THIK2_ARATH
ID THIK2_ARATH Reviewed; 462 AA.
AC Q56WD9; Q93Z35; Q9S7M3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=3-ketoacyl-CoA thiolase 2, peroxisomal;
DE EC=2.3.1.16;
DE AltName: Full=Acetyl-CoA acyltransferase 2;
DE AltName: Full=Beta-ketothiolase 2;
DE AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase 2;
DE AltName: Full=Peroxisome defective protein 1;
DE Flags: Precursor;
GN Name=PED1; Synonyms=KAT2; OrderedLocusNames=At2g33150; ORFNames=F25I18.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INDUCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=9490742; DOI=10.2307/3870697;
RA Hayashi M., Toriyama K., Kondo M., Nishimura M.;
RT "2,4-Dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have
RT defects in glyoxysomal fatty acid beta-oxidation.";
RL Plant Cell 10:183-195(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND PTS2-TYPE IMPORT.
RX PubMed=14630959; DOI=10.1104/pp.103.028217;
RA Johnson T.L., Olsen L.J.;
RT "Import of the peroxisomal targeting signal type 2 protein 3-ketoacyl-
RT coenzyme A thiolase into glyoxysomes.";
RL Plant Physiol. 133:1991-1999(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-462.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10212254; DOI=10.1074/jbc.274.18.12715;
RA Hayashi H., De Bellis L., Ciurli A., Kondo M., Hayashi M., Nishimura M.;
RT "A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant
RT peroxisomes.";
RL J. Biol. Chem. 274:12715-12721(1999).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=11356168; DOI=10.1042/0300-5127:0290283;
RA Rylott E.L., Hooks M.A., Graham I.A.;
RT "Co-ordinate regulation of genes involved in storage lipid mobilization in
RT Arabidopsis thaliana.";
RL Biochem. Soc. Trans. 29:283-287(2001).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11696182; DOI=10.1046/j.1365-313x.2001.01095.x;
RA Germain V., Rylott E.L., Larson T.R., Sherson S.M., Bechtold N.,
RA Carde J.-P., Bryce J.H., Graham I.A., Smith S.M.;
RT "Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty
RT acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of
RT Arabidopsis seedlings.";
RL Plant J. 28:1-12(2001).
RN [11]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11891244; DOI=10.1104/pp.010843;
RA He Y., Fukushige H., Hildebrand D.F., Gan S.;
RT "Evidence supporting a role of jasmonic acid in Arabidopsis leaf
RT senescence.";
RL Plant Physiol. 128:876-884(2002).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15141068; DOI=10.1104/pp.104.039925;
RA Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J.;
RT "Gene-specific involvement of beta-oxidation in wound-activated responses
RT in Arabidopsis.";
RL Plant Physiol. 135:85-94(2004).
RN [13]
RP FUNCTION.
RX PubMed=15979881; DOI=10.1016/j.plaphy.2005.03.016;
RA Afitlhile M.M., Fukushige H., Nishimura M., Hildebrand D.F.;
RT "A defect in glyoxysomal fatty acid beta-oxidation reduces jasmonic acid
RT accumulation in Arabidopsis.";
RL Plant Physiol. Biochem. 43:603-609(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 38-441, AND SUBUNIT.
RX PubMed=16630629; DOI=10.1016/j.jmb.2006.03.032;
RA Sundaramoorthy R., Micossi E., Alphey M.S., Germain V., Bryce J.H.,
RA Smith S.M., Leonard G.A., Hunter W.N.;
RT "The crystal structure of a plant 3-ketoacyl-CoA thiolase reveals the
RT potential for redox control of peroxisomal fatty acid beta-oxidation.";
RL J. Mol. Biol. 359:347-357(2006).
CC -!- FUNCTION: Involved in long chain fatty-acid beta-oxidation prior to
CC gluconeogenesis during germination and subsequent seedling growth.
CC Confers sensitivity to 2,4-dichlorophenoxybutiric acid (2,4-DB).
CC Required for local and systemic induction of jasmonic acid (JA)
CC biosynthesis after wounding. Seems to be involved in JA biosynthesis
CC during senescence. {ECO:0000269|PubMed:11696182,
CC ECO:0000269|PubMed:11891244, ECO:0000269|PubMed:15141068,
CC ECO:0000269|PubMed:15979881, ECO:0000269|PubMed:9490742}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=77.5 uM for acetoacetyl-CoA (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:11696182};
CC Vmax=5000 nmol/min/mg enzyme (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:11696182};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16630629}.
CC -!- INTERACTION:
CC Q56WD9; Q9XF57: PEX7; NbExp=3; IntAct=EBI-4468126, EBI-9536794;
CC -!- SUBCELLULAR LOCATION: Peroxisome. Glyoxysome. Note=Peroxisomal
CC targeting signal type 2 (PTS2-type) import is temperature and ATP-
CC dependent, induced by zinc ions and PTS1-type import, but repressed by
CC mature forms of PED1.
CC -!- TISSUE SPECIFICITY: Accumulates in etiolated cotyledons and in
CC seedlings, also present in roots, flowers and siliques (at protein
CC level). High levels in wounded leaves. {ECO:0000269|PubMed:10212254,
CC ECO:0000269|PubMed:11696182, ECO:0000269|PubMed:15141068,
CC ECO:0000269|PubMed:9490742}.
CC -!- DEVELOPMENTAL STAGE: Levels increase strongly upon imbibition and
CC decrease 3 days later. Strongly induced in leaves during senescence.
CC {ECO:0000269|PubMed:11356168, ECO:0000269|PubMed:11696182,
CC ECO:0000269|PubMed:11891244}.
