ID   UGPA1_YEAST             Reviewed;         499 AA.
AC   P32861; D6VXQ0;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000305};
DE            EC=2.7.7.9 {ECO:0000269|PubMed:7588797};
DE   AltName: Full=UDP-glucose pyrophosphorylase {ECO:0000303|PubMed:7588797};
DE            Short=UDPGP {ECO:0000303|PubMed:7588797};
DE            Short=UGPase {ECO:0000303|PubMed:7588797};
GN   Name=UGP1 {ECO:0000303|PubMed:7588797}; OrderedLocusNames=YKL035W;
GN   ORFNames=YKL248;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1481573; DOI=10.1002/yea.320081108;
RA   Purnelle B., Skala J., van Dyck L., Goffeau A.;
RT   "The sequence of a 12 kb fragment on the left arm of yeast chromosome XI
RT   reveals five new open reading frames, including a zinc finger protein and a
RT   homolog of the UDP-glucose pyrophosphorylase from potato.";
RL   Yeast 8:977-986(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
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   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=7588797; DOI=10.1111/j.1432-1033.1995.520_2.x;
RA   Daran J.M., Dallies N., Thines-Sempoux D., Paquet V., Francois J.;
RT   "Genetic and biochemical characterization of the UGP1 gene encoding the
RT   UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae.";
RL   Eur. J. Biochem. 233:520-530(1995).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   IDENTIFICATION BY 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-19 AND SER-21, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP   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   [9]
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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [11]
RP   METHYLATION AT ARG-369.
RX   PubMed=23865587; DOI=10.1021/pr400556c;
RA   Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.;
RT   "Analysis of the proteome of Saccharomyces cerevisiae for methylarginine.";
RL   J. Proteome Res. 12:3884-3899(2013).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 12-499, SUBUNIT, OLIGOMERIZATION
RP   REGION, AND PROBABLE MAGNESIUM-BINDING SITES.
RX   PubMed=17010990; DOI=10.1016/j.jmb.2006.08.079;
RA   Roeben A., Plitzko J.M., Korner R., Bottcher U.M., Siegers K.,
RA   Hayer-Hartl M., Bracher A.;
RT   "Structural basis for subunit assembly in UDP-glucose pyrophosphorylase
RT   from Saccharomyces cerevisiae.";
RL   J. Mol. Biol. 364:551-560(2006).
CC   -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC       metabolic pathways. {ECO:0000269|PubMed:7588797}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-
CC         alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601,
CC         ChEBI:CHEBI:58885; EC=2.7.7.9; Evidence={ECO:0000269|PubMed:7588797};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:17010990}.
CC   -!- INTERACTION:
CC       P32861; P31374: PSK1; NbExp=3; IntAct=EBI-19987, EBI-9442;
CC       P32861; Q08217: PSK2; NbExp=3; IntAct=EBI-19987, EBI-9839;
CC   -!- MISCELLANEOUS: Present with 17200 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR   EMBL; X69584; CAA49303.1; -; Genomic_DNA.
DR   EMBL; Z28035; CAA81872.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09120.1; -; Genomic_DNA.
DR   PIR; S30007; S30007.
DR   RefSeq; NP_012889.3; NM_001179601.3.
DR   PDB; 2I5K; X-ray; 3.10 A; A/B=12-499.
DR   PDBsum; 2I5K; -.
DR   AlphaFoldDB; P32861; -.
DR   SMR; P32861; -.
DR   BioGRID; 34096; 184.
DR   DIP; DIP-4534N; -.
DR   IntAct; P32861; 42.
DR   MINT; P32861; -.
DR   STRING; 4932.YKL035W; -.
DR   GlyGen; P32861; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P32861; -.
DR   MaxQB; P32861; -.
DR   PaxDb; 4932-YKL035W; -.
DR   PeptideAtlas; P32861; -.
DR   EnsemblFungi; YKL035W_mRNA; YKL035W; YKL035W.
DR   GeneID; 853830; -.
DR   KEGG; sce:YKL035W; -.
DR   AGR; SGD:S000001518; -.
DR   SGD; S000001518; UGP1.
