UGGG1_RAT
ID UGGG1_RAT Reviewed; 1551 AA.
AC Q9JLA3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase 1;
DE Short=UGT1;
DE Short=rUGT1;
DE EC=2.4.1.- {ECO:0000269|PubMed:1533626};
DE AltName: Full=UDP--Glc:glycoprotein glucosyltransferase;
DE AltName: Full=UDP-glucose ceramide glucosyltransferase-like 1;
DE Flags: Precursor;
GN Name=Uggt1;
GN Synonyms=Gt, Ugcgl1, Uggt {ECO:0000312|EMBL:AAF67072.1}, Ugt1,
GN Ugtr {ECO:0000303|PubMed:11278576};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF67072.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-1551, PROTEIN SEQUENCE OF 43-59; 223-237;
RP 256-267; 293-302; 307-315; 320-328; 440-456; 732-744; 764-776; 779-783;
RP 950-958; 968-972; 1035-1056; 1158-1165; 1170-1179; 1239-1244; 1301-1308;
RP 1314-1319; 1354-1368 AND 1400-1411, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ASP-1358; ASP-1360; GLN-1453 AND ASN-1457.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAF67072.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAF67072.1};
RX PubMed=10764828; DOI=10.1093/glycob/10.4.403;
RA Tessier D.C., Dignard D., Zapun A., Radominska-Pandya A., Parodi A.J.,
RA Bergeron J.J.M., Thomas D.Y.;
RT "Cloning and characterization of mammalian UDP-glucose
RT glycoprotein:glucosyltransferase and the development of a specific
RT substrate for this enzyme.";
RL Glycobiology 10:403-412(2000).
RN [3]
RP PROTEIN SEQUENCE OF 46-54; 950-959; 1028-1034 AND 1273-1283, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 55-75; 554-577; 668-691 AND 890-910, AND INTERACTION
RP WITH SELENOF.
RX PubMed=11278576; DOI=10.1074/jbc.m009861200;
RA Korotkov K.V., Kumaraswamy E., Zhou Y., Hatfield D.L., Gladyshev V.N.;
RT "Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein
RT glucosyltransferase in the endoplasmic reticulum of mammalian cells.";
RL J. Biol. Chem. 276:15330-15336(2001).
RN [5] {ECO:0000305}
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1533626; DOI=10.1016/s0021-9258(19)50413-6;
RA Trombetta S.E., Parodi A.J.;
RT "Purification to apparent homogeneity and partial characterization of rat
RT liver UDP-glucose:glycoprotein glucosyltransferase.";
RL J. Biol. Chem. 267:9236-9240(1992).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11535823; DOI=10.1073/pnas.191359198;
RA Zuber C., Fan J.-Y., Guhl B., Parodi A., Fessler J.H., Parker C., Roth J.;
RT "Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase
RT indicates involvement of pre-Golgi intermediates in protein quality
RT control.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10710-10715(2001).
RN [7]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [8]
RP FUNCTION.
RX PubMed=14730348; DOI=10.1038/nsmb715;
RA Taylor S.C., Ferguson A.D., Bergeron J.J.M., Thomas D.Y.;
RT "The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase
RT modifies substrates distant to local changes in glycoprotein
RT conformation.";
RL Nat. Struct. Mol. Biol. 11:128-134(2004).
RN [9]
RP FUNCTION.
RX PubMed=15861139; DOI=10.1038/sj.emboj.7600645;
RA Ritter C., Quirin K., Kowarik M., Helenius A.;
RT "Minor folding defects trigger local modification of glycoproteins by the
RT ER folding sensor GT.";
RL EMBO J. 24:1730-1738(2005).
CC -!- FUNCTION: Recognizes glycoproteins with minor folding defects.
CC Reglucosylates single N-glycans near the misfolded part of the protein,
CC thus providing quality control for protein folding in the endoplasmic
CC reticulum. Reglucosylated proteins are recognized by calreticulin for
CC recycling to the endoplasmic reticulum and refolding or degradation.
