HMGC2_HUMAN
ID HMGC2_HUMAN Reviewed; 370 AA.
AC Q8TB92; B1AQ42; B3KNV0; B7Z1S7; F8W793; Q6ZSA9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic;
DE EC=4.1.3.4 {ECO:0000269|PubMed:22847177, ECO:0000269|PubMed:22865860};
DE AltName: Full=3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1;
DE Short=HMGCL-like 1;
DE AltName: Full=Endoplasmic reticulum 3-hydroxy-3-methylglutaryl-CoA lyase {ECO:0000303|PubMed:22847177};
DE Short=er-cHL {ECO:0000303|PubMed:22847177};
GN Name=HMGCLL1;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=22865860; DOI=10.1074/jbc.m112.393231;
RA Montgomery C., Pei Z., Watkins P.A., Miziorko H.M.;
RT "Identification and characterization of an extramitochondrial human 3-
RT Hydroxy-3-methylglutaryl-CoA lyase.";
RL J. Biol. Chem. 287:33227-33236(2012).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ARG-86; LEU-237 AND HIS-278.
RX PubMed=22847177; DOI=10.1194/jlr.m025700;
RA Arnedo M., Menao S., Puisac B., Teresa-Rodrigo M.E., Gil-Rodriguez M.C.,
RA Lopez-Vinas E., Gomez-Puertas P., Casals N., Casale C.H., Hegardt F.G.,
RA Pie J.;
RT "Characterization of a novel HMG-CoA Lyase enzyme with a dual location in
RT endoplasmic reticulum and cytosol.";
RL J. Lipid Res. 53:2046-2056(2012).
CC -!- FUNCTION: Non-mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase
CC that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-
CC methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in
CC ketogenesis, the products of which support energy production in
CC nonhepatic animal tissues. {ECO:0000269|PubMed:22847177,
CC ECO:0000269|PubMed:22865860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA;
CC Xref=Rhea:RHEA:24404, ChEBI:CHEBI:13705, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57288; EC=4.1.3.4; Evidence={ECO:0000269|PubMed:22847177,
CC ECO:0000269|PubMed:22865860};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000305|PubMed:22865860};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for (S)-3-hydroxy-3-methylglutaryl-CoA (at pH 9)
CC {ECO:0000269|PubMed:22847177};
CC KM=75 uM for (S)-3-hydroxy-3-methylglutaryl-CoA (at pH 8)
CC {ECO:0000269|PubMed:22847177};
CC KM=28 uM for (S)-3-hydroxy-3-methylglutaryl-CoA
CC {ECO:0000269|PubMed:22865860};
CC KM=49 uM for (S)-3-hydroxy-3-methylglutaryl-CoA (in presence of
CC magnesium) {ECO:0000269|PubMed:22865860};
CC KM=0.18 uM for (S)-3-hydroxy-3-methylglutaryl-CoA (in presence of
CC manganese) {ECO:0000269|PubMed:22865860};
CC Vmax=12 nmol/min/mg enzyme with (S)-3-hydroxy-3-methylglutaryl-CoA as
CC substrate at pH 9 {ECO:0000269|PubMed:22847177};
CC Vmax=25 nmol/min/mg enzyme with (S)-3-hydroxy-3-methylglutaryl-CoA as
CC substrate at pH 8 {ECO:0000269|PubMed:22847177};
CC -!- PATHWAY: Metabolic intermediate metabolism; (S)-3-hydroxy-3-
CC methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-
CC methylglutaryl-CoA: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22847177}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:22847177};
CC Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TB92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TB92-2; Sequence=VSP_033752;
CC Name=3;
CC IsoId=Q8TB92-4; Sequence=VSP_038021, VSP_038022;
CC Name=4;
CC IsoId=Q8TB92-5; Sequence=VSP_033752, VSP_044324;
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC87045.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAG51462.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK055075; BAG51462.1; ALT_SEQ; mRNA.
DR EMBL; AK127587; BAC87045.1; ALT_FRAME; mRNA.
DR EMBL; AK293856; BAH11613.1; -; mRNA.
DR EMBL; AL590290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04442.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04444.1; -; Genomic_DNA.
DR EMBL; BC024194; AAH24194.2; -; mRNA.
DR CCDS; CCDS43474.1; -. [Q8TB92-2]
DR CCDS; CCDS43475.1; -. [Q8TB92-1]
DR CCDS; CCDS75473.1; -. [Q8TB92-5]
DR RefSeq; NP_001035865.1; NM_001042406.1. [Q8TB92-2]
DR RefSeq; NP_001274670.1; NM_001287741.1. [Q8TB92-5]
DR RefSeq; NP_001274675.1; NM_001287746.1.
DR RefSeq; NP_061909.2; NM_019036.2. [Q8TB92-1]
DR AlphaFoldDB; Q8TB92; -.
DR SMR; Q8TB92; -.
DR BioGRID; 120006; 20.
DR IntAct; Q8TB92; 2.
DR STRING; 9606.ENSP00000381654; -.
DR SwissLipids; SLP:000001291; -. [Q8TB92-2]
DR iPTMnet; Q8TB92; -.
DR PhosphoSitePlus; Q8TB92; -.
DR BioMuta; HMGCLL1; -.
