AMPD1_HUMAN
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 03-AUG-2022, entry version 191.
DE RecName: Full=AMP deaminase 1 {ECO:0000305};
DE EC=3.5.4.6;
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.
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 -!- 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 -!- 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.
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}.
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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; CCDS53349.1; -. [P23109-2]
DR CCDS; CCDS876.2; -. [P23109-1]
DR PIR; I39444; I39444.
DR RefSeq; NP_000027.2; NM_000036.2.
DR RefSeq; NP_001166097.1; NM_001172626.1. [P23109-2]
DR AlphaFoldDB; P23109; -.
DR BioGRID; 106767; 12.
DR IntAct; P23109; 11.
DR STRING; 9606.ENSP00000430075; -.
DR BindingDB; P23109; -.
DR ChEMBL; CHEMBL2869; -.
DR DrugBank; DB00131; Adenosine phosphate.
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; P23109; -.
DR PeptideAtlas; P23109; -.
DR PRIDE; P23109; -.
DR ProteomicsDB; 54053; -. [P23109-1]
DR ProteomicsDB; 54054; -. [P23109-2]
DR Antibodypedia; 33863; 268 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 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 OMA; MYVYNDA; -.
DR OrthoDB; 49756at2759; -.
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 UniPathway; UPA00591; UER00663.
DR BioGRID-ORCS; 270; 14 hits in 1073 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 121 other tissues.
DR ExpressionAtlas; P23109; baseline and differential.
DR Genevisible; P23109; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003876; F:AMP deaminase activity; IBA:GO_Central.
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 InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR029770; AMPD1.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR PANTHER; PTHR11359:SF1; PTHR11359:SF1; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
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 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 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
