PHSG_YEAST
ID PHSG_YEAST Reviewed; 902 AA.
AC P06738; D6W4G1;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Glycogen phosphorylase;
DE EC=2.4.1.1;
GN Name=GPH1; OrderedLocusNames=YPR160W; ORFNames=P9584.1;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3537803; DOI=10.1038/324080a0;
RA Hwang P.K., Fletterick R.J.;
RT "Convergent and divergent evolution of regulatory sites in eukaryotic
RT phosphorylases.";
RL Nature 324:80-84(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7871892; DOI=10.1002/yea.320101117;
RA Roemer T.D., Fortin N., Bussey H.;
RT "DNA sequence analysis of a 10.4 kbp region on the right arm of yeast
RT chromosome XVI positions GPH1 and SGV1 adjacent to KRE6, and identifies two
RT novel tRNA genes.";
RL Yeast 10:1527-1530(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 2-10, AND PHOSPHORYLATION AT THR-31.
RX PubMed=1613787; DOI=10.1016/0022-2836(92)90102-p;
RA Rath V.L., Hwang P.K., Fletterick R.J.;
RT "Purification and crystallization of glycogen phosphorylase from
RT Saccharomyces cerevisiae.";
RL J. Mol. Biol. 225:1027-1034(1992).
RN [6]
RP PROTEIN SEQUENCE OF 30-37 AND 737-754, PHOSPHORYLATION AT THR-31, AND
RP PYRIDOXAL PHOSPHATE AT LYS-751.
RX PubMed=1092346; DOI=10.1021/bi00680a031;
RA Lerch K., Fischer E.H.;
RT "Amino acid sequence of two functional sites in yeast glycogen
RT phosphorylase.";
RL Biochemistry 14:2009-2014(1975).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-333, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-333, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-901.
RX PubMed=8703213; DOI=10.1126/science.273.5281.1539;
RA Lin K., Rath V.L., Dai S.C., Fletterick R.J., Hwang P.K.;
RT "A protein phosphorylation switch at the conserved allosteric site in GP.";
RL Science 273:1539-1542(1996).
RN [13]
RP SUBUNIT.
RX PubMed=6354094; DOI=10.1016/0003-9861(83)90078-4;
RA Becker J.U., Wingender-Drissen R., Schiltz E.;
RT "Purification and properties of phosphorylase from baker's yeast.";
RL Arch. Biochem. Biophys. 225:667-678(1983).
CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Activated by phosphorylation of Thr-31.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6354094}.
CC -!- INTERACTION:
CC P06738; P33203: PRP40; NbExp=2; IntAct=EBI-13389, EBI-701;
CC P06738; P39940: RSP5; NbExp=2; IntAct=EBI-13389, EBI-16219;
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28273.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X04604; CAA28273.1; ALT_INIT; Genomic_DNA.
DR EMBL; L33835; AAB59313.1; -; Genomic_DNA.
DR EMBL; U28371; AAB68057.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11577.1; -; Genomic_DNA.
DR PIR; S61144; S61144.
DR RefSeq; NP_015486.1; NM_001184257.1.
DR PDB; 1YGP; X-ray; 2.80 A; A/B=24-902.
DR PDBsum; 1YGP; -.
DR AlphaFoldDB; P06738; -.
DR SMR; P06738; -.
DR BioGRID; 36333; 291.
DR DIP; DIP-2648N; -.
DR IntAct; P06738; 26.
DR MINT; P06738; -.
DR STRING; 4932.YPR160W; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; P06738; -.
DR MaxQB; P06738; -.
DR PaxDb; P06738; -.
DR PRIDE; P06738; -.
DR EnsemblFungi; YPR160W_mRNA; YPR160W; YPR160W.
DR GeneID; 856289; -.
DR KEGG; sce:YPR160W; -.
DR SGD; S000006364; GPH1.
DR VEuPathDB; FungiDB:YPR160W; -.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_0_1; -.
DR InParanoid; P06738; -.
DR OMA; KHKRTFT; -.
DR BioCyc; MetaCyc:YPR160W-MON; -.
DR BioCyc; YEAST:YPR160W-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-70221; Glycogen breakdown (glycogenolysis).
DR EvolutionaryTrace; P06738; -.