DR DMDM; 189028466; -.
DR MassIVE; Q8TB92; -.
DR MaxQB; Q8TB92; -.
DR PaxDb; Q8TB92; -.
DR PeptideAtlas; Q8TB92; -.
DR PRIDE; Q8TB92; -.
DR ProteomicsDB; 29914; -.
DR ProteomicsDB; 73974; -. [Q8TB92-1]
DR ProteomicsDB; 73975; -. [Q8TB92-2]
DR Antibodypedia; 31030; 61 antibodies from 14 providers.
DR DNASU; 54511; -.
DR Ensembl; ENST00000274901.9; ENSP00000274901.4; ENSG00000146151.14. [Q8TB92-2]
DR Ensembl; ENST00000308161.8; ENSP00000309737.4; ENSG00000146151.14. [Q8TB92-5]
DR Ensembl; ENST00000370852.6; ENSP00000359889.2; ENSG00000146151.14. [Q8TB92-4]
DR Ensembl; ENST00000398661.6; ENSP00000381654.2; ENSG00000146151.14. [Q8TB92-1]
DR GeneID; 54511; -.
DR KEGG; hsa:54511; -.
DR MANE-Select; ENST00000274901.9; ENSP00000274901.4; NM_001042406.2; NP_001035865.1. [Q8TB92-2]
DR UCSC; uc003pcn.4; human. [Q8TB92-1]
DR CTD; 54511; -.
DR DisGeNET; 54511; -.
DR GeneCards; HMGCLL1; -.
DR HGNC; HGNC:21359; HMGCLL1.
DR HPA; ENSG00000146151; Tissue enhanced (brain).
DR MIM; 619050; gene.
DR neXtProt; NX_Q8TB92; -.
DR OpenTargets; ENSG00000146151; -.
DR PharmGKB; PA134989971; -.
DR VEuPathDB; HostDB:ENSG00000146151; -.
DR eggNOG; KOG2368; Eukaryota.
DR GeneTree; ENSGT00940000159467; -.
DR HOGENOM; CLU_214024_0_0_1; -.
DR InParanoid; Q8TB92; -.
DR OMA; FHNTRGT; -.
DR PhylomeDB; Q8TB92; -.
DR TreeFam; TF105363; -.
DR PathwayCommons; Q8TB92; -.
DR Reactome; R-HSA-77111; Synthesis of Ketone Bodies.
DR SABIO-RK; Q8TB92; -.
DR SignaLink; Q8TB92; -.
DR UniPathway; UPA00896; UER00863.
DR BioGRID-ORCS; 54511; 37 hits in 1062 CRISPR screens.
DR ChiTaRS; HMGCLL1; human.
DR GenomeRNAi; 54511; -.
DR Pharos; Q8TB92; Tbio.
DR PRO; PR:Q8TB92; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8TB92; protein.
DR Bgee; ENSG00000146151; Expressed in cortical plate and 137 other tissues.
DR ExpressionAtlas; Q8TB92; baseline and differential.
DR Genevisible; Q8TB92; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0046951; P:ketone body biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR030021; ER-cHL.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; PTHR42738; 1.
DR PANTHER; PTHR42738:SF5; PTHR42738:SF5; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Lipid metabolism;
KW Lipoprotein; Lyase; Membrane; Metal-binding; Myristate; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..370
FT /note="3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic"
FT /id="PRO_0000334669"
FT DOMAIN 78..345
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT ACT_SITE 311
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:22865860"
FT VAR_SEQ 37..66
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033752"
FT VAR_SEQ 37..53
FT /note="TSLLTNLHCFQPDVSGF -> ELQSVMLMLHHGPLRKP (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038021"
FT VAR_SEQ 54..370
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038022"
FT VAR_SEQ 130..161
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044324"
FT MUTAGEN 2
FT /note="G->A: Abolishes myristoylation and induces a
FT subcellular location change."
FT /evidence="ECO:0000269|PubMed:22865860"
FT MUTAGEN 86
FT /note="R->Q: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22847177"
FT MUTAGEN 237
FT /note="L->S: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22847177"
FT MUTAGEN 278
FT /note="H->R: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22847177"
FT CONFLICT 99
FT /note="D -> G (in Ref. 1; BAH11613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 39514 MW; 7DDEE81555E092A1 CRC64;
MGNVPSAVKH CLSYQQLLRE HLWIGDSVAG ALDPAQTSLL TNLHCFQPDV SGFSVSLAGT
VACIHWETSQ LSGLPEFVKI VEVGPRDGLQ NEKVIVPTDI KIEFINRLSQ TGLSVIEVTS
FVSSRWVPQM ADHTEVMKGI HQYPGVRYPV LTPNLQGFHH AVAAGATEIS VFGAASESFS
KKNINCSIEE SMGKFEEVVK SARHMNIPAR GYVSCALGCP YEGSITPQKV TEVSKRLYGM
GCYEISLGDT IGVGTPGSMK RMLESVMKEI PPGALAVHCH DTYGQALANI LTALQMGINV
VDSAVSGLGG CPYAKGASGN VATEDLIYML NGLGLNTGVN LYKVMEAGDF ICKAVNKTTN
SKVAQASFNA
