KPB1_HUMAN
ID KPB1_HUMAN Reviewed; 1223 AA.
AC P46020; B7ZL05; B7ZL07; Q2M3D7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform;
DE Short=Phosphorylase kinase alpha M subunit;
GN Name=PHKA1; Synonyms=PHKA;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Muscle;
RX PubMed=8226841; DOI=10.1016/s0021-9258(19)49449-0;
RA Wuellrich A., Hamacher C., Schneider A., Kilimann M.W.;
RT "The multiphosphorylation domain of the phosphorylase kinase alpha M and
RT alpha L subunits is a hotspot of differential mRNA processing and of
RT molecular evolution.";
RL J. Biol. Chem. 268:23208-23214(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-972 AND SER-985, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758; SER-972 AND SER-985, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729; SER-972; SER-981 AND
RP SER-985, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP VARIANT GSD9D VAL-299.
RX PubMed=12825073; DOI=10.1038/sj.ejhg.5200996;
RA Burwinkel B., Hu B., Schroers A., Clemens P.R., Moses S.W., Shin Y.S.,
RA Pongratz D., Vorgerd M., Kilimann M.W.;
RT "Muscle glycogenosis with low phosphorylase kinase activity: mutations in
RT PHKA1, PHKG1 or six other candidate genes explain only a minority of
RT cases.";
RL Eur. J. Hum. Genet. 11:516-526(2003).
CC -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC serine in certain substrates, including troponin I. The alpha chain may
CC bind calmodulin.
CC -!- ACTIVITY REGULATION: By phosphorylation of various serine residues.
CC Allosteric regulation by calcium.
CC -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC -!- SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha,
CC beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB)
CC are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic
CC subunit, and delta is calmodulin.
CC -!- INTERACTION:
CC P46020-2; Q9UGJ1-2: TUBGCP4; NbExp=3; IntAct=EBI-11135904, EBI-10964469;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=AC;
CC IsoId=P46020-1; Sequence=Displayed;
CC Name=2; Synonyms=C;
CC IsoId=P46020-2; Sequence=VSP_004697;
CC Name=3;
CC IsoId=P46020-3; Sequence=VSP_042517, VSP_042518;
CC -!- TISSUE SPECIFICITY: Muscle specific. Isoform 1 is predominant in vastus
CC lateralis muscle. Isoform 2 predominates slightly in heart, and it
CC predominates clearly in the other tissues tested.
CC -!- PTM: Although the final Cys may be farnesylated, the terminal
CC tripeptide is probably not removed, and the C-terminus is not
CC methylated. {ECO:0000250|UniProtKB:P18688}.
CC -!- DISEASE: Glycogen storage disease 9D (GSD9D) [MIM:300559]: A metabolic
CC disorder characterized by slowly progressive, predominantly distal
CC muscle weakness and atrophy. Clinical features include exercise
CC intolerance with early fatigability, pain, cramps and occasionally
CC myoglobinuria. {ECO:0000269|PubMed:12825073}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; X73874; CAA52083.1; -; mRNA.
DR EMBL; BX295541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX295542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104944; AAI04945.1; -; mRNA.
DR EMBL; BC143499; AAI43500.1; -; mRNA.
DR EMBL; BC143501; AAI43502.1; -; mRNA.
DR CCDS; CCDS14421.1; -. [P46020-1]
DR CCDS; CCDS48137.1; -. [P46020-2]
DR CCDS; CCDS55453.1; -. [P46020-3]
DR PIR; I38111; I38111.
DR RefSeq; NP_001116142.1; NM_001122670.1. [P46020-2]
DR RefSeq; NP_001165907.1; NM_001172436.1. [P46020-3]
DR RefSeq; NP_002628.2; NM_002637.3. [P46020-1]
DR AlphaFoldDB; P46020; -.
DR BioGRID; 111273; 31.
DR CORUM; P46020; -.
DR IntAct; P46020; 10.
DR MINT; P46020; -.
DR STRING; 9606.ENSP00000362643; -.
DR ChEMBL; CHEMBL2111324; -.
DR iPTMnet; P46020; -.
DR MetOSite; P46020; -.
DR PhosphoSitePlus; P46020; -.
DR BioMuta; PHKA1; -.
DR DMDM; 110282976; -.
DR EPD; P46020; -.
DR jPOST; P46020; -.
DR MassIVE; P46020; -.
DR MaxQB; P46020; -.
DR PaxDb; P46020; -.
DR PeptideAtlas; P46020; -.
DR PRIDE; P46020; -.
DR ProteomicsDB; 55708; -. [P46020-1]
DR ProteomicsDB; 55709; -. [P46020-2]
DR ProteomicsDB; 55710; -. [P46020-3]
DR TopDownProteomics; P46020-2; -. [P46020-2]
DR Antibodypedia; 339; 108 antibodies from 27 providers.
DR DNASU; 5255; -.
DR Ensembl; ENST00000339490.7; ENSP00000342469.3; ENSG00000067177.15. [P46020-2]
DR Ensembl; ENST00000373542.9; ENSP00000362643.4; ENSG00000067177.15. [P46020-1]
DR Ensembl; ENST00000541944.5; ENSP00000441251.1; ENSG00000067177.15. [P46020-3]
DR GeneID; 5255; -.
DR KEGG; hsa:5255; -.
DR MANE-Select; ENST00000373542.9; ENSP00000362643.4; NM_002637.4; NP_002628.2.
DR UCSC; uc004eax.5; human. [P46020-1]
DR CTD; 5255; -.