CC {ECO:0000269|PubMed:10764828, ECO:0000269|PubMed:14730348,
CC ECO:0000269|PubMed:15861139}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC mannose isomer 9A1,2,3B1,2,3) + UDP-alpha-D-glucose = H(+) + N(4)-
CC (alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:61304, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:59080, ChEBI:CHEBI:139493;
CC Evidence={ECO:0000269|PubMed:1533626};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:1533626};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44 uM for UDP-glucose (in the presence of 0.5 uM denatured acid
CC phosphatase) {ECO:0000269|PubMed:10764828,
CC ECO:0000269|PubMed:1533626};
CC Vmax=34 pmol/h/mg enzyme toward UDP-glucose (in the presence of 0.5
CC uM denatured acid phosphatase) {ECO:0000269|PubMed:10764828,
CC ECO:0000269|PubMed:1533626};
CC pH dependence:
CC Optimum pH is 7.6-8.0. {ECO:0000269|PubMed:10764828,
CC ECO:0000269|PubMed:1533626};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:1533626}.
CC -!- SUBUNIT: Monomer as well as in a tight complex with SELENOF
CC (PubMed:11278576). Interacts with METTL23 (By similarity). Part of a
CC large chaperone multiprotein complex comprising DNAJB11, HSP90B1,
CC HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small
CC amounts of ERP29, but not, or at very low levels, CALR nor CANX
CC (PubMed:12475965). {ECO:0000250|UniProtKB:Q9NYU2,
CC ECO:0000269|PubMed:11278576, ECO:0000269|PubMed:12475965}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:11535823}. Endoplasmic reticulum-
CC Golgi intermediate compartment {ECO:0000255|PROSITE-ProRule:PRU10138,
CC ECO:0000269|PubMed:11535823}.
CC -!- DOMAIN: N-terminal non-catalytic domain is assumed to mediate
CC recognition of proteins with partial folding defects.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC {ECO:0000269|PubMed:10764828}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67072.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF200359; AAF67072.1; ALT_INIT; mRNA.
DR RefSeq; NP_598280.1; NM_133596.1.
DR RefSeq; XP_006244796.1; XM_006244734.3.
DR AlphaFoldDB; Q9JLA3; -.
DR SMR; Q9JLA3; -.
DR BioGRID; 251136; 1.
DR CORUM; Q9JLA3; -.
DR IntAct; Q9JLA3; 3.
DR STRING; 10116.ENSRNOP00000020558; -.
DR CAZy; GT24; Glycosyltransferase Family 24.
DR GlyGen; Q9JLA3; 4 sites.
DR iPTMnet; Q9JLA3; -.
DR PhosphoSitePlus; Q9JLA3; -.
DR jPOST; Q9JLA3; -.
DR PaxDb; Q9JLA3; -.
DR PRIDE; Q9JLA3; -.
DR Ensembl; ENSRNOT00000020558; ENSRNOP00000020558; ENSRNOG00000014901.
DR GeneID; 171129; -.
DR KEGG; rno:171129; -.
DR UCSC; RGD:619710; rat.
DR CTD; 56886; -.
DR RGD; 619710; Uggt1.
DR eggNOG; KOG1879; Eukaryota.
DR GeneTree; ENSGT00390000004600; -.
DR HOGENOM; CLU_002668_1_1_1; -.
DR InParanoid; Q9JLA3; -.
DR OMA; EFAIDIR; -.
DR OrthoDB; 231263at2759; -.
DR PhylomeDB; Q9JLA3; -.
DR TreeFam; TF300320; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9JLA3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000014901; Expressed in liver and 19 other tissues.
DR Genevisible; Q9JLA3; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0051084; P:'de novo' post-translational protein folding; TAS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; TAS:RGD.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR InterPro; IPR040525; UGGT_TRXL_4.
