ID SYCM_HUMAN Reviewed; 564 AA. AC Q9HA77; Q8NI84; Q96IV4; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 183. DE RecName: Full=Probable cysteine--tRNA ligase, mitochondrial; DE EC=6.1.1.16; DE AltName: Full=Cysteinyl-tRNA synthetase; DE Short=CysRS; DE Flags: Precursor; GN Name=CARS2 {ECO:0000312|HGNC:HGNC:25695}; ORFNames=OK/SW-cl.10; 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]. RC TISSUE=Mammary gland; 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=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-555. RC TISSUE=Lung; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-564. RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that recognized by tumor-reactive CTL RT generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP IDENTIFICATION. RX PubMed=15779907; DOI=10.1021/bi047527z; RA Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C., RA Sissler M.; RT "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: RT characterization of AspRS and TyrRS."; RL Biochemistry 44:4805-4816(2005). 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]. 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). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-78; RP 124-LYS--LYS-127; CYS-257 AND 317-LYS--LYS-320, AND DOMAIN. RX PubMed=29079736; DOI=10.1038/s41467-017-01311-y; RA Akaike T., Ida T., Wei F.Y., Nishida M., Kumagai Y., Alam M.M., Ihara H., RA Sawa T., Matsunaga T., Kasamatsu S., Nishimura A., Morita M., Tomizawa K., RA Nishimura A., Watanabe S., Inaba K., Shima H., Tanuma N., Jung M., RA Fujii S., Watanabe Y., Ohmuraya M., Nagy P., Feelisch M., Fukuto J.M., RA Motohashi H.; RT "Cysteinyl-tRNA synthetase governs cysteine polysulfidation and RT mitochondrial bioenergetics."; RL Nat. Commun. 8:1177-1177(2017). RN [9] RP INVOLVEMENT IN COXPD27, AND VARIANT COXPD27 191-GLY--PRO-218 DEL. RX PubMed=25361775; DOI=10.1212/wnl.0000000000001055; RA Hallmann K., Zsurka G., Moskau-Hartmann S., Kirschner J., Korinthenberg R., RA Ruppert A.K., Ozdemir O., Weber Y., Becker F., Lerche H., Elger C.E., RA Thiele H., Nuernberg P., Sander T., Kunz W.S.; RT "A homozygous splice-site mutation in CARS2 is associated with progressive RT myoclonic epilepsy."; RL Neurology 83:2183-2187(2014). RN [10] RP INVOLVEMENT IN COXPD27, AND VARIANTS COXPD27 GLU-217 DEL AND LEU-251. RX PubMed=25787132; DOI=10.1136/jmedgenet-2015-103049; RA Coughlin C.R. II, Scharer G.H., Friederich M.W., Yu H.C., Geiger E.A., RA Creadon-Swindell G., Collins A.E., Vanlander A.V., Coster R.V., RA Powell C.A., Swanson M.A., Minczuk M., Van Hove J.L., Shaikh T.H.; RT "Mutations in the mitochondrial cysteinyl-tRNA synthase gene, CARS2, lead RT to a severe epileptic encephalopathy and complex movement disorder."; RL J. Med. Genet. 52:532-540(2015). CC -!- FUNCTION: Mitochondrial cysteine-specific aminoacyl-tRNA synthetase CC that catalyzes the ATP-dependent ligation of cysteine to tRNA(Cys). CC {ECO:0000269|PubMed:29079736}. CC -!- FUNCTION: In addition to its role as an aminoacyl-tRNA synthetase, has CC also cysteine persulfide synthase activity. Produces reactive CC persulfide species such as cysteine persulfide (CysSSH) from substrate CC cysteine and mediate direct incorporation of CysSSH into proteins CC during translations, resulting in protein persulfides and polysulfides CC (PubMed:29079736). CysSSHs behave as potent antioxidants and cellular CC protectants (PubMed:29079736). {ECO:0000269|PubMed:29079736}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L- CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661, CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517, CC ChEBI:CHEBI:456215; EC=6.1.1.16; CC Evidence={ECO:0000305|PubMed:29079736}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17775; CC Evidence={ECO:0000305|PubMed:29079736}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P21888}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P21888}; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:29079736}. CC -!