DR DisGeNET; 5255; -.
DR GeneCards; PHKA1; -.
DR GeneReviews; PHKA1; -.
DR HGNC; HGNC:8925; PHKA1.
DR HPA; ENSG00000067177; Group enriched (parathyroid gland, skeletal muscle, tongue).
DR MalaCards; PHKA1; -.
DR MIM; 300559; phenotype.
DR MIM; 311870; gene.
DR neXtProt; NX_P46020; -.
DR OpenTargets; ENSG00000067177; -.
DR Orphanet; 715; Glycogen storage disease due to muscle phosphorylase kinase deficiency.
DR PharmGKB; PA33266; -.
DR VEuPathDB; HostDB:ENSG00000067177; -.
DR eggNOG; KOG3635; Eukaryota.
DR GeneTree; ENSGT00950000183118; -.
DR HOGENOM; CLU_004177_1_0_1; -.
DR InParanoid; P46020; -.
DR OMA; HTMLVQD; -.
DR OrthoDB; 55049at2759; -.
DR PhylomeDB; P46020; -.
DR TreeFam; TF313970; -.
DR BioCyc; MetaCyc:HS00901-MON; -.
DR BRENDA; 2.7.11.19; 2681.
DR PathwayCommons; P46020; -.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; P46020; -.
DR SIGNOR; P46020; -.
DR UniPathway; UPA00163; -.
DR BioGRID-ORCS; 5255; 7 hits in 696 CRISPR screens.
DR ChiTaRS; PHKA1; human.
DR GeneWiki; Phosphorylase_kinase,_alpha_1; -.
DR GenomeRNAi; 5255; -.
DR Pharos; P46020; Tbio.
DR PRO; PR:P46020; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P46020; protein.
DR Bgee; ENSG00000067177; Expressed in gastrocnemius and 148 other tissues.
DR ExpressionAtlas; P46020; baseline and differential.
DR Genevisible; P46020; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005964; C:phosphorylase kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004689; F:phosphorylase kinase activity; TAS:ProtInc.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR045583; KPBA/B_C.
DR InterPro; IPR008734; PHK_A/B_su.
DR PANTHER; PTHR10749; PTHR10749; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR Pfam; PF19292; KPBB_C; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Carbohydrate metabolism;
KW Cell membrane; Disease variant; Glycogen metabolism;
KW Glycogen storage disease; Lipoprotein; Membrane; Muscle protein;
KW Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..1223
FT /note="Phosphorylase b kinase regulatory subunit alpha,
FT skeletal muscle isoform"
FT /id="PRO_0000057726"
FT REGION 810..840
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 1021..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1086
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1021..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64649"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1007
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1018
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64649"
FT LIPID 1220
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT VAR_SEQ 654..713
FT /note="ARCGDEVARYLDHLLAHTAPHPKLAPTSQKGGLDRFQAAVQTTCDLMSLVTK
FT AKELHVQN -> D (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042517"
FT VAR_SEQ 1011..1023
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042518"
FT VAR_SEQ 1012..1024
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8226841"
FT /id="VSP_004697"
FT VARIANT 299
FT /note="D -> V (in GSD9D; dbSNP:rs137852547)"
FT /evidence="ECO:0000269|PubMed:12825073"
FT /id="VAR_020856"
FT CONFLICT 568
FT /note="H -> Y (in Ref. 1; CAA52083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1223 AA; 137312 MW; 48511719C0BFE40F CRC64;
MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA
YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTKD SLHAKYNTKT
CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD
FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS
ILNSLLPRAS TSKEVDASLL SVVSFPAFAV EDSQLVELTK QEIITKLQGR YGCCRFLRDG
YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGV FSGNAEQVQE YKEALEAVLI
KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG SLMAEGFLAP
GEIDPLNRRF STVPKPDVVV QVSILAETEE IKTILKDKGI YVETIAEVYP IRVQPARILS
HIYSSLGCNN RMKLSGRPYR HMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNKMIV
EMLRTDLSYL CSRWRMTGQP TITFPISHSM LDEDGTSLNS SILAALRKMQ DGYFGGARVQ
TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDDNYDYLE SGNWMNDYDS TSHARCGDEV
ARYLDHLLAH TAPHPKLAPT SQKGGLDRFQ AAVQTTCDLM SLVTKAKELH VQNVHMYLPT
KLFQASRPSF NLLDSPHPRQ ENQVPSVRVE IHLPRDQSGE VDFKALVLQL KETSSLQEQA
DILYMLYTMK GPDWNTELYN ERSATVRELL TELYGKVGEI RHWGLIRYIS GILRKKVEAL
DEACTDLLSH QKHLTVGLPP EPREKTISAP LPYEALTQLI DEASEGDMSI SILTQEIMVY
LAMYMRTQPG LFAEMFRLRI GLIIQVMATE LAHSLRCSAE EATEGLMNLS PSAMKNLLHH
ILSGKEFGVE RSVRPTDSNV SPAISIHEIG AVGATKTERT GIMQLKSEIK QVEFRRLSIS
AESQSPGTSM TPSSGSFPSA YDQQSSKDSR QGQWQRRRRL DGALNRVPVG FYQKVWKVLQ
KCHGLSVEGF VLPSSTTREM TPGEIKFSVH VESVLNRVPQ PEYRQLLVEA ILVLTMLADI
EIHSIGSIIA VEKIVHIAND LFLQEQKTLG ADDTMLAKDP ASGICTLLYD SAPSGRFGTM
TYLSKAAATY VQEFLPHSIC AMQ