CC -!- INDUCTION: Expressed in the dark, repressed by light (at protein
CC level). Induced by dehydration, by abscisic acid (ABA) and by wounding,
CC both locally and systemically. {ECO:0000269|PubMed:10212254,
CC ECO:0000269|PubMed:15141068, ECO:0000269|PubMed:9490742}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25590.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB008854; BAA25248.1; -; mRNA.
DR EMBL; AB008855; BAA25249.1; -; Genomic_DNA.
DR EMBL; AC002334; AAC04908.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08791.1; -; Genomic_DNA.
DR EMBL; AY058176; AAL25590.1; ALT_FRAME; mRNA.
DR EMBL; AF327529; AAG42910.1; -; mRNA.
DR EMBL; AF349530; AAK15577.1; -; mRNA.
DR EMBL; AY052702; AAK96606.1; -; mRNA.
DR EMBL; AY063720; AAL36070.1; -; mRNA.
DR EMBL; AY087543; AAM65085.1; -; mRNA.
DR EMBL; AK222103; BAD95031.1; -; mRNA.
DR PIR; T52110; T52110.
DR RefSeq; NP_180873.1; NM_128874.4.
DR PDB; 2C7Y; X-ray; 2.10 A; A/B=38-441.
DR PDB; 2C7Z; X-ray; 2.37 A; A=38-441.
DR PDB; 2WU9; X-ray; 1.50 A; A/B=36-462.
DR PDBsum; 2C7Y; -.
DR PDBsum; 2C7Z; -.
DR PDBsum; 2WU9; -.
DR AlphaFoldDB; Q56WD9; -.
DR SMR; Q56WD9; -.
DR BioGRID; 3223; 24.
DR IntAct; Q56WD9; 4.
DR MINT; Q56WD9; -.
DR STRING; 3702.AT2G33150.1; -.
DR MetOSite; Q56WD9; -.
DR PaxDb; Q56WD9; -.
DR PRIDE; Q56WD9; -.
DR ProteomicsDB; 234272; -.
DR EnsemblPlants; AT2G33150.1; AT2G33150.1; AT2G33150.
DR GeneID; 817876; -.
DR Gramene; AT2G33150.1; AT2G33150.1; AT2G33150.
DR KEGG; ath:AT2G33150; -.
DR Araport; AT2G33150; -.
DR TAIR; locus:2046565; AT2G33150.
DR eggNOG; KOG1389; Eukaryota.
DR HOGENOM; CLU_031026_1_1_1; -.
DR InParanoid; Q56WD9; -.
DR OMA; DYYWGMG; -.
DR OrthoDB; 1129049at2759; -.
DR PhylomeDB; Q56WD9; -.
DR BioCyc; MetaCyc:AT2G33150-MON; -.
DR BRENDA; 2.3.1.16; 399.
DR SABIO-RK; Q56WD9; -.
DR UniPathway; UPA00199; -.
DR EvolutionaryTrace; Q56WD9; -.
DR PRO; PR:Q56WD9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q56WD9; baseline and differential.
DR Genevisible; Q56WD9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:TAIR.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010111; P:glyoxysome organization; IMP:TAIR.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; NAS:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; NAS:TAIR.
DR CDD; cd00751; thiolase; 1.
DR DisProt; DP02979; -.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Glyoxysome; Lipid biosynthesis; Lipid metabolism;
KW Oxylipin biosynthesis; Peroxisome; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..34
FT /note="Peroxisome"
FT /evidence="ECO:0000305"
FT CHAIN 35..462
FT /note="3-ketoacyl-CoA thiolase 2, peroxisomal"
FT /id="PRO_0000034073"
FT ACT_SITE 138
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT CONFLICT 17
FT /note="P -> F (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:2C7Y"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:2WU9"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2WU9"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 75..90
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:2WU9"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 211..230
FT /evidence="ECO:0007829|PDB:2WU9"
FT TURN 231..237
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:2WU9"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2C7Y"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 295..305
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 306..312
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 318..327
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 330..335
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 336..347
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 397..413
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 419..426
FT /evidence="ECO:0007829|PDB:2WU9"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:2WU9"
FT STRAND 430..438
FT /evidence="ECO:0007829|PDB:2WU9"
FT HELIX 441..446
FT /evidence="ECO:0007829|PDB:2WU9"
SQ SEQUENCE 462 AA; 48579 MW; 7405F81968489ADB CRC64;
MEKAIERQRV LLEHLRPSSS SSHNYEASLS ASACLAGDSA AYQRTSLYGD DVVIVAAHRT
PLCKSKRGNF KDTYPDDLLA PVLRALIEKT NLNPSEVGDI VVGTVLAPGS QRASECRMAA
FYAGFPETVA VRTVNRQCSS GLQAVADVAA AIKAGFYDIG IGAGLESMTT NPMAWEGSVN
PAVKKFAQAQ NCLLPMGVTS ENVAQRFGVS RQEQDQAAVD SHRKAAAATA AGKFKDEIIP
VKTKLVDPKT GDEKPITVSV DDGIRPTTTL ASLGKLKPVF KKDGTTTAGN SSQVSDGAGA
VLLMKRSVAM QKGLPVLGVF RTFAAVGVDP AIMGIGPAVA IPAAVKAAGL ELDDIDLFEI
NEAFASQFVY CRNKLGLDPE KINVNGGAMA IGHPLGATGA RCVATLLHEM KRRGKDCRFG
VVSMCIGTGM GAAAVFERGD GVDELRNARK VEAQGLLSKD AR