- DOMAIN: 'KIIK' region and 'KMSKS' region are required for cysteine CC persulfide synthase activity. {ECO:0000269|PubMed:29079736}. CC -!- DISEASE: Combined oxidative phosphorylation deficiency 27 (COXPD27) CC [MIM:616672]: An autosomal recessive mitochondrial disorder CC characterized by multiple mitochondrial respiratory-chain-complex CC deficiencies causing neurological regression, progressive cognitive CC decline, complex movement disorder, epileptic encephalopathy, CC progressive spastic tetraparesis, and progressive impairment of vision CC and hearing. {ECO:0000269|PubMed:25361775, CC ECO:0000269|PubMed:25787132}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB93499.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AK022180; BAB13978.1; -; mRNA. DR EMBL; AL157820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL139385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007220; AAH07220.1; -; mRNA. DR EMBL; AB062436; BAB93499.1; ALT_INIT; mRNA. DR CCDS; CCDS9514.1; -. DR RefSeq; NP_078813.1; NM_024537.3. DR AlphaFoldDB; Q9HA77; -. DR SMR; Q9HA77; -. DR BioGRID; 122730; 101. DR IntAct; Q9HA77; 19. DR MINT; Q9HA77; -. DR STRING; 9606.ENSP00000257347; -. DR DrugBank; DB00151; Cysteine. DR GlyGen; Q9HA77; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9HA77; -. DR PhosphoSitePlus; Q9HA77; -. DR SwissPalm; Q9HA77; -. DR BioMuta; CARS2; -. DR DMDM; 74761587; -. DR EPD; Q9HA77; -. DR jPOST; Q9HA77; -. DR MassIVE; Q9HA77; -. DR MaxQB; Q9HA77; -. DR PaxDb; 9606-ENSP00000257347; -. DR PeptideAtlas; Q9HA77; -. DR ProteomicsDB; 81383; -. DR Pumba; Q9HA77; -. DR Antibodypedia; 42558; 37 antibodies from 18 providers. DR DNASU; 79587; -. DR Ensembl; ENST00000257347.9; ENSP00000257347.4; ENSG00000134905.17. DR GeneID; 79587; -. DR KEGG; hsa:79587; -. DR MANE-Select; ENST00000257347.9; ENSP00000257347.4; NM_024537.4; NP_078813.1. DR UCSC; uc001vrd.3; human. DR AGR; HGNC:25695; -. DR CTD; 79587; -. DR DisGeNET; 79587; -. DR GeneCards; CARS2; -. DR HGNC; HGNC:25695; CARS2. DR HPA; ENSG00000134905; Low tissue specificity. DR MalaCards; CARS2; -. DR MIM; 612800; gene. DR MIM; 616672; phenotype. DR neXtProt; NX_Q9HA77; -. DR OpenTargets; ENSG00000134905; -. DR Orphanet; 477774; Combined oxidative phosphorylation defect type 27. DR PharmGKB; PA162381083; -. DR VEuPathDB; HostDB:ENSG00000134905; -. DR eggNOG; KOG2007; Eukaryota. DR GeneTree; ENSGT00390000006347; -. DR HOGENOM; CLU_013528_0_3_1; -. DR InParanoid; Q9HA77; -. DR OMA; HAWPASE; -. DR OrthoDB; 2140072at2759; -. DR PhylomeDB; Q9HA77; -. DR TreeFam; TF300384; -. DR BRENDA; 6.1.1.16; 2681. DR PathwayCommons; Q9HA77; -. DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation. DR SignaLink; Q9HA77; -. DR SIGNOR; Q9HA77; -. DR BioGRID-ORCS; 79587; 253 hits in 1087 CRISPR screens. DR ChiTaRS; CARS2; human. DR GenomeRNAi; 79587; -. DR Pharos; Q9HA77; Tbio. DR PRO; PR:Q9HA77; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9HA77; Protein. DR Bgee; ENSG00000134905; Expressed in monocyte and 186 other cell types or tissues. DR ExpressionAtlas; Q9HA77; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IMP:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IMP:UniProtKB. DR CDD; cd00672; CysRS_core; 1. DR Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00041; Cys_tRNA_synth; 1. DR InterPro; IPR015803; Cys-tRNA-ligase. DR InterPro; IPR024909; Cys-tRNA/MSH_ligase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR032678; tRNA-synt_1_cat_dom. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR NCBIfam; TIGR00435; cysS; 1. DR PANTHER; PTHR10890:SF27; CYSTEINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1. DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR Genevisible; Q9HA77; HS. PE 1: Evidence at protein level; KW Aminoacyl-tRNA synthetase; ATP-binding; Disease variant; Ligase; KW Metal-binding; Mitochondrion; Nucleotide-binding; KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome; KW Transit peptide; Zinc. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..564 FT /note="Probable cysteine--tRNA ligase, mitochondrial" FT /id="PRO_0000250741" FT MOTIF 80..90 FT /note="'HIGH' region" FT MOTIF 124..127 FT /note="'KIIK' region" FT MOTIF 317..321 FT /note="'KMSKS' region" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P21888" FT BINDING 79 FT /ligand="L-cysteine" FT /ligand_id="ChEBI:CHEBI:35235" FT /evidence="ECO:0000250|UniProtKB:P21888" FT BINDING 119 FT /ligand="L-cysteine" FT /ligand_id="ChEBI:CHEBI:35235" FT /evidence="ECO:0000250|UniProtKB:P21888" FT BINDING 257 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P21888" FT BINDING 282 FT /ligand="L-cysteine" FT /ligand_id="ChEBI:CHEBI:35235" FT /evidence="ECO:0000250|UniProtKB:P21888" FT BINDING 282 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P21888" FT BINDING 286 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P21888" FT BINDING 320 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT VARIANT 191..218 FT /note="Missing (in COXPD27)" FT /evidence="ECO:0000269|PubMed:25361775" FT /id="VAR_075667" FT VARIANT 217 FT /note="Missing (in COXPD27; dbSNP:rs753472937)" FT /evidence="ECO:0000269|PubMed:25787132" FT /id="VAR_075668" FT VARIANT 251 FT /note="P -> L (in COXPD27; dbSNP:rs557671802)" FT /evidence="ECO:0000269|PubMed:25787132" FT /id="VAR_075669" FT VARIANT 440 FT /note="E -> K (in dbSNP:rs965189)" FT /id="VAR_034523" FT VARIANT 555 FT /note="Q -> P (in dbSNP:rs1043886)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_034524" FT MUTAGEN 78 FT /note="C->D: No effect on cysteine persulfide synthase FT activity; when associated with D-257. Loss of FT cysteine--tRNA ligase activity; when associated with FT D-257." FT /evidence="ECO:0000269|PubMed:29079736" FT MUTAGEN 124..127 FT /note="KIIK->AIIA: No effect on cysteine--tRNA ligase FT activity. Loss of cysteine persulfide synthase activity." FT /evidence="ECO:0000269|PubMed:29079736" FT MUTAGEN 257 FT /note="C->D: No effect on cysteine persulfide synthase FT activity; when associated with D-78. Loss of cysteine--tRNA FT ligase activity; when associated with D-78." FT /evidence="ECO:0000269|PubMed:29079736" FT MUTAGEN 317..320 FT /note="KMSK->AMSA: No effect on cysteine--tRNA ligase FT activity. Loss of cysteine persulfide synthase activity." FT /evidence="ECO:0000269|PubMed:29079736" FT CONFLICT 182..202 FT /note="RGNAYSTAKGNVYFDLKSRGD -> SWERLFNGKRQCLLRSESLEET (in FT Ref. 4; BAB93499)" FT /evidence="ECO:0000305" FT CONFLICT 207..223 FT /note="LVGVVPGPVGEPADSDK -> IGRRGPWSSPETSGLLTS (in Ref. 4; FT BAB93499)" FT /evidence="ECO:0000305" FT CONFLICT 227 FT /note="S -> N (in Ref. 4; BAB93499)" FT /evidence="ECO:0000305" SQ SEQUENCE 564 AA; 62224 MW; 92F8B615E6657D50 CRC64; MLRTTRGPGL GPPLLQAALG LGRAGWHWPA GRAASGGRGR AWLQPTGRET GVQVYNSLTG RKEPLIVAHA EAASWYSCGP TVYDHAHLGH ACSYVRFDII RRILTKVFGC SIVMVMGITD VDDKIIKRAN EMNISPASLA SLYEEDFKQD MAALKVLPPT VYLRVTENIP QIISFIEGII ARGNAYSTAK GNVYFDLKSR GDKYGKLVGV VPGPVGEPAD SDKRHASDFA LWKAAKPQEV FWASPWGPGR PGWHIECSAI ASMVFGSQLD IHSGGIDLAF PHHENEIAQC EVFHQCEQWG NYFLHSGHLH AKGKEEKMSK SLKNYITIKD FLKTFSPDVF RFFCLRSSYR SAIDYSDSAM LQAQQLLLGL GSFLEDARAY MKGQLACGSV REAMLWERLS STKRAVKAAL ADDFDTPRVV DAILGLAHHG NGQLRASLKE PEGPRSPAVF GAIISYFEQF FETVGISLAN QQYVSGDGSE ATLHGVVDEL VRFRQKVRQF ALAMPEATGD ARRQQLLERQ PLLEACDTLR RGLTAHGINI KDRSSTTSTW ELLDQRTKDQ KSAG //