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   24-JAN-2024, entry version 143.
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, Ugtr
GN   {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)-beta-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)-beta-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   GlyCosmos; Q9JLA3; 4 sites, No reported glycans.
DR   GlyGen; Q9JLA3; 4 sites.
DR   iPTMnet; Q9JLA3; -.
DR   PhosphoSitePlus; Q9JLA3; -.
DR   jPOST; Q9JLA3; -.
DR   PaxDb; 10116-ENSRNOP00000020558; -.
DR   Ensembl; ENSRNOT00000020558.6; ENSRNOP00000020558.3; ENSRNOG00000014901.6.
DR   Ensembl; ENSRNOT00055032617; ENSRNOP00055026419; ENSRNOG00055019007.
DR   Ensembl; ENSRNOT00060031338; ENSRNOP00060025426; ENSRNOG00060017900.
DR   Ensembl; ENSRNOT00065017860; ENSRNOP00065013654; ENSRNOG00065010911.
DR   GeneID; 171129; -.
DR   KEGG; rno:171129; -.
DR   UCSC; RGD:619710; rat.
DR   AGR; RGD:619710; -.
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   OrthoDB; 1734at2759; -.
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 cell types or tissues.
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   CDD; cd06432; GT8_HUGT1_C_like; 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; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11226:SF3; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 1; 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; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   Genevisible; Q9JLA3; RN.
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
//