KBL_HUMAN
ID KBL_HUMAN Reviewed; 419 AA.
AC O75600; E2QC23; Q6ZWF1; Q96CA9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial;
DE Short=AKB ligase;
DE EC=2.3.1.29 {ECO:0000250|UniProtKB:Q0P5L8};
DE AltName: Full=Aminoacetone synthase;
DE AltName: Full=Glycine acetyltransferase;
DE Flags: Precursor;
GN Name=GCAT {ECO:0000312|HGNC:HGNC:4188}; Synonyms=KBL;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=10712613; DOI=10.1046/j.1432-1327.2000.01175.x;
RA Edgar A.J., Polak J.M.;
RT "Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme
RT A ligase cDNAs.";
RL Eur. J. Biochem. 267:1805-1812(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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=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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 SUBCELLULAR LOCATION.
RX PubMed=17688197; DOI=10.1379/csc-264r.1;
RA Hoshino A., Fujii H.;
RT "Nuclear translocation of 2-amino-3-ketobutyrate coenzyme A ligase by cold
RT and osmotic stress.";
RL Cell Stress Chaperones 12:186-191(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes
CC the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA.
CC {ECO:0000250|UniProtKB:Q0P5L8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA;
CC Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29;
CC Evidence={ECO:0000250|UniProtKB:Q0P5L8};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20738;
CC Evidence={ECO:0000250|UniProtKB:Q0P5L8};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q0P5L8};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q0P5L8}.
CC Nucleus {ECO:0000269|PubMed:17688197}. Note=Translocates to the nucleus
CC upon cold and osmotic stress. {ECO:0000269|PubMed:17688197}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75600-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75600-2; Sequence=VSP_044607;
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, brain, liver and
CC pancreas. Also found in lung. {ECO:0000269|PubMed:10712613}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: One of the major routes for the degradation of L-threonine to
CC glycine in both prokaryotes and eukaryotes takes place through a two-
CC step biochemical pathway in mitochondria. In the first step, L-
CC threonine is oxidized to (2S)-2-amino-3-oxobutanoate, by L-threonine 3-
CC dehydrogenase tetramer (TDH). In the second step, mitochondrial 2-
CC amino-3-ketobutyrate coenzyme A ligase (GCAT) catalyzes the reaction
CC between (2S)-2-amino-3-oxobutanoate and coenzyme A to form glycine and
CC acetyl-CoA. In human, however the enzyme thats catalyzes the fist
CC reaction, TDH, is an expressed pseudogene encoding non-functional
CC truncated proteins. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC85552.1; Type=Frameshift; Evidence={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; AF077740; AAC27720.1; -; mRNA.
DR EMBL; AK123190; BAC85552.1; ALT_FRAME; mRNA.
DR EMBL; Z97630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014457; AAH14457.1; -; mRNA.
DR CCDS; CCDS13957.1; -. [O75600-1]
DR CCDS; CCDS54527.1; -. [O75600-2]
DR RefSeq; NP_001165161.1; NM_001171690.1. [O75600-2]
DR RefSeq; NP_055106.1; NM_014291.3. [O75600-1]
DR RefSeq; XP_005261467.1; XM_005261410.3. [O75600-2]
DR RefSeq; XP_016884166.1; XM_017028677.1. [O75600-1]
DR AlphaFoldDB; O75600; -.
DR SMR; O75600; -.
DR BioGRID; 117027; 60.
DR IntAct; O75600; 15.
DR MINT; O75600; -.
DR STRING; 9606.ENSP00000371110; -.
DR DrugBank; DB00145; Glycine.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR iPTMnet; O75600; -.
DR PhosphoSitePlus; O75600; -.
DR BioMuta; GCAT; -.
DR EPD; O75600; -.
DR jPOST; O75600; -.
DR MassIVE; O75600; -.
DR MaxQB; O75600; -.
DR PeptideAtlas; O75600; -.
