deficiency, elevated plasma and urinary levels of C27 intermediate bile CC acids 3alpha,7alpha-dihydroxy-5beta-cholestanoic acid (DHCA) and CC 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid (THCA). Serum CC levels of phytanic and pristanic acids are normal. Clinical features CC include liver fibrosis, mild ataxia, delayed development, and cognitive CC impairment. Liver histology shows many thin fibrous septa, swollen CC hepatocytes, glycogenated nuclei, and focal acinar transformation, CC consistent with hepatocellular injury and regeneration, without signs CC of obvious cholestasis, cholate stasis, or steatosis. CBAS6 CC transmission pattern is consistent with autosomal recessive CC inheritance. {ECO:0000269|PubMed:27647924, CC ECO:0000269|PubMed:27884763}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {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; X95190; CAA64489.1; -; mRNA. DR EMBL; AJ001541; CAB65596.1; -; Genomic_DNA. DR EMBL; AJ001542; CAB65596.1; JOINED; Genomic_DNA. DR EMBL; AJ001543; CAB65596.1; JOINED; Genomic_DNA. DR EMBL; AJ001544; CAB65596.1; JOINED; Genomic_DNA. DR EMBL; AJ001545; CAB65596.1; JOINED; Genomic_DNA. DR EMBL; AJ001546; CAB65596.1; JOINED; Genomic_DNA. DR EMBL; AJ001547; CAB65596.1; JOINED; Genomic_DNA. DR EMBL; AJ001548; CAB65596.1; JOINED; Genomic_DNA. DR EMBL; AK313512; BAG36292.1; -; mRNA. DR EMBL; AC116036; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW65375.1; -; Genomic_DNA. DR EMBL; BC047700; AAH47700.1; -; mRNA. DR CCDS; CCDS33775.1; -. DR RefSeq; NP_003491.1; NM_003500.3. DR RefSeq; XP_005265562.1; XM_005265505.1. DR AlphaFoldDB; Q99424; -. DR SMR; Q99424; -. DR BioGRID; 113906; 6. DR IntAct; Q99424; 3. DR STRING; 9606.ENSP00000307697; -. DR GlyGen; Q99424; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99424; -. DR PhosphoSitePlus; Q99424; -. DR SwissPalm; Q99424; -. DR BioMuta; ACOX2; -. DR DMDM; 17366636; -. DR jPOST; Q99424; -. DR MassIVE; Q99424; -. DR MaxQB; Q99424; -. DR PaxDb; 9606-ENSP00000307697; -. DR PeptideAtlas; Q99424; -. DR ProteomicsDB; 78260; -. DR Antibodypedia; 31666; 339 antibodies from 33 providers. DR DNASU; 8309; -. DR Ensembl; ENST00000302819.10; ENSP00000307697.5; ENSG00000168306.13. DR GeneID; 8309; -. DR MANE-Select; ENST00000302819.10; ENSP00000307697.5; NM_003500.4; NP_003491.1. DR UCSC; uc003dkl.4; human. DR AGR; HGNC:120; -. DR CTD; 8309; -. DR DisGeNET; 8309; -. DR GeneCards; ACOX2; -. DR HGNC; HGNC:120; ACOX2. DR HPA; ENSG00000168306; Tissue enriched (liver). DR MalaCards; ACOX2; -. DR MIM; 601641; gene. DR MIM; 617308; phenotype. DR neXtProt; NX_Q99424; -. DR OpenTargets; ENSG00000168306; -. DR PharmGKB; PA24444; -. DR VEuPathDB; HostDB:ENSG00000168306; -. DR eggNOG; KOG0136; Eukaryota. DR GeneTree; ENSGT00940000160985; -. DR HOGENOM; CLU_014629_3_1_1; -. DR InParanoid; Q99424; -. DR OMA; CYYISVK; -. DR OrthoDB; 5777at2759; -. DR PhylomeDB; Q99424; -. DR TreeFam; TF300672; -. DR BioCyc; MetaCyc:HS09732-MONOMER; -. DR PathwayCommons; Q99424; -. DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol. DR Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR SignaLink; Q99424; -. DR BioGRID-ORCS; 8309; 7 hits in 1147 CRISPR screens. DR ChiTaRS; ACOX2; human. DR GenomeRNAi; 8309; -. DR Pharos; Q99424; Tbio. DR PRO; PR:Q99424; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q99424; Protein. DR Bgee; ENSG00000168306; Expressed in right lobe of liver and 136 other cell types or tissues. DR ExpressionAtlas; Q99424; baseline and differential. DR Genevisible; Q99424; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0033791; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity; IDA:UniProtKB. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB. DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB. DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IDA:UniProtKB. DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central. DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IBA:GO_Central. DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1. DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2. DR InterPro; IPR029320; Acyl-CoA_ox_N. DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf. DR InterPro; IPR012258; Acyl-CoA_oxidase. DR InterPro; IPR002655; Acyl-CoA_oxidase_C. DR InterPro; IPR036250; AcylCo_DH-like_C. DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf. DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1. DR PANTHER; PTHR10909:SF344; PEROXISOMAL ACYL-COENZYME A OXIDASE 2; 1. DR Pfam; PF01756; ACOX; 1. DR Pfam; PF14749; Acyl-CoA_ox_N; 1. DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1. DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2. DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disease variant; FAD; Fatty acid metabolism; KW Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein; KW Reference proteome. FT CHAIN 1..681 FT /note="Peroxisomal acyl-coenzyme A oxidase 2" FT /id="PRO_0000204681" FT MOTIF 679..681 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97562" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 13 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 66 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9QXD1" FT MOD_RES 137 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9QXD1" FT MOD_RES 453 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9QXD1" FT MOD_RES 561 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9QXD1" FT VARIANT 69..681 FT /note="Missing (in CBAS6; patient liver samples show FT absence of the protein; complete loss of fatty acid beta- FT oxidation activity)" FT /evidence="ECO:0000269|PubMed:27647924" FT /id="VAR_078764" FT VARIANT 225 FT /note="R -> W (in CBAS6; reduces fatty acid beta-oxidation FT activity; does not alter subcellular location; FT dbSNP:rs150832314)" FT /evidence="ECO:0000269|PubMed:27884763" FT /id="VAR_078765" SQ SEQUENCE 681 AA; 76827 MW; 7FAE9236FCBE6D4D CRC64; MGSPVHRVSL GDTWSRQMHP DIESERYMQS FDVERLTNIL DGGAQNTALR RKVESIIHSY PEFSCKDNYF MTQNERYKAA MRRAFHIRLI ARRLGWLEDG RELGYAYRAL SGDVALNIHR VFVRALRSLG SEEQIAKWDP LCKNIQIIAT YAQTELGHGT YLQGLETEAT YDAATQEFVI HSPTLTATKW WPGDLGRSAT HALVQAQLIC SGARRGMHAF IVPIRSLQDH TPLPGIIIGD IGPKMDFDQT DNGFLQLNHV RVPRENMLSR FAQVLPDGTY VKLGTAQSNY LPMVVVRVEL LSGEILPILQ KACVIAMRYS VIRRQSRLRP SDPEAKVLDY QTQQQKLFPQ LAISYAFHFL AVSLLEFFQH SYTAILNQDF SFLPELHALS TGMKAMMSEF CTQGAEMCRR ACGGHGYSKL SGLPSLVTKL SASCTYEGEN TVLYLQVARF LVKSYLQTQM SPGSTPQRSL SPSVAYLTAP DLARCPAQRA ADFLCPELYT TAWAHVAVRL IKDSVQHLQT LTQSGADQHE AWNQTTVIHL QAAKVHCYYV TVKGFTEALE KLENEPAIQQ VLKRLCDLHA IHGILTNSGD FLHDAFLSGA QVDMARTAYL DLLRLIRKDA ILLTDAFDFT DQCLNSALGC YDGNVYERLF QWAQKSPTNT QENPAYEEYI RPLLQSWRSK L //