CPT1A_RAT
ID CPT1A_RAT Reviewed; 773 AA.
AC P32198; P97780; Q6IMZ4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, liver isoform;
DE Short=CPT1-L;
DE EC=2.3.1.21 {ECO:0000269|PubMed:16908527, ECO:0000269|PubMed:18349115, ECO:0000269|PubMed:21990363};
DE AltName: Full=Carnitine O-palmitoyltransferase I, liver isoform;
DE Short=CPT I;
DE Short=CPTI-L;
DE AltName: Full=Carnitine palmitoyltransferase 1A;
GN Name=Cpt1a; Synonyms=Cpt-1, Cpt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8449948; DOI=10.1016/s0021-9258(18)53392-5;
RA Esser V., Britton C.H., Weis B.C., Foster D.W., McGarry J.D.;
RT "Cloning, sequencing, and expression of a cDNA encoding rat liver carnitine
RT palmitoyltransferase I. Direct evidence that a single polypeptide is
RT involved in inhibitor interaction and catalytic function.";
RL J. Biol. Chem. 268:5817-5822(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9136891; DOI=10.1021/bi962875p;
RA de Vries Y., Arvidson D.N., Waterham H.R., Cregg J.M., Woldegiorgis G.;
RT "Functional characterization of mitochondrial carnitine
RT palmitoyltransferases I and II expressed in the yeast Pichia pastoris.";
RL Biochemistry 36:5285-5292(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [4]
RP PROTEIN SEQUENCE OF 2-22; 272-283; 585-595 AND 599-606, ACETYLATION AT
RP ALA-2, NITRATION AT TYR-282 AND TYR-589, PHOSPHORYLATION AT THR-588;
RP THR-604; SER-741 AND SER-747, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=17478130; DOI=10.1016/j.bbapap.2007.03.012;
RA Distler A.M., Kerner J., Hoppel C.L.;
RT "Post-translational modifications of rat liver mitochondrial outer membrane
RT proteins identified by mass spectrometry.";
RL Biochim. Biophys. Acta 1774:628-636(2007).
RN [5]
RP PROTEIN SEQUENCE OF 4-21; 259-276; 361-379; 529-543 AND 696-717.
RC TISSUE=Liver;
RX PubMed=8348957; DOI=10.1016/0014-5793(93)81007-m;
RA Kolodziej M.P., Zammit V.A.;
RT "Mature carnitine palmitoyltransferase I retains the N-terminus of the
RT nascent protein in rat liver.";
RL FEBS Lett. 327:294-296(1993).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=8449947; DOI=10.1016/s0021-9258(18)53391-3;
RA Esser V., Kuwajima M., Britton C.H., Krishnan K., Foster D.W.,
RA McGarry J.D.;
RT "Inhibitors of mitochondrial carnitine palmitoyltransferase I limit the
RT action of proteases on the enzyme. Isolation and partial amino acid
RT analysis of a truncated form of the rat liver isozyme.";
RL J. Biol. Chem. 268:5810-5816(1993).
RN [7]
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=8636126; DOI=10.1074/jbc.271.12.6972;
RA Esser V., Brown N.F., Cowan A.T., Foster D.W., McGarry J.D.;
RT "Expression of a cDNA isolated from rat brown adipose tissue and heart
RT identifies the product as the muscle isoform of carnitine
RT palmitoyltransferase I (M-CPT I). M-CPT I is the predominant CPT I isoform
RT expressed in both white (epididymal) and brown adipocytes.";
RL J. Biol. Chem. 271:6972-6977(1996).
RN [8]
RP TOPOLOGY.
RX PubMed=9169604; DOI=10.1042/bj3230711;
RA Fraser F., Corstorphine C.G., Zammit V.A.;
RT "Topology of carnitine palmitoyltransferase I in the mitochondrial outer
RT membrane.";
RL Biochem. J. 323:711-718(1997).
RN [9]
RP MUTAGENESIS OF ALA-381 AND HIS-473, AND 3D-STRUCTURE MODELING.