DR PRIDE; O75600; -.
DR ProteomicsDB; 15221; -.
DR ProteomicsDB; 50106; -. [O75600-1]
DR Antibodypedia; 12139; 116 antibodies from 24 providers.
DR DNASU; 23464; -.
DR Ensembl; ENST00000248924.11; ENSP00000248924.6; ENSG00000100116.17. [O75600-1]
DR Ensembl; ENST00000323205.10; ENSP00000371110.3; ENSG00000100116.17. [O75600-2]
DR GeneID; 23464; -.
DR KEGG; hsa:23464; -.
DR MANE-Select; ENST00000248924.11; ENSP00000248924.6; NM_014291.4; NP_055106.1.
DR UCSC; uc003atz.4; human. [O75600-1]
DR CTD; 23464; -.
DR DisGeNET; 23464; -.
DR GeneCards; GCAT; -.
DR HGNC; HGNC:4188; GCAT.
DR HPA; ENSG00000100116; Tissue enhanced (pancreas).
DR MIM; 607422; gene.
DR neXtProt; NX_O75600; -.
DR OpenTargets; ENSG00000100116; -.
DR PharmGKB; PA28603; -.
DR VEuPathDB; HostDB:ENSG00000100116; -.
DR eggNOG; KOG1359; Eukaryota.
DR GeneTree; ENSGT00940000155729; -.
DR HOGENOM; CLU_015846_11_0_1; -.
DR InParanoid; O75600; -.
DR OMA; MDTHGFG; -.
DR OrthoDB; 930001at2759; -.
DR PhylomeDB; O75600; -.
DR TreeFam; TF105923; -.
DR BioCyc; MetaCyc:HS01980-MON; -.
DR PathwayCommons; O75600; -.
DR Reactome; R-HSA-8849175; Threonine catabolism.
DR SignaLink; O75600; -.
DR BioGRID-ORCS; 23464; 16 hits in 1087 CRISPR screens.
DR ChiTaRS; GCAT; human.
DR GenomeRNAi; 23464; -.
DR Pharos; O75600; Tbio.
DR PRO; PR:O75600; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O75600; protein.
DR Bgee; ENSG00000100116; Expressed in body of pancreas and 172 other tissues.
DR ExpressionAtlas; O75600; baseline and differential.
DR Genevisible; O75600; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008890; F:glycine C-acetyltransferase activity; NAS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; NAS:UniProtKB.
DR GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00985; 2am3keto_CoA_ligase; 1.
DR InterPro; IPR011282; 2am3keto_CoA_ligase.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01822; 2am3keto_CoA; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Mitochondrion; Nucleus;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q0P5L8"
FT CHAIN 22..419
FT /note="2-amino-3-ketobutyrate coenzyme A ligase,
FT mitochondrial"
FT /id="PRO_0000001246"
FT BINDING 134..135
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 206
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250, ECO:0000250|UniProtKB:P0AB77"
FT BINDING 262..265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 295..296
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT MOD_RES 45
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 45
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 187
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 187
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q0P5L8"
FT MOD_RES 326
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 368
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 383
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 383
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT VAR_SEQ 65
FT /note="G -> GGPGTVIFPGLPLPHLSCCIHLLSFTS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044607"
FT VARIANT 39
FT /note="R -> C (in dbSNP:rs710187)"
FT /id="VAR_015094"
FT VARIANT 100
FT /note="S -> N (in dbSNP:rs34468367)"
FT /id="VAR_048229"
FT CONFLICT 387
FT /note="R -> W (in Ref. 4; AAH14457)"
FT /evidence="ECO:0000305"
FT CONFLICT O75600-2:77
FT /note="L -> S (in Ref. 2; BAC85552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 45285 MW; C7760699E0474821 CRC64;
MWPGNAWRAA LFWVPRGRRA QSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV
DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA
RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD
MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG
PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP
AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS
RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP
