CPT1B_HUMAN
ID CPT1B_HUMAN Reviewed; 772 AA.
AC Q92523; B7Z4U4; B7Z5T8; E9PCP2; Q13389; Q99655; Q9BY90;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, muscle isoform;
DE Short=CPT1-M;
DE EC=2.3.1.21 {ECO:0000269|PubMed:9344464};
DE AltName: Full=Carnitine O-palmitoyltransferase I, muscle isoform;
DE Short=CPT I;
DE Short=CPTI-M;
DE AltName: Full=Carnitine palmitoyltransferase 1B;
DE AltName: Full=Carnitine palmitoyltransferase I-like protein;
GN Name=CPT1B; Synonyms=KIAA1670;
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] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=8679700; DOI=10.1016/0167-4781(96)00069-3;
RA Yamazaki N., Shinohara Y., Shima A., Yamanaka Y., Terada H.;
RT "Isolation and characterization of cDNA and genomic clones encoding human
RT muscle type carnitine palmitoyltransferase I.";
RL Biochim. Biophys. Acta 1307:157-161(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9344464; DOI=10.1006/abbi.1997.0314;
RA Zhu H., Shi J., de Vries Y., Arvidson D.N., Cregg J.M., Woldegiorgis G.;
RT "Functional studies of yeast-expressed human heart muscle carnitine
RT palmitoyltransferase I.";
RL Arch. Biochem. Biophys. 347:53-61(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=9070950; DOI=10.1006/geno.1996.4539;
RA Britton C.H., Mackey D.W., Esser V., Foster D.W., Burns D.K., Yarnall D.P.,
RA Froguel P., McGarry J.D.;
RT "Fine chromosome mapping of the genes for human liver and muscle carnitine
RT palmitoyltransferase I (CPT1A and CPT1B).";
RL Genomics 40:209-211(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=9199240; DOI=10.1016/s0167-4781(97)00037-7;
RA van der Leij F.R., Takens J., van der Veen A.Y., Terpstra P.,
RA Kuipers J.R.G.;
RT "Localization and intron usage analysis of the human CPT1B gene for muscle
RT type carnitine palmitoyltransferase I.";
RL Biochim. Biophys. Acta 1352:123-128(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9224698; DOI=10.1016/s0014-5793(97)00561-9;
RA Yamazaki N., Yamanaka Y., Hashimoto Y., Shinohara Y., Shima A., Terada H.;
RT "Structural features of the gene encoding human muscle type carnitine
RT palmitoyltransferase I.";
RL FEBS Lett. 409:401-406(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LYS-531.
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22 by
RT expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP LYS-531.
RC TISSUE=Heart, and Tongue;
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 [8]
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., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., 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., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., 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., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:12661, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:17490, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=2.3.1.21;
CC Evidence={ECO:0000269|PubMed:9344464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12662;
CC Evidence={ECO:0000305|PubMed:9344464};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=666 uM for carnitine {ECO:0000269|PubMed:9344464};
CC KM=42 uM for palmitoyl-CoA {ECO:0000269|PubMed:9344464};
CC Vmax=1.3 nmol/min/mg enzyme toward carnitine
CC {ECO:0000269|PubMed:9344464};
CC Vmax=1.44 nmol/min/mg enzyme toward palmitoyl-CoA
CC {ECO:0000269|PubMed:9344464};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- INTERACTION:
CC Q92523; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-10278486, EBI-17231387;
CC Q92523; Q53QW1: TEX44; NbExp=6; IntAct=EBI-10278486, EBI-10278496;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:9344464}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q92523-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92523-2; Sequence=VSP_034246, VSP_034247;
CC Name=3;
CC IsoId=Q92523-3; Sequence=VSP_043184;
CC Name=4;
CC IsoId=Q92523-4; Sequence=VSP_044451;
CC -!- TISSUE SPECIFICITY: Strong expression in heart and skeletal muscle. No
CC expression in liver and kidney.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the CHKB protein from a non-overlapping reading frame.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB33340.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D87812; BAA13461.1; -; mRNA.
DR EMBL; U66828; AAB40651.1; -; mRNA.
DR EMBL; U62733; AAC51122.1; -; mRNA.