RX PubMed=11553629; DOI=10.1074/jbc.m106920200;
RA Morillas M., Gomez-Puertas P., Roca R., Serra D., Asins G., Valencia A.,
RA Hegardt F.G.;
RT "Structural model of the catalytic core of carnitine palmitoyltransferase I
RT and carnitine octanoyltransferase (COT): mutation of CPT I histidine 473
RT and alanine 381 and COT alanine 238 impairs the catalytic activity.";
RL J. Biol. Chem. 276:45001-45008(2001).
RN [10]
RP MUTAGENESIS OF MET-593 AND CYS-608.
RX PubMed=12499375; DOI=10.1074/jbc.m209999200;
RA Morillas M., Gomez-Puertas P., Bentebibel A., Selles E., Casals N.,
RA Valencia A., Hegardt F.G., Asins G., Serra D.;
RT "Identification of conserved amino acid residues in rat liver carnitine
RT palmitoyltransferase I critical for malonyl-CoA inhibition. Mutation of
RT methionine 593 abolishes malonyl-CoA inhibition.";
RL J. Biol. Chem. 278:9058-9063(2003).
RN [11]
RP MUTAGENESIS OF ASP-477; LYS-560; GLU-590; SER-685; THR-686 AND SER-687, AND
RP 3D-STRUCTURE MODELING.
RX PubMed=14711372; DOI=10.1042/bj20031373;
RA Morillas M., Lopez-Vinas E., Valencia A., Serra D., Gomez-Puertas P.,
RA Hegardt F.G., Asins G.;
RT "Structural model of carnitine palmitoyltransferase I based on the
RT carnitine acetyltransferase crystal.";
RL Biochem. J. 379:777-784(2004).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16908527; DOI=10.1074/jbc.m600843200;
RA Borthwick K., Jackson V.N., Price N.T., Zammit V.A.;
RT "The mitochondrial intermembrane loop region of rat carnitine
RT palmitoyltransferase 1A is a major determinant of its malonyl-CoA
RT sensitivity.";
RL J. Biol. Chem. 281:32946-32952(2006).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18349115; DOI=10.1152/ajpendo.00497.2007;
RA Stefanovic-Racic M., Perdomo G., Mantell B.S., Sipula I.J., Brown N.F.,
RA O'Doherty R.M.;
RT "A moderate increase in carnitine palmitoyltransferase 1a activity is
RT sufficient to substantially reduce hepatic triglyceride levels.";
RL Am. J. Physiol. 294:E969-E977(2008).
RN [14]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19136561; DOI=10.1074/jbc.m808487200;
RA Jenei Z.A., Borthwick K., Zammit V.A., Dixon A.M.;
RT "Self-association of transmembrane domain 2 (TM2), but not TM1, in
RT carnitine palmitoyltransferase 1A: role of GXXXG(A) motifs.";
RL J. Biol. Chem. 284:6988-6997(2009).
RN [15]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH ACSL1 AND VDAC1;
RP IDENTIFICATION IN COMPLEXES WITH ACSL1; VDAC2 AND VDAC3, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=21622568; DOI=10.1074/jbc.m111.228692;
RA Lee K., Kerner J., Hoppel C.L.;
RT "Mitochondrial carnitine palmitoyltransferase 1a (CPT1a) is part of an
RT outer membrane fatty acid transfer complex.";
RL J. Biol. Chem. 286:25655-25662(2011).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, AND MUTAGENESIS
RP OF GLU-3; ALA-9 AND GLY-18.
RX PubMed=21990363; DOI=10.1074/jbc.m111.306951;
RA Rao J.N., Warren G.Z., Estolt-Povedano S., Zammit V.A., Ulmer T.S.;
RT "An environment-dependent structural switch underlies the regulation of
RT carnitine palmitoyltransferase 1A.";
RL J. Biol. Chem. 286:42545-42554(2011).
CC -!- FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty
CC acid-CoA conjugates onto carnitine, an essential step for the
CC mitochondrial uptake of long-chain fatty acids and their subsequent
CC beta-oxidation in the mitochondrion (PubMed:16908527, PubMed:21990363).
CC Plays an important role in hepatic triglyceride metabolism
CC (PubMed:18349115). {ECO:0000269|PubMed:16908527,
CC ECO:0000269|PubMed:18349115, ECO:0000269|PubMed:21990363}.