DR PANTHER; PTHR11226; PTHR11226; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF18403; Thioredoxin_15; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..42
FT /evidence="ECO:0000269|PubMed:10764828"
FT CHAIN 43..1551
FT /note="UDP-glucose:glycoprotein glucosyltransferase 1"
FT /id="PRO_0000012273"
FT REGION 1244..1551
FT /note="Glucosyltransferase"
FT REGION 1531..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1548..1551
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYU2"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1358
FT /note="D->A: Inactive."
FT /evidence="ECO:0000269|PubMed:10764828"
FT MUTAGEN 1360
FT /note="D->A: Inactive."
FT /evidence="ECO:0000269|PubMed:10764828"
FT MUTAGEN 1453
FT /note="Q->A: Less than 2% activity retained."
FT /evidence="ECO:0000269|PubMed:10764828"
FT MUTAGEN 1457
FT /note="N->A: Less than 15% activity retained."
FT /evidence="ECO:0000269|PubMed:10764828"
FT CONFLICT 12
FT /note="A -> C (in Ref. 2; AAF67072)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="S -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..325
FT /note="QD -> MV (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="F -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1165
FT /note="L -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1551 AA; 176431 MW; FD4A1B6BCCBF7738 CRC64;
MCSRGDANAA GAAAARRVTG LCYNMGLLIA LALLCLFSLA EANSKAITTS LTTKWFSAPL
LLEASEFLAE DSQEKFWSFV EASQNIGSSD QHDTDRSYYD AILEAAFRFL SPLQQNLLKF
CLSLRSYSAS IQAFQQIAVD EPPPEGCKSF LSVHGKQTCD LGTLESLLLT APDRPKPLLF
KGDHRYPSSN PESPVVIFYS EIGHEEFSNI HHQLISKSNE GKINYVFRHY ISNPRKEPVH
LSGYGVELAI KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RELYPSLEGQ
LKEFRKHLVE STNEMAPLKV WQLQDLSFQT AARILAAPVE LALVVMKDIS QNFPTKARAI
TKTAVSAQLR AEVEENQKYF KGTIGLQPGD SALFINGLHI DLDTQDIFSL FDTLRNEARV
MEGLHRLGIE GLSLHNILKL NIQPSETDYA VDIRSPAISW VNNLEVDSRY NSWPSSLQEL
LRPTFPGVIR QIRKNLHNMV FIVDPVHETT AELVSIAEMF LSNHIPLRIG FIFVVNDSED
VDGMQDAGVA VLRAYNYVGQ EVDGYHAFQT LTQIYNKVRT GEKVKVEHVV SVLEKKYPYV
EVNSILGIDS AYDQNRKEAR GYYEQTGVGP LPVVLFNGMP FEKEQLDPDE LETITMHKIL
ETTTFFQRAV YLGELSHDQD VVEYIMNQPN VVPRINSRIL TAKREYLDLT ASNNFYVDDF
ARFSALDSRG KTAAIANSMN YLTKKGMSSK EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD
AIKHQKTSNN VRISMINNPS REISDSSTPV SRAIWAALQT QTSNSAKNFI TKMVKEETAE
ALAAGVDIGE FSVGGMDVSL FKEVFESSRM DFILSHALYC RDVLKLKKGQ RVVISNGRII
GPLEDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV DALLSAQPKG
EARIEYQFFE DKHSAIKLKP KEGETYYDVV AVVDPVTREA QRLAPLLLVL AQLINMSLRV
FMNCQSKLSD MPLKSFYRYV LEPEISFTAD NSFAKGPIAK FLDMPQSPLF TLNLNTPESW
MVESVRTPYD LDNIYLEEVD SIVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP
TTVDTIVMAN LGYFQLKANP GAWILRLRKG RSDDIYRIYS HDGTDSPPDA NDVVVILNNF
KSKIIKVKVQ KKADMANEDL LSDGTNENES GFWDSFKWGF SGQKTEEVKQ DKDDIINIFS
VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK EFIPYMAKKY NFQYELVQYK
WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY
GYTPFCDSRR EMDGYRFWKS GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG
LSQDPNSLSN LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE
PKLEAAVRIV PEWQDYDQEI KQLQTLFQEE KELGTLHEEE TQEGSQKHEE L
