ID AMPD1_HUMAN Reviewed; 747 AA. AC P23109; A8K5N4; B2RAM1; F2Z3B3; Q5TF00; Q5TF02; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 3. DT 27-MAR-2024, entry version 200. DE RecName: Full=AMP deaminase 1 {ECO:0000305|PubMed:11102975}; DE EC=3.5.4.6 {ECO:0000269|PubMed:11102975}; DE AltName: Full=AMP deaminase isoform M; DE AltName: Full=Myoadenylate deaminase; GN Name=AMPD1 {ECO:0000312|HGNC:HGNC:468}; 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 [GENOMIC DNA]. RX PubMed=2345176; DOI=10.1016/s0021-9258(19)38866-0; RA Sabina R.L., Morisaki T., Clarke P., Eddy R., Shows T.B., Morton C.C., RA Holmes E.W.; RT "Characterization of the human and rat myoadenylate deaminase genes."; RL J. Biol. Chem. 265:9423-9433(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). 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 [MRNA] (ISOFORM 1). RX PubMed=1370861; DOI=10.1212/wnl.42.1.170; RA Sabina R.L., Fishbein W.N., Pezeshkpour G., Clarke P.R., Holmes E.W.; RT "Molecular analysis of the myoadenylate deaminase deficiencies."; RL Neurology 42:170-179(1992). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pericardium, and Tongue; 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 [6] RP VARIANT LEU-48. RX PubMed=1631143; DOI=10.1073/pnas.89.14.6457; RA Morisaki T., Gross M., Morisaki H., Pongratz D., Zoellner N., Holmes E.W.; RT "Molecular basis of AMP deaminase deficiency in skeletal muscle."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6457-6461(1992). RN [7] RP VARIANTS MMDD TRP-388 AND HIS-425, CHARACTERIZATION OF VARIANTS MMDD RP TRP-388 AND HIS-425, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=11102975; RX DOI=10.1002/1098-1004(200012)16:6<467::aid-humu3>3.0.co;2-v; RA Morisaki H., Higuchi I., Abe M., Osame M., Morisaki T.; RT "First missense mutations (R388W and R425H) of AMPD1 accompanied with RT myopathy found in a Japanese patient."; RL Hum. Mutat. 16:467-472(2000). RN [8] RP VARIANT [LARGE SCALE ANALYSIS] HIS-633. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism. CC {ECO:0000269|PubMed:11102975}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6; CC Evidence={ECO:0000269|PubMed:11102975}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778; CC Evidence={ECO:0000269|PubMed:11102975}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP CC from AMP: step 1/1. {ECO:0000269|PubMed:11102975}. CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC P23109; P23109: AMPD1; NbExp=3; IntAct=EBI-2959675, EBI-2959675; CC P23109; Q01433-2: AMPD2; NbExp=3; IntAct=EBI-2959675, EBI-11957578; CC P23109; Q01432-4: AMPD3; NbExp=3; IntAct=EBI-2959675, EBI-11955621; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P23109-1; Sequence=Displayed; CC Name=2; CC IsoId=P23109-2; Sequence=VSP_042638; CC -!- DISEASE: Myopathy due to myoadenylate deaminase deficiency (MMDD) CC [MIM:615511]: A metabolic disorder resulting in exercise-related CC myopathy. It is characterized by exercise-induced muscle aches, cramps, CC and early fatigue. {ECO:0000269|PubMed:11102975}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Adenosine and AMP deaminases family. {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; M37931; AAG24258.1; -; Genomic_DNA. DR EMBL; M37920; AAG24258.1; JOINED; Genomic_DNA. DR EMBL; M37921; AAG24258.1; JOINED; Genomic_DNA. DR EMBL; M37922; AAG24258.1; JOINED; Genomic_DNA. DR EMBL; M37923; AAG24258.1; JOINED; Genomic_DNA. DR