ID CP8B1_HUMAN Reviewed; 501 AA. AC Q9UNU6; B2RCY3; O75958; Q6NWT2; Q6NWT3; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 2. DT 24-JAN-2024, entry version 179. DE RecName: Full=7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase; DE EC=1.14.14.139 {ECO:0000269|PubMed:10051404}; DE AltName: Full=7-alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase; DE AltName: Full=CYPVIIIB1; DE AltName: Full=Cytochrome P450 8B1; DE AltName: Full=Sterol 12-alpha-hydroxylase; GN Name=CYP8B1 {ECO:0000303|PubMed:10051404, ECO:0000312|HGNC:HGNC:2653}; GN Synonyms=CYP12; 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 [GENOMIC DNA / MRNA], VARIANTS PRO-88 AND HIS-234, RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=10051404; DOI=10.1006/geno.1998.5606; RA Gaafvels M., Olin M., Chowdhary B.P., Raudsepp T., Andersson U., RA Persson B., Jansson M., Bjoerkhem I., Eggertsen G.; RT "Structure and chromosomal assignment of the sterol 12alpha-hydroxylase RT gene (CYP8B1) in human and mouse: eukaryotic cytochrome P-450 gene devoid RT of introns."; RL Genomics 56:184-196(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-88. RC TISSUE=Liver; 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-88. 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY RP 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). CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in primary bile acid CC biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4- CC cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis CC (PubMed:10051404). Controls biliary balance of cholic acid and CC chenodeoxycholic acid, ultimately regulating the intestinal absorption CC of dietary lipids (By similarity). Mechanistically, uses molecular CC oxygen inserting one oxygen atom into a substrate, and reducing the CC second into a water molecule, with two electrons provided by NADPH via CC cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase) (By CC similarity). {ECO:0000250|UniProtKB:O02766, CC ECO:0000250|UniProtKB:O88962, ECO:0000269|PubMed:10051404}. CC -!- CATALYTIC ACTIVITY: CC Reaction=7alpha-hydroxycholest-4-en-3-one + O2 + reduced CC [NADPH--hemoprotein reductase] = 7alpha,12alpha-dihydroxycholest-4- CC en-3-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; CC Xref=Rhea:RHEA:46752, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17899, ChEBI:CHEBI:28477, ChEBI:CHEBI:57618, CC ChEBI:CHEBI:58210; EC=1.14.14.139; CC Evidence={ECO:0000269|PubMed:10051404}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46753; CC Evidence={ECO:0000305|PubMed:10051404}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5beta-cholestane-3alpha,7alpha-diol + O2 + reduced CC [NADPH--hemoprotein reductase] = 5beta-cholestane- CC 3alpha,7alpha,12alpha-triol + H(+) + H2O + oxidized CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:15261, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16496, CC ChEBI:CHEBI:28047, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; CC EC=1.14.14.139; Evidence={ECO:0000269|PubMed:10051404}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15262; CC Evidence={ECO:0000305|PubMed:10051404}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chenodeoxycholate + O2 + reduced [NADPH--hemoprotein CC reductase] = cholate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:65700, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29747, ChEBI:CHEBI:36234, ChEBI:CHEBI:57618, CC ChEBI:CHEBI:58210; EC=1.14.14.139; CC Evidence={ECO:0000269|PubMed:10051404}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65701; CC Evidence={ECO:0000305|PubMed:10051404}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:O02766}; CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis. CC {ECO:0000250|UniProtKB:O88962}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:O02766}; Single-pass membrane protein CC {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:O02766}; CC Single-pass membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:10051404}. CC -!