DR EMBL; Y08682; CAA69938.1; -; mRNA.
DR EMBL; Y08683; CAA69939.1; -; mRNA.
DR EMBL; AB003286; BAA21492.1; -; Genomic_DNA.
DR EMBL; AB051457; BAB33340.1; ALT_INIT; mRNA.
DR EMBL; AK297866; BAH12680.1; -; mRNA.
DR EMBL; AK299395; BAH13024.1; -; mRNA.
DR EMBL; U62317; AAB03343.1; -; Genomic_DNA.
DR CCDS; CCDS14098.1; -. [Q92523-1]
DR CCDS; CCDS46734.1; -. [Q92523-3]
DR PIR; G02860; G02860.
DR RefSeq; NP_001138606.1; NM_001145134.1. [Q92523-3]
DR RefSeq; NP_001138607.1; NM_001145135.1. [Q92523-1]
DR RefSeq; NP_001138609.1; NM_001145137.1. [Q92523-1]
DR RefSeq; NP_004368.1; NM_004377.3. [Q92523-1]
DR RefSeq; NP_689451.1; NM_152245.2. [Q92523-1]
DR RefSeq; NP_689452.1; NM_152246.2. [Q92523-1]
DR AlphaFoldDB; Q92523; -.
DR SMR; Q92523; -.
DR BioGRID; 107766; 4.
DR IntAct; Q92523; 2.
DR STRING; 9606.ENSP00000379011; -.
DR BindingDB; Q92523; -.
DR ChEMBL; CHEMBL2216739; -.
DR SwissLipids; SLP:000001052; -.
DR iPTMnet; Q92523; -.
DR PhosphoSitePlus; Q92523; -.
DR BioMuta; CPT1B; -.
DR DMDM; 2493497; -.
DR EPD; Q92523; -.
DR jPOST; Q92523; -.
DR MassIVE; Q92523; -.
DR MaxQB; Q92523; -.
DR PaxDb; Q92523; -.
DR PeptideAtlas; Q92523; -.
DR PRIDE; Q92523; -.
DR ProteomicsDB; 19483; -.
DR ProteomicsDB; 75282; -. [Q92523-1]
DR ProteomicsDB; 75283; -. [Q92523-2]
DR ProteomicsDB; 75284; -. [Q92523-3]
DR Antibodypedia; 28758; 426 antibodies from 35 providers.
DR DNASU; 1375; -.
DR Ensembl; ENST00000312108.12; ENSP00000312189.8; ENSG00000205560.13. [Q92523-1]
DR Ensembl; ENST00000360719.6; ENSP00000353945.2; ENSG00000205560.13. [Q92523-1]
DR Ensembl; ENST00000395650.6; ENSP00000379011.2; ENSG00000205560.13. [Q92523-1]
DR Ensembl; ENST00000405237.7; ENSP00000385486.3; ENSG00000205560.13. [Q92523-1]
DR Ensembl; ENST00000457250.5; ENSP00000409342.1; ENSG00000205560.13. [Q92523-3]
DR GeneID; 1375; -.
DR KEGG; hsa:1375; -.
DR MANE-Select; ENST00000312108.12; ENSP00000312189.8; NM_152246.3; NP_689452.1.
DR UCSC; uc003bmk.5; human. [Q92523-1]
DR CTD; 1375; -.
DR DisGeNET; 1375; -.
DR GeneCards; CPT1B; -.
DR HGNC; HGNC:2329; CPT1B.
DR HPA; ENSG00000205560; Group enriched (heart muscle, skeletal muscle, testis, tongue).
DR MIM; 601987; gene.
DR neXtProt; NX_Q92523; -.
DR OpenTargets; ENSG00000205560; -.
DR PharmGKB; PA26848; -.
DR VEuPathDB; HostDB:ENSG00000205560; -.
DR eggNOG; KOG3716; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; Q92523; -.
DR OMA; GLVCCIQ; -.
DR PhylomeDB; Q92523; -.
DR TreeFam; TF313836; -.
DR BioCyc; MetaCyc:MON66-34409; -.
DR BRENDA; 2.3.1.21; 2681.
DR PathwayCommons; Q92523; -.