DR PRO; PR:P06738; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P06738; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:SGD.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; IMP:SGD.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycogen metabolism; Glycosyltransferase; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1613787"
FT CHAIN 2..902
FT /note="Glycogen phosphorylase"
FT /id="PRO_0000188545"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:1092346,
FT ECO:0000269|PubMed:1613787, ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 751
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 167..168
FT /note="DL -> EG (in Ref. 1; CAA28273 and 2; AAB59313)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="A -> P (in Ref. 1; CAA28273 and 2; AAB59313)"
FT /evidence="ECO:0000305"
FT CONFLICT 440..441
FT /note="VG -> RR (in Ref. 1; CAA28273 and 2; AAB59313)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="A -> V (in Ref. 1; CAA28273 and 2; AAB59313)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="V -> I (in Ref. 1; CAA28273 and 2; AAB59313)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="G -> E (in Ref. 1; CAA28273 and 2; AAB59313)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="V -> L (in Ref. 1; CAA28273 and 2; AAB59313)"
FT /evidence="ECO:0000305"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 88..117
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1YGP"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 244..256
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 277..290
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 297..308
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 345..372
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:1YGP"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 395..406
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 412..422
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 440..446
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 448..468
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 474..479
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 493..500
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 501..508
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 509..517
FT /evidence="ECO:0007829|PDB:1YGP"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 521..527
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 541..544
FT /evidence="ECO:0007829|PDB:1YGP"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 550..559
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 571..582
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 585..607
FT /evidence="ECO:0007829|PDB:1YGP"
FT TURN 608..611
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 624..630
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 638..657
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 662..668
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 672..677
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 685..701
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 721..727
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 732..736
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 747..753
FT /evidence="ECO:0007829|PDB:1YGP"
FT TURN 754..756
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 758..763
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 766..774
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:1YGP"
FT STRAND 779..783
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 786..798
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 805..813
FT /evidence="ECO:0007829|PDB:1YGP"
FT TURN 824..827
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 828..836
FT /evidence="ECO:0007829|PDB:1YGP"
FT TURN 838..841
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 843..863
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 865..879
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:1YGP"
FT HELIX 884..894
FT /evidence="ECO:0007829|PDB:1YGP"
SQ SEQUENCE 902 AA; 103275 MW; F5B6098D69ABAE43 CRC64;
MPPASTSTTN DMITEEPTSP HQIPRLTRRL TGFLPQEIKS IDTMIPLKSR ALWNKHQVKK
FNKAEDFQDR FIDHVETTLA RSLYNCDDMA AYEAASMSIR DNLVIDWNKT QQKFTTRDPK
RVYYLSLEFL MGRALDNALI NMKIEDPEDP AASKGKPREM IKGALDDLGF KLEDVLDQEP
DAGLGNGGLG RLAACFVDSM ATEGIPAWGY GLRYEYGIFA QKIIDGYQVE TPDYWLNSGN
PWEIERNEVQ IPVTFYGYVD RPEGGKTTLS ASQWIGGERV LAVAYDFPVP GFKTSNVNNL
RLWQARPTTE FDFAKFNNGD YKNSVAQQQR AESITAVLYP NDNFAQGKEL RLKQQYFWCA
ASLHDILRRF KKSKRPWTEF PDQVAIQLND THPTLAIVEL QRVLVDLEKL DWHEAWDIVT
KTFAYTNHTV MQEALEKWPV GLFGHLLPRH LEIIYDINWF FLQDVAKKFP KDVDLLSRIS
IIEENSPERQ IRMAFLAIVG SHKVNGVAEL HSELIKTTIF KDFVKFYGPS KFVNVTNGIT
PRRWLKQANP SLAKLISETL NDPTEEYLLD MAKLTQLGKY VEDKEFLKKW NQVKLNNKIR
LVDLIKKEND GVDIINREYL DDTLFDMQVK RIHEYKRQQL NVFGIIYRYL AMKNMLKNGA
SIEEVAKKYP RKVSIFGGKS APGYYMAKLI IKLINCVADI VNNDESIEHL LKVVFVADYN
VSKAEIIIPA SDLSEHISTA GTEASGTSNM KFVMNGGLII GTVDGANVEI TREIGEDNVF
LFGNLSENVE ELRYNHQYHP QDLPSSLDSV LSYIESGQFS PENPNEFKPL VDSIKYHGDY
YLVSDDFESY LATHELVDQE FHNQRSEWLK KSVLSVANVG FFSSDRCIEE YSDTIWNVEP
VT