- SIMILARITY: Belongs to the cytochrome P450 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; AF090318; AAC63037.1; -; mRNA. DR EMBL; AF090320; AAD19877.1; -; Genomic_DNA. DR EMBL; AK315330; BAG37730.1; -; mRNA. DR EMBL; AC099329; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC067434; AAH67434.1; -; mRNA. DR EMBL; BC067441; AAH67441.1; -; mRNA. DR EMBL; BC067442; AAH67442.1; -; mRNA. DR EMBL; BC067444; AAH67444.1; -; mRNA. DR CCDS; CCDS2707.1; -. DR RefSeq; NP_004382.2; NM_004391.2. DR PDB; 7LYX; X-ray; 2.60 A; A=26-501. DR PDB; 8EOH; X-ray; 2.65 A; A=26-501. DR PDBsum; 7LYX; -. DR PDBsum; 8EOH; -. DR AlphaFoldDB; Q9UNU6; -. DR SMR; Q9UNU6; -. DR BioGRID; 107954; 11. DR IntAct; Q9UNU6; 5. DR STRING; 9606.ENSP00000318867; -. DR ChEMBL; CHEMBL4523494; -. DR SwissLipids; SLP:000001319; -. DR iPTMnet; Q9UNU6; -. DR PhosphoSitePlus; Q9UNU6; -. DR BioMuta; CYP8B1; -. DR DMDM; 308153428; -. DR MassIVE; Q9UNU6; -. DR PaxDb; 9606-ENSP00000318867; -. DR PeptideAtlas; Q9UNU6; -. DR ProteomicsDB; 85332; -. DR Antibodypedia; 53027; 250 antibodies from 26 providers. DR DNASU; 1582; -. DR Ensembl; ENST00000316161.6; ENSP00000318867.4; ENSG00000180432.6. DR GeneID; 1582; -. DR KEGG; hsa:1582; -. DR MANE-Select; ENST00000316161.6; ENSP00000318867.4; NM_004391.3; NP_004382.2. DR UCSC; uc003cmh.4; human. DR AGR; HGNC:2653; -. DR CTD; 1582; -. DR DisGeNET; 1582; -. DR GeneCards; CYP8B1; -. DR HGNC; HGNC:2653; CYP8B1. DR HPA; ENSG00000180432; Tissue enriched (liver). DR MIM; 602172; gene. DR neXtProt; NX_Q9UNU6; -. DR OpenTargets; ENSG00000180432; -. DR VEuPathDB; HostDB:ENSG00000180432; -. DR eggNOG; KOG0684; Eukaryota. DR GeneTree; ENSGT00940000153709; -. DR HOGENOM; CLU_018012_1_3_1; -. DR InParanoid; Q9UNU6; -. DR OMA; MRDRFMF; -. DR OrthoDB; 1537669at2759; -. DR PhylomeDB; Q9UNU6; -. DR TreeFam; TF105090; -. DR PathwayCommons; Q9UNU6; -. DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol. DR Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol. DR Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol. DR Reactome; R-HSA-197264; Nicotinamide salvaging. DR Reactome; R-HSA-211979; Eicosanoids. DR Reactome; R-HSA-211994; Sterols are 12-hydroxylated by CYP8B1. DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX). DR SignaLink; Q9UNU6; -. DR UniPathway; UPA00221; -. DR BioGRID-ORCS; 1582; 13 hits in 1144 CRISPR screens. DR GeneWiki; CYP8B1; -. DR GenomeRNAi; 1582; -. DR Pharos; Q9UNU6; Tchem. DR PRO; PR:Q9UNU6; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9UNU6; Protein. DR Bgee; ENSG00000180432; Expressed in right lobe of liver and 55 other cell types or tissues. DR ExpressionAtlas; Q9UNU6; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0033779; F:5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase activity; IEA:RHEA. DR GO; GO:0033778; F:7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase activity; TAS:Reactome. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0019825; F:oxygen binding; TAS:ProtInc. DR GO; GO:0008397; F:sterol 12-alpha-hydroxylase activity; ISS:UniProtKB. DR GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB. DR GO; GO:0038183; P:bile acid signaling pathway; IEA:Ensembl. DR GO; GO:0045797; P:positive regulation of intestinal cholesterol absorption; ISS:UniProtKB. DR GO; GO:0070723; P:response to cholesterol; IEA:Ensembl. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0016125; P:sterol metabolic process; TAS:Reactome. DR CDD; cd20633; Cyp8B1; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR024204; Cyt_P450_CYP7A1-type. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR InterPro; IPR036396; Cyt_P450_sf. DR InterPro; IPR030686; Cytochrome_CYP8B1. DR PANTHER; PTHR24306; -; 1. DR PANTHER; PTHR24306:SF0; 7-ALPHA-HYDROXYCHOLEST-4-EN-3-ONE 12-ALPHA-HYDROXYLASE; 1. DR Pfam; PF00067; p450; 1. DR PIRSF; PIRSF500627; Cytochrome_CYP8B1; 1. DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1. DR PRINTS; PR00465; EP450IV. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR Genevisible; Q9UNU6; HS. PE 1: Evidence at protein level; KW 3D-structure; Endoplasmic reticulum; Heme; Iron; Lipid biosynthesis; KW Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase; KW Oxidoreductase; Phosphoprotein; Reference proteome; Steroid biosynthesis; KW Transmembrane; Transmembrane helix. FT CHAIN 1..501 FT /note="7-alpha-hydroxycholest-4-en-3-one 12-alpha- FT hydroxylase" FT /id="PRO_0000051913" FT TRANSMEM 1..21 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 440 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" FT MOD_RES 326 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 88 FT /note="S -> P (in dbSNP:rs9865715)" FT /evidence="ECO:0000269|PubMed:10051404, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_055102" FT VARIANT 234 FT /note="R -> H (in dbSNP:rs199955644)" FT /evidence="ECO:0000269|PubMed:10051404" FT /id="VAR_010381" FT VARIANT 238 FT /note="K -> R (in dbSNP:rs35764459)" FT /id="VAR_055103" FT VARIANT 357 FT /note="L -> F (in dbSNP:rs35637877)" FT /id="VAR_055104" FT CONFLICT 24 FT /note="M -> I (in Ref. 2; BAG37730)" FT /evidence="ECO:0000305" FT CONFLICT 60 FT /note="M -> V (in Ref. 4; AAH67444)" FT /evidence="ECO:0000305" FT CONFLICT 454 FT /note="I -> T (in Ref. 4; AAH67434/AAH67441)" FT /evidence="ECO:0000305" FT CONFLICT 468 FT /note="P -> L (in Ref. 4; AAH67444)" FT /evidence="ECO:0000305" FT TURN 41..45 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 46..51 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 53..64 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 66..72 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 86..90 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 100..111 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 119..130 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 133..153 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 165..168 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 169..186 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 192..217 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 223..239 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 253..264 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 269..284 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 287..299 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 302..313 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 338..351 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 356..362 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 364..367 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 373..376 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 381..384 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 386..389 FT /evidence="ECO:0007829|PDB:7LYX" FT TURN 390..392 FT /evidence="ECO:0007829|PDB:7LYX" FT TURN 394..396 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 397..399 FT /evidence="ECO:0007829|PDB:7LYX" FT TURN 405..408 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 443..460 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 461..466 FT /evidence="ECO:0007829|PDB:7LYX" FT HELIX 477..479 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 481..484 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:7LYX" FT STRAND 492..497 FT /evidence="ECO:0007829|PDB:7LYX" SQ SEQUENCE 501 AA; 58068 MW; 1B97698E8453E51A CRC64; MVLWGPVLGA LLVVIAGYLC LPGMLRQRRP WEPPLDKGTV PWLGHAMAFR KNMFEFLKRM RTKHGDVFTV QLGGQYFTFV MDPLSFGSIL KDTQRKLDFG QYAKKLVLKV FGYRSVQGDH EMIHSASTKH LRGDGLKDLN ETMLDSLSFV MLTSKGWSLD ASCWHEDSLF RFCYYILFTA GYLSLFGYTK DKEQDLLQAG ELFMEFRKFD LLFPRFVYSL LWPREWLEVG RLQRLFHKML SVSHSQEKEG ISNWLGNMLQ FLREQGVPSA MQDKFNFMML WASQGNTGPT SFWALLYLLK HPEAIRAVRE EATQVLGEAR LETKQSFAFK LGALQHTPVL DSVVEETLRL RAAPTLLRLV HEDYTLKMSS GQEYLFRHGD ILALFPYLSV HMDPDIHPEP TVFKYDRFLN PNGSRKVDFF KTGKKIHHYT MPWGSGVSIC PGRFFALSEV KLFILLMVTH FDLELVDPDT PLPHVDPQRW GFGTMQPSHD VRFRYRLHPT E //