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:16908527, ECO:0000269|PubMed:18349115,
CC ECO:0000269|PubMed:21990363};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12662;
CC Evidence={ECO:0000305|PubMed:16908527};
CC -!- ACTIVITY REGULATION: Inhibited by malonyl-CoA.
CC {ECO:0000269|PubMed:16908527, ECO:0000269|PubMed:21990363}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=184.2 uM for carnitine {ECO:0000269|PubMed:16908527};
CC KM=46.5 uM for palmitoyl-CoA {ECO:0000269|PubMed:16908527};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Homohexamer and homotrimer (PubMed:19136561). Identified in a
CC complex that contains at least CPT1A, ACSL1 and VDAC1
CC (PubMed:21622568). Also identified in complexes with ACSL1 and VDAC2
CC and VDAC3. {ECO:0000269|PubMed:19136561, ECO:0000269|PubMed:21622568}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:16908527, ECO:0000269|PubMed:19136561,
CC ECO:0000269|PubMed:21622568}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Liver and kidney. {ECO:0000269|PubMed:8636126}.
CC -!- DOMAIN: A conformation change in the N-terminal region spanning the
CC first 42 residues plays an important role in the regulation of enzyme
CC activity by malonyl-CoA. {ECO:0000269|PubMed:21990363}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; L07736; AAA40876.1; -; mRNA.
DR EMBL; U88294; AAB48046.1; -; mRNA.
DR EMBL; BC072522; AAH72522.1; -; mRNA.
DR PIR; A46627; A46627.
DR RefSeq; NP_113747.2; NM_031559.2.
DR RefSeq; XP_006230757.1; XM_006230695.2.
DR RefSeq; XP_017444326.1; XM_017588837.1.
DR AlphaFoldDB; P32198; -.
DR SMR; P32198; -.
DR CORUM; P32198; -.
DR IntAct; P32198; 2.
DR MINT; P32198; -.
DR STRING; 10116.ENSRNOP00000019652; -.
DR BindingDB; P32198; -.
DR ChEMBL; CHEMBL3858; -.
DR DrugCentral; P32198; -.
DR SwissLipids; SLP:000000777; -.
DR iPTMnet; P32198; -.
DR PhosphoSitePlus; P32198; -.
DR jPOST; P32198; -.
DR PaxDb; P32198; -.
DR PRIDE; P32198; -.
DR Ensembl; ENSRNOT00000019652; ENSRNOP00000019652; ENSRNOG00000014254.
DR GeneID; 25757; -.
DR KEGG; rno:25757; -.
DR UCSC; RGD:2396; rat.
DR CTD; 1374; -.
DR RGD; 2396; Cpt1a.
DR eggNOG; KOG3716; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; P32198; -.
DR OMA; PSSWFIV; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; P32198; -.
DR TreeFam; TF313836; -.
DR BioCyc; MetaCyc:MON-14439; -.
DR BRENDA; 2.3.1.21; 5301.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
DR SABIO-RK; P32198; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:P32198; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014254; Expressed in liver and 19 other tissues.
DR Genevisible; P32198; RN.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:1990698; F:palmitoleoyltransferase activity; ISO:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; IDA:UniProtKB.
DR GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
DR GO; GO:0042755; P:eating behavior; IMP:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEP:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEP:RGD.
DR GO; GO:0006006; P:glucose metabolic process; IMP:RGD.
DR GO; GO:0010876; P:lipid localization; IEP:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:RGD.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; TAS:RGD.
DR GO; GO:0046320; P:regulation of fatty acid oxidation; IMP:RGD.
DR GO; GO:0050796; P:regulation of insulin secretion; IMP:RGD.
DR GO; GO:0010883; P:regulation of lipid storage; IEP:RGD.
DR GO; GO:0043279; P:response to alkaloid; IEP:RGD.
DR GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:1904772; P:response to tetrachloromethane; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:RGD.
