KPBB_HUMAN
ID KPBB_HUMAN Reviewed; 1093 AA.
AC Q93100; Q8N4T5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Phosphorylase b kinase regulatory subunit beta;
DE Short=Phosphorylase kinase subunit beta;
GN Name=PHKB;
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 / MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=8681948; DOI=10.1111/j.1432-1033.1996.0374z.x;
RA Wuellrich-Schmoll A., Kilimann M.W.;
RT "Structure of the human gene encoding the phosphorylase kinase beta subunit
RT (PHKB).";
RL Eur. J. Biochem. 238:374-380(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Uterus;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [4]
RP IDENTIFICATION BY 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-27, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORMS 2 AND 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORMS 2 AND 4),
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2),
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP VARIANT CYS-770.
RX PubMed=9326319; DOI=10.1086/515502;
RA van den Berg I.E.T., van Beurden E.A.C.M., de Klerk J.B.C.,
RA van Diggelen O.P., Malingre H.E.M., Boer M.M., Berger R.;
RT "Autosomal recessive phosphorylase kinase deficiency in liver, caused by
RT mutations in the gene encoding the beta subunit (PHKB).";
RL Am. J. Hum. Genet. 61:539-546(1997).
RN [12]
RP VARIANT GSD9B PRO-118.
RX PubMed=9402963; DOI=10.1007/s004390050608;
RA Burwinkel B., Moses S.W., Kilimann M.W.;
RT "Phosphorylase-kinase-deficient liver glycogenosis with an unusual
RT biochemical phenotype in blood cells associated with a missense mutation in
RT the beta subunit gene (PHKB).";
RL Hum. Genet. 101:170-174(1997).
RN [13]
RP VARIANTS LYS-657 AND CYS-770.
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).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-867 AND ARG-877.
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: Phosphorylase b kinase catalyzes the phosphorylation of
CC serine in certain substrates, including troponin I. The beta chain acts
CC as a regulatory unit and modulates the activity of the holoenzyme in
CC response to phosphorylation.
CC -!- ACTIVITY REGULATION: By phosphorylation of various serine residues.
CC {ECO:0000250}.
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 Q93100; Q13554: CAMK2B; NbExp=3; IntAct=EBI-740559, EBI-1058722;
CC Q93100; Q96RG2: PASK; NbExp=2; IntAct=EBI-740559, EBI-1042651;
CC Q93100-4; P46019: PHKA2; NbExp=3; IntAct=EBI-11064505, EBI-1642846;
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=4;
CC Name=1;
CC IsoId=Q93100-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93100-2; Sequence=VSP_012445;
CC Name=3;
CC IsoId=Q93100-3; Sequence=VSP_012446;
CC Name=4;
CC IsoId=Q93100-4; Sequence=VSP_012445, VSP_012446;
CC -!- PTM: Ser-701 is probably phosphorylated by PKA.
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:P12798}.
CC -!- DISEASE: Glycogen storage disease 9B (GSD9B) [MIM:261750]: A metabolic
CC disorder characterized by hepatomegaly, only slightly elevated
CC transaminases and plasma lipids, clinical improvement with increasing
CC age, and remarkably no clinical muscle involvement. Biochemical
CC observations suggest that this mild phenotype is caused by an
CC incomplete holoenzyme that lacks the beta subunit, but that may possess
CC residual activity. {ECO:0000269|PubMed:9402963}. 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; X84909; CAA59333.1; -; Genomic_DNA.
DR EMBL; X84911; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84912; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84913; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84914; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84915; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84916; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84917; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84918; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84919; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84920; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84921; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84922; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84923; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84924; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84925; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84926; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84927; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84928; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84929; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84930; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84931; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84933; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84934; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84935; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84936; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84937; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84938; CAA59333.1; JOINED; Genomic_DNA.
DR EMBL; X84908; CAA59332.1; -; mRNA.
DR EMBL; BC033657; AAH33657.1; -; mRNA.
DR CCDS; CCDS10729.1; -. [Q93100-1]
DR CCDS; CCDS42161.1; -. [Q93100-4]
DR PIR; S74250; S74250.
DR PIR; S74251; S74251.
DR RefSeq; NP_000284.1; NM_000293.2. [Q93100-1]
DR RefSeq; NP_001027005.1; NM_001031835.2. [Q93100-4]
DR RefSeq; XP_005256040.1; XM_005255983.4.