DR Reactome; R-HSA-200425; Carnitine metabolism.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR SABIO-RK; Q92523; -.
DR SignaLink; Q92523; -.
DR SIGNOR; Q92523; -.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 1375; 14 hits in 1073 CRISPR screens.
DR GenomeRNAi; 1375; -.
DR Pharos; Q92523; Tchem.
DR PRO; PR:Q92523; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q92523; protein.
DR Bgee; ENSG00000205560; Expressed in apex of heart and 94 other tissues.
DR ExpressionAtlas; Q92523; baseline and differential.
DR Genevisible; Q92523; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IMP:UniProtKB.
DR GO; GO:0009437; P:carnitine metabolic process; IBA:GO_Central.
DR GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:ProtInc.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0015909; P:long-chain fatty acid transport; IBA:GO_Central.
DR GO; GO:0009637; P:response to blue light; ISS:UniProtKB.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR InterPro; IPR032476; CPT_N.
DR PANTHER; PTHR22589; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF16484; CPT_N; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Fatty acid metabolism;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..772
FT /note="Carnitine O-palmitoyltransferase 1, muscle isoform"
FT /id="PRO_0000210162"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..102
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT BINDING 555..567
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 589
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT BINDING 602
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT VAR_SEQ 154..187
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043184"
FT VAR_SEQ 355..435
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044451"
FT VAR_SEQ 581
FT /note="D -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11258795"
FT /id="VSP_034246"
FT VAR_SEQ 582..772
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11258795"
FT /id="VSP_034247"
FT VARIANT 66
FT /note="I -> V (in dbSNP:rs3213445)"
FT /id="VAR_020029"
FT VARIANT 320
FT /note="G -> D (in dbSNP:rs2269383)"
FT /id="VAR_021854"
FT VARIANT 427
FT /note="S -> C (in dbSNP:rs8142477)"
FT /id="VAR_024188"
FT VARIANT 531
FT /note="E -> K (in dbSNP:rs470117)"
FT /evidence="ECO:0000269|PubMed:11258795,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_011739"
FT VARIANT 664
FT /note="S -> Y (in dbSNP:rs1804702)"
FT /id="VAR_011740"
FT CONFLICT 75
FT /note="C -> S (in Ref. 7; BAH13024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 87801 MW; F7E3ED40643DFC81 CRC64;
MAEAHQAVAF QFTVTPDGVD FRLSREALKH VYLSGINSWK KRLIRIKNGI LRGVYPGSPT
SWLVVIMATV GSSFCNVDIS LGLVSCIQRC LPQGCGPYQT PQTRALLSMA IFSTGVWVTG
IFFFRQTLKL LLCYHGWMFE MHGKTSNLTR IWAMCIRLLS SRHPMLYSFQ TSLPKLPVPR
VSATIQRYLE SVRPLLDDEE YYRMELLAKE FQDKTAPRLQ KYLVLKSWWA SNYVSDWWEE
YIYLRGRSPL MVNSNYYVMD LVLIKNTDVQ AARLGNIIHA MIMYRRKLDR EEIKPVMALG
IVPMCSYQME RMFNTTRIPG KDTDVLQHLS DSRHVAVYHK GRFFKLWLYE GARLLKPQDL
EMQFQRILDD PSPPQPGEEK LAALTAGGRV EWAQARQAFF SSGKNKAALE AIERAAFFVA
LDEESYSYDP EDEASLSLYG KALLHGNCYN RWFDKSFTLI SFKNGQLGLN AEHAWADAPI
IGHLWEFVLG TDSFHLGYTE TGHCLGKPNP ALAPPTRLQW DIPKQCQAVI ESSYQVAKAL
ADDVELYCFQ FLPFGKGLIK KCRTSPDAFV QIALQLAHFR DRGKFCLTYE ASMTRMFREG
RTETVRSCTS ESTAFVQAMM EGSHTKADLR DLFQKAAKKH QNMYRLAMTG AGIDRHLFCL
YLVSKYLGVS SPFLAEVLSE PWRLSTSQIP QSQIRMFDPE QHPNHLGAGG GFGPVADDGY
GVSYMIAGEN TIFFHISSKF SSSETNAQRF GNHIRKALLD IADLFQVPKA YS