DR   VEuPathDB; FungiDB:YKL035W; -.
DR   eggNOG; KOG2638; Eukaryota.
DR   GeneTree; ENSGT00940000153464; -.
DR   HOGENOM; CLU_023632_3_0_1; -.
DR   InParanoid; P32861; -.
DR   OMA; KEYCFLS; -.
DR   OrthoDB; 45684at2759; -.
DR   BioCyc; MetaCyc:YKL035W-MONOMER; -.
DR   BioCyc; YEAST:YKL035W-MONOMER; -.
DR   BRENDA; 2.7.7.9; 984.
DR   Reactome; R-SCE-173599; Formation of the active cofactor, UDP-glucuronate.
DR   Reactome; R-SCE-3322077; Glycogen synthesis.
DR   BioGRID-ORCS; 853830; 4 hits in 10 CRISPR screens.
DR   ChiTaRS; UGP1; yeast.
DR   EvolutionaryTrace; P32861; -.
DR   PRO; PR:P32861; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P32861; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070569; F:uridylyltransferase activity; IDA:SGD.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IMP:SGD.
DR   GO; GO:0006078; P:(1->6)-beta-D-glucan biosynthetic process; IMP:SGD.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IMP:SGD.
DR   GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IGI:SGD.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IMP:SGD.
DR   CDD; cd00897; UGPase_euk; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR002618; UDPGP_fam.
DR   InterPro; IPR016267; UDPGP_trans.
DR   PANTHER; PTHR43511; -; 1.
DR   PANTHER; PTHR43511:SF4; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01704; UDPGP; 1.
DR   PIRSF; PIRSF000806; UDPGP; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Magnesium; Metal-binding; Methylation;
KW   Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..499
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000185765"
FT   REGION          448..499
FT                   /note="Oligomerization"
FT   ACT_SITE        388
FT                   /evidence="ECO:0000305"
FT   BINDING         109..112
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         111..112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         123
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         186
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         215
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         244..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         246
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         388
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         19
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         369
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000269|PubMed:23865587"
FT   HELIX           23..30
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           49..67
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   TURN            82..84
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           88..92
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           134..149
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          154..158
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   TURN            161..163
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           164..171
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          176..178
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          202..206
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           216..218
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           219..226
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           228..234
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          239..243
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           254..262
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          266..273
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          279..281
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          283..287
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           304..307
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   TURN            310..312
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          315..324
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           325..333
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           364..370
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          371..373
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          375..379
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           381..383
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           390..396
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          401..404
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          407..410
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          420..423
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           425..427
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   HELIX           430..436
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          446..457
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          462..470
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          477..479
FT                   /evidence="ECO:0007829|PDB:2I5K"
FT   STRAND          484..498
FT                   /evidence="ECO:0007829|PDB:2I5K"
SQ   SEQUENCE   499 AA;  55988 MW;  9B9F4BED885E004D CRC64;
     MSTKKHTKTH STYAFESNTN SVAASQMRNA LNKLADSSKL DDAARAKFEN ELDSFFTLFR
     RYLVEKSSRT TLEWDKIKSP NPDEVVKYEI ISQQPENVSN LSKLAVLKLN GGLGTSMGCV
     GPKSVIEVRE GNTFLDLSVR QIEYLNRQYD SDVPLLLMNS FNTDKDTEHL IKKYSANRIR
     IRSFNQSRFP RVYKDSLLPV PTEYDSPLDA WYPPGHGDLF ESLHVSGELD ALIAQGREIL
     FVSNGDNLGA TVDLKILNHM IETGAEYIME LTDKTRADVK GGTLISYDGQ VRLLEVAQVP
     KEHIDEFKNI RKFTNFNTNN LWINLKAVKR LIESSNLEME IIPNQKTITR DGHEINVLQL
     ETACGAAIRH FDGAHGVVVP RSRFLPVKTC SDLLLVKSDL FRLEHGSLKL DPSRFGPNPL
     IKLGSHFKKV SGFNARIPHI PKIVELDHLT ITGNVFLGKD VTLRGTVIIV CSDGHKIDIP
     NGSILENVVV TGNLQILEH
//