DR RefSeq; XP_005256041.1; XM_005255984.4.
DR AlphaFoldDB; Q93100; -.
DR BioGRID; 111275; 45.
DR CORUM; Q93100; -.
DR IntAct; Q93100; 20.
DR MINT; Q93100; -.
DR STRING; 9606.ENSP00000313504; -.
DR ChEMBL; CHEMBL2111324; -.
DR iPTMnet; Q93100; -.
DR PhosphoSitePlus; Q93100; -.
DR SwissPalm; Q93100; -.
DR BioMuta; PHKB; -.
DR DMDM; 2499582; -.
DR EPD; Q93100; -.
DR jPOST; Q93100; -.
DR MassIVE; Q93100; -.
DR MaxQB; Q93100; -.
DR PaxDb; Q93100; -.
DR PeptideAtlas; Q93100; -.
DR PRIDE; Q93100; -.
DR ProteomicsDB; 75726; -. [Q93100-1]
DR ProteomicsDB; 75727; -. [Q93100-2]
DR ProteomicsDB; 75728; -. [Q93100-3]
DR ProteomicsDB; 75729; -. [Q93100-4]
DR Antibodypedia; 28116; 183 antibodies from 29 providers.
DR DNASU; 5257; -.
DR Ensembl; ENST00000299167.12; ENSP00000299167.8; ENSG00000102893.16. [Q93100-3]
DR Ensembl; ENST00000323584.10; ENSP00000313504.5; ENSG00000102893.16. [Q93100-1]
DR Ensembl; ENST00000566044.5; ENSP00000456729.1; ENSG00000102893.16. [Q93100-4]
DR GeneID; 5257; -.
DR KEGG; hsa:5257; -.
DR MANE-Select; ENST00000323584.10; ENSP00000313504.5; NM_000293.3; NP_000284.1.
DR UCSC; uc002eeu.5; human. [Q93100-1]
DR CTD; 5257; -.
DR DisGeNET; 5257; -.
DR GeneCards; PHKB; -.
DR GeneReviews; PHKB; -.
DR HGNC; HGNC:8927; PHKB.
DR HPA; ENSG00000102893; Tissue enhanced (skeletal).
DR MalaCards; PHKB; -.
DR MIM; 172490; gene.
DR MIM; 261750; phenotype.
DR neXtProt; NX_Q93100; -.
DR OpenTargets; ENSG00000102893; -.
DR Orphanet; 79240; Glycogen storage disease due to liver and muscle phosphorylase kinase deficiency.
DR PharmGKB; PA33268; -.
DR VEuPathDB; HostDB:ENSG00000102893; -.
DR eggNOG; KOG3635; Eukaryota.
DR GeneTree; ENSGT00950000183118; -.
DR HOGENOM; CLU_004177_0_1_1; -.
DR InParanoid; Q93100; -.
DR OMA; VIYTHHE; -.
DR OrthoDB; 55049at2759; -.
DR PhylomeDB; Q93100; -.
DR TreeFam; TF313970; -.
DR BioCyc; MetaCyc:HS02424-MON; -.
DR BRENDA; 2.7.11.19; 2681.
DR PathwayCommons; Q93100; -.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; Q93100; -.
DR UniPathway; UPA00163; -.
DR BioGRID-ORCS; 5257; 7 hits in 1076 CRISPR screens.
DR ChiTaRS; PHKB; human.
DR GeneWiki; PHKB; -.
DR GenomeRNAi; 5257; -.
DR Pharos; Q93100; Tbio.
DR PRO; PR:Q93100; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q93100; protein.
DR Bgee; ENSG00000102893; Expressed in adrenal tissue and 210 other tissues.
DR ExpressionAtlas; Q93100; baseline and differential.