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 Acetylation; Acyltransferase; Direct protein sequencing;
KW Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nitration; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17478130"
FT CHAIN 2..773
FT /note="Carnitine O-palmitoyltransferase 1, liver isoform"
FT /id="PRO_0000210161"
FT TOPO_DOM 2..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..773
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 282
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 589
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 604
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MUTAGEN 3
FT /note="E->R: Decreases susceptibility to inhibition by
FT malonyl-CoA."
FT /evidence="ECO:0000269|PubMed:21990363"
FT MUTAGEN 9
FT /note="A->G: Increases susceptibility to inhibition by
FT malonyl-CoA."
FT /evidence="ECO:0000269|PubMed:21990363"
FT MUTAGEN 18
FT /note="G->A: Increases susceptibility to inhibition by
FT malonyl-CoA."
FT /evidence="ECO:0000269|PubMed:21990363"
FT MUTAGEN 381
FT /note="A->D: Reduces activity by 86%. No effect on
FT inhibition by malonyl-coenzyme A."
FT /evidence="ECO:0000269|PubMed:11553629"
FT MUTAGEN 473
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11553629"
FT MUTAGEN 477
FT /note="D->A: Reduces activity by 98%."
FT /evidence="ECO:0000269|PubMed:14711372"
FT MUTAGEN 560
FT /note="K->A: Reduces activity by 50%."
FT /evidence="ECO:0000269|PubMed:14711372"
FT MUTAGEN 567
FT /note="D->A: Reduces activity by 97%."
FT MUTAGEN 590
FT /note="E->D: Reduces activity by over 60%."
FT /evidence="ECO:0000269|PubMed:14711372"
FT MUTAGEN 593
FT /note="M->A,E,S: Almost abolishes inhibition by malonyl-
FT coenzyme A."
FT /evidence="ECO:0000269|PubMed:12499375"
FT MUTAGEN 608
FT /note="C->A: Slightly lowers inhibition by malonyl-coenzyme
FT A."
FT /evidence="ECO:0000269|PubMed:12499375"
FT MUTAGEN 685
FT /note="S->A: Reduces activity by 50%."
FT /evidence="ECO:0000269|PubMed:14711372"
FT MUTAGEN 686
FT /note="T->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14711372"
FT MUTAGEN 687
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14711372"
FT CONFLICT 266
FT /note="H -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 374..375
FT /note="QP -> NG (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="V -> I (in Ref. 1; AAA40876)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="D -> Y (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="C -> R (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 88125 MW; 8C15594D45430CB8 CRC64;
MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGI ITGVFPANPS
SWLIVVVGVI SSMHAKVDPS LGMIAKISRT LDTTGRMSSQ TKNIVSGVLF GTGLWVAVIM
TMRYSLKVLL SYHGWMFAEH GKMSRSTKIW MAMVKVLSGR KPMLYSFQTS LPRLPVPAVK
DTVSRYLESV RPLMKEEDFQ RMTALAQDFA VNLGPKLQWY LKLKSWWATN YVSDWWEEYI
YLRGRGPLMV NSNYYAMEML YITPTHIQAA RAGNTIHAIL LYRRTLDREE LKPIRLLGST
IPLCSAQWER LFNTSRIPGE ETDTIQHIKD SRHIVVYHRG RYFKVWLYHD GRLLRPRELE
QQMQQILDDP SEPQPGEAKL AALTAADRVP WAKCRQTYFA RGKNKQSLDA VEKAAFFVTL
DESEQGYREE DPEASIDSYA KSLLHGRCFD RWFDKSITFV VFKNSKIGIN AEHSWADAPV
VGHLWEYVMA TDVFQLGYSE DGHCKGDTNP NIPKPTRLQW DIPGECQEVI DASLSSASLL
ANDVDLHSFP FDSFGKGLIK KCRTSPDAFI QLALQLAHYK DMGKFCLTYE ASMTRLFREG
RTETVRSCTM ESCNFVQAMM DPKSTAEQRL KLFKIACEKH QHLYRLAMTG AGIDRHLFCL
YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDFE KNPDYVSCGG GFGPVADDGY
GVSYIIVGEN FIHFHISSKF SSPETDSHRF GKHLRQAMMD IITLFGLTIN SKK