EMBL; M37924; AAG24258.1; JOINED; Genomic_DNA. DR EMBL; M37927; AAG24258.1; JOINED; Genomic_DNA. DR EMBL; M37928; AAG24258.1; JOINED; Genomic_DNA. DR EMBL; M37929; AAG24258.1; JOINED; Genomic_DNA. DR EMBL; M37930; AAG24258.1; JOINED; Genomic_DNA. DR EMBL; AL096773; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471122; EAW56607.1; -; Genomic_DNA. DR EMBL; M60092; AAA57281.1; -; mRNA. DR EMBL; AK314252; BAG36918.1; -; mRNA. DR EMBL; AK291349; BAF84038.1; -; mRNA. DR CCDS; CCDS53349.2; -. [P23109-2] DR CCDS; CCDS876.3; -. [P23109-1] DR PIR; I39444; I39444. DR RefSeq; NP_000027.2; NM_000036.2. [P23109-1] DR RefSeq; NP_001166097.1; NM_001172626.1. [P23109-2] DR AlphaFoldDB; P23109; -. DR SMR; P23109; -. DR BioGRID; 106767; 13. DR IntAct; P23109; 11. DR STRING; 9606.ENSP00000430075; -. DR BindingDB; P23109; -. DR ChEMBL; CHEMBL2869; -. DR DrugBank; DB00131; Adenosine phosphate. DR GlyGen; P23109; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P23109; -. DR PhosphoSitePlus; P23109; -. DR BioMuta; AMPD1; -. DR DMDM; 384872309; -. DR CPTAC; CPTAC-1752; -. DR CPTAC; CPTAC-1753; -. DR MassIVE; P23109; -. DR PaxDb; 9606-ENSP00000430075; -. DR PeptideAtlas; P23109; -. DR ProteomicsDB; 54053; -. [P23109-1] DR ProteomicsDB; 54054; -. [P23109-2] DR Antibodypedia; 33863; 311 antibodies from 31 providers. DR DNASU; 270; -. DR Ensembl; ENST00000369538.4; ENSP00000358551.4; ENSG00000116748.22. [P23109-2] DR Ensembl; ENST00000520113.7; ENSP00000430075.3; ENSG00000116748.22. [P23109-1] DR GeneID; 270; -. DR KEGG; hsa:270; -. DR MANE-Select; ENST00000520113.7; ENSP00000430075.3; NM_000036.3; NP_000027.3. DR UCSC; uc001efe.3; human. [P23109-1] DR AGR; HGNC:468; -. DR CTD; 270; -. DR DisGeNET; 270; -. DR GeneCards; AMPD1; -. DR HGNC; HGNC:468; AMPD1. DR HPA; ENSG00000116748; Group enriched (skeletal muscle, tongue). DR MalaCards; AMPD1; -. DR MIM; 102770; gene. DR MIM; 615511; phenotype. DR neXtProt; NX_P23109; -. DR OpenTargets; ENSG00000116748; -. DR Orphanet; 45; Adenosine monophosphate deaminase deficiency. DR PharmGKB; PA24776; -. DR VEuPathDB; HostDB:ENSG00000116748; -. DR eggNOG; KOG1096; Eukaryota. DR GeneTree; ENSGT00950000183011; -. DR HOGENOM; CLU_003782_4_0_1; -. DR InParanoid; P23109; -. DR OrthoDB; 20951at2759; -. DR PhylomeDB; P23109; -. DR TreeFam; TF300439; -. DR BRENDA; 3.5.4.6; 2681. DR PathwayCommons; P23109; -. DR Reactome; R-HSA-74217; Purine salvage. DR SABIO-RK; P23109; -. DR SignaLink; P23109; -. DR SIGNOR; P23109; -. DR UniPathway; UPA00591; UER00663. DR BioGRID-ORCS; 270; 14 hits in 1151 CRISPR screens. DR ChiTaRS; AMPD1; human. DR GeneWiki; AMP_deaminase; -. DR GenomeRNAi; 270; -. DR Pharos; P23109; Tchem. DR PRO; PR:P23109; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P23109; Protein. DR Bgee; ENSG00000116748; Expressed in triceps brachii and 122 other cell types or tissues. DR ExpressionAtlas; P23109; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003876; F:AMP deaminase activity; IMP:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central. DR GO; GO:0032263; P:GMP salvage; IDA:MGI. DR GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central. DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway. DR CDD; cd01319; AMPD; 1. DR Gene3D; 4.10.800.20; -; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR006650; A/AMP_deam_AS. DR InterPro; IPR006329; AMPD. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR01429; AMP_deaminase; 1. DR PANTHER; PTHR11359; AMP DEAMINASE; 1. DR PANTHER; PTHR11359:SF1; AMP DEAMINASE 1; 1. DR Pfam; PF19326; AMP_deaminase; 1. DR PIRSF; PIRSF001251; AMP_deaminase_met; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS00485; A_DEAMINASE; 1. DR Genevisible; P23109; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; Hydrolase; Metal-binding; KW Nucleotide metabolism; Phosphoprotein; Reference proteome; Zinc. FT CHAIN 1..747 FT /note="AMP deaminase 1" FT /id="PRO_0000194403" FT ACT_SITE 594 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104" FT BINDING 303 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 305 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 305 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 374..379 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 572 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 575 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 649 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 650..653 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 81 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10759" FT MOD_RES 85 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10759" FT MOD_RES 216 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P10759" FT MOD_RES 441 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10759" FT VAR_SEQ 8..12 FT /note="AEEKQ -> E (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_042638" FT VARIANT 22 FT /note="E -> K (in dbSNP:rs2273268)" FT /id="VAR_048860" FT VARIANT 48 FT /note="P -> L (activity comparable to wild-type; FT dbSNP:rs61752479)" FT /evidence="ECO:0000269|PubMed:1631143" FT /id="VAR_013270" FT VARIANT 388 FT /note="R -> W (in MMDD; loss of AMP deaminase activity; FT dbSNP:rs35859650)" FT /evidence="ECO:0000269|PubMed:11102975" FT /id="VAR_013271" FT VARIANT 425 FT /note="R -> H (in MMDD; loss of AMP deaminase activity; FT dbSNP:rs121912682)" FT /evidence="ECO:0000269|PubMed:11102975" FT /id="VAR_013272" FT VARIANT 633 FT /note="P -> H (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035801" FT CONFLICT 201 FT /note="P -> S (in Ref. 5; BAF84038)" FT /evidence="ECO:0000305" FT CONFLICT 273 FT /note="V -> A (in Ref. 5; BAF84038)" FT /evidence="ECO:0000305" FT CONFLICT 434 FT /note="D -> G (in Ref. 5; BAG36918)" FT /evidence="ECO:0000305" FT CONFLICT 442 FT /note="W -> R (in Ref. 5; BAF84038)" FT /evidence="ECO:0000305" FT CONFLICT 626 FT /note="F -> S (in Ref. 5; BAF84038)" FT /evidence="ECO:0000305" SQ SEQUENCE 747 AA; 86490 MW; 1E15EBEE98B95763 CRC64; MPLFKLPAEE KQIDDAMRNF AEKVFASEVK DEGGRQEISP FDVDEICPIS HHEMQAHIFH LETLSTSTEA RRKKRFQGRK TVNLSIPLSE TSSTKLSHID EYISSSPTYQ TVPDFQRVQI TGDYASGVTV EDFEIVCKGL YRALCIREKY MQKSFQRFPK TPSKYLRNID GEAWVANESF YPVFTPPVKK GEDPFRTDNL PENLGYHLKM KDGVVYVYPN EAAVSKDEPK PLPYPNLDTF LDDMNFLLAL IAQGPVKTYT HRRLKFLSSK FQVHQMLNEM DELKELKNNP HRDFYNCRKV DTHIHAAACM NQKHLLRFIK KSYQIDADRV VYSTKEKNLT LKELFAKLKM HPYDLTVDSL DVHAGRQTFQ RFDKFNDKYN PVGASELRDL YLKTDNYING EYFATIIKEV GADLVEAKYQ HAEPRLSIYG RSPDEWSKLS SWFVCNRIHC PNMTWMIQVP RIYDVFRSKN FLPHFGKMLE NIFMPVFEAT INPQADPELS VFLKHITGFD SVDDESKHSG HMFSSKSPKP QEWTLEKNPS YTYYAYYMYA NIMVLNSLRK ERGMNTFLFR PHCGEAGALT HLMTAFMIAD DISHGLNLKK SPVLQYLFFL AQIPIAMSPL SNNSLFLEYA KNPFLDFLQK GLMISLSTDD PMQFHFTKEP LMEEYAIAAQ VFKLSTCDMC EVARNSVLQC GISHEEKVKF LGDNYLEEGP AGNDIRRTNV AQIRMAYRYE TWCYELNLIA EGLKSTE //