DR Genevisible; Q93100; 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:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR InterPro; IPR008928; 6-hairpin_glycosidase_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 Acetylation; Alternative splicing; Calmodulin-binding;
KW Carbohydrate metabolism; Cell membrane; Disease variant;
KW Glycogen metabolism; Glycogen storage disease; Lipoprotein; Membrane;
KW Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P12798"
FT CHAIN 2..1093
FT /note="Phosphorylase b kinase regulatory subunit beta"
FT /id="PRO_0000057736"
FT REGION 7..29
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 689..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..795
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 920..951
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 697..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P12798"
FT MOD_RES 12
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P12798"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12798"
FT LIPID 1090
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P12798"
FT VAR_SEQ 1..23
FT /note="MAGAAGLTAEVSWKVLERRARTK -> MACSPDAVVSPSSAFL (in
FT isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012445"
FT VAR_SEQ 780..806
FT /note="LAVRYGAAFTQKFSSSIAPHITTFLVH -> SVVRRAASLLSKVVDSLAPSI
FT TNVLVQ (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012446"
FT VARIANT 118
FT /note="A -> P (in GSD9B; dbSNP:rs121918022)"
FT /evidence="ECO:0000269|PubMed:9402963"
FT /id="VAR_015536"
FT VARIANT 657
FT /note="Q -> K (in dbSNP:rs34667348)"
FT /evidence="ECO:0000269|PubMed:12825073"
FT /id="VAR_020857"
FT VARIANT 770
FT /note="Y -> C (in dbSNP:rs16945474)"
FT /evidence="ECO:0000269|PubMed:12825073,
FT ECO:0000269|PubMed:9326319"
FT /id="VAR_006187"
FT VARIANT 820
FT /note="E -> V (in dbSNP:rs9934849)"
FT /id="VAR_034056"
FT VARIANT 867
FT /note="L -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036486"
FT VARIANT 877
FT /note="G -> R (in a breast cancer sample; somatic mutation;
FT dbSNP:rs150902092)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036487"
FT INIT_MET Q93100-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q93100-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q93100-2:4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT INIT_MET Q93100-4:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q93100-4:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q93100-4:4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
SQ SEQUENCE 1093 AA; 124884 MW; 48F05EE306195472 CRC64;
MAGAAGLTAE VSWKVLERRA RTKRSGSVYE PLKSINLPRP DNETLWDKLD HYYRIVKSTL
LLYQSPTTGL FPTKTCGGDQ KAKIQDSLYC AAGAWALALA YRRIDDDKGR THELEHSAIK
CMRGILYCYM RQADKVQQFK QDPRPTTCLH SVFNVHTGDE LLSYEEYGHL QINAVSLYLL
YLVEMISSGL QIIYNTDEVS FIQNLVFCVE RVYRVPDFGV WERGSKYNNG STELHSSSVG
LAKAALEAIN GFNLFGNQGC SWSVIFVDLD AHNRNRQTLC SLLPRESRSH NTDAALLPCI
SYPAFALDDE VLFSQTLDKV VRKLKGKYGF KRFLRDGYRT SLEDPNRCYY KPAEIKLFDG
IECEFPIFFL YMMIDGVFRG NPKQVQEYQD LLTPVLHHTT EGYPVVPKYY YVPADFVEYE
KNNPGSQKRF PSNCGRDGKL FLWGQALYII AKLLADELIS PKDIDPVQRY VPLKDQRNVS
MRFSNQGPLE NDLVVHVALI AESQRLQVFL NTYGIQTQTP QQVEPIQIWP QQELVKAYLQ
LGINEKLGLS GRPDRPIGCL GTSKIYRILG KTVVCYPIIF DLSDFYMSQD VFLLIDDIKN
ALQFIKQYWK MHGRPLFLVL IREDNIRGSR FNPILDMLAA LKKGIIGGVK VHVDRLQTLI
SGAVVEQLDF LRISDTEELP EFKSFEELEP PKHSKVKRQS STPSAPELGQ QPDVNISEWK
DKPTHEILQK LNDCSCLASQ AILLGILLKR EGPNFITKEG TVSDHIERVY RRAGSQKLWL
AVRYGAAFTQ KFSSSIAPHI TTFLVHGKQV TLGAFGHEEE VISNPLSPRV IQNIIYYKCN
THDEREAVIQ QELVIHIGWI ISNNPELFSG MLKIRIGWII HAMEYELQIR GGDKPALDLY
QLSPSEVKQL LLDILQPQQN GRCWLNRRQI DGSLNRTPTG FYDRVWQILE RTPNGIIVAG
KHLPQQPTLS DMTMYEMNFS LLVEDTLGNI DQPQYRQIVV ELLMVVSIVL ERNPELEFQD
KVDLDRLVKE AFNEFQKDQS RLKEIEKQDD MTSFYNTPPL GKRGTCSYLT KAVMNLLLEG
EVKPNNDDPC LIS
