UGGG_DROME
ID UGGG_DROME Reviewed; 1548 AA.
AC Q09332; B5RIN4; Q95U28; Q9VVT7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase {ECO:0000312|FlyBase:FBgn0014075};
DE Short=UGT;
DE Short=dUGT {ECO:0000303|PubMed:7729408};
DE EC=2.4.1.- {ECO:0000269|PubMed:22960071, ECO:0000269|PubMed:7729408};
DE AltName: Full=UDP--Glc:glycoprotein glucosyltransferase;
DE Flags: Precursor;
GN Name=Uggt {ECO:0000312|FlyBase:FBgn0014075};
GN Synonyms=GT {ECO:0000312|FlyBase:FBgn0014075},
GN UGGG {ECO:0000312|FlyBase:FBgn0014075},
GN Ugt {ECO:0000312|FlyBase:FBgn0014075};
GN ORFNames=CG6850 {ECO:0000312|FlyBase:FBgn0014075};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-37, CATALYTIC ACTIVITY,
RP PATHWAY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=7729408; DOI=10.1002/j.1460-2075.1995.tb07115.x;
RA Parker C.G., Fessler L.I., Nelson R.E., Fessler J.H.;
RT "Drosophila UDP-glucose:glycoprotein glucosyltransferase: sequence and
RT characterization of an enzyme that distinguishes between denatured and
RT native proteins.";
RL EMBO J. 14:1294-1303(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND 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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22960071; DOI=10.1016/j.bbrc.2012.08.112;
RA Sakono M., Seko A., Takeda Y., Hachisu M., Ito Y.;
RT "Biophysical properties of UDP-glucose:glycoprotein glucosyltransferase, a
RT folding sensor enzyme in the ER, delineated by synthetic probes.";
RL Biochem. Biophys. Res. Commun. 426:504-510(2012).
RN [8]
RP SUBUNIT, INTERACTION WITH CG7484, AND MUTAGENESIS OF 262-GLU--GLY-272;
RP 274-ASP--HIS-282; 285-LEU--ARG-295 AND 298-GLN--GLN-305.
RX PubMed=28490633; DOI=10.1074/jbc.m117.789495;
RA Calles-Garcia D., Yang M., Soya N., Melero R., Menade M., Ito Y.,
RA Vargas J., Lukacs G.L., Kollman J.M., Kozlov G., Gehring K.;
RT "Single-particle electron microscopy structure of UDP-glucose:glycoprotein
RT glucosyltransferase suggests a selectivity mechanism for misfolded
RT proteins.";
RL J. Biol. Chem. 292:11499-11507(2017).
CC -!- FUNCTION: Recognizes glycoproteins with minor folding defects
CC (PubMed:22960071). Reglucosylates single N-glycans near the misfolded
CC part of the protein, thus providing quality control for protein folding
CC in the endoplasmic reticulum (PubMed:22960071). Reglucosylated proteins
CC are recognized by calreticulin for recycling to the endoplasmic
CC reticulum and refolding or degradation (PubMed:11535823).
CC {ECO:0000269|PubMed:11535823, ECO:0000269|PubMed:22960071}.
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:22960071, ECO:0000269|PubMed:7729408};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:7729408};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:7729408};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=69 uM for Man9GlcNAc2 (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:22960071};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:7729408}.
CC -!- SUBUNIT: Monomer (PubMed:28490633). May interact with CG7484/Sep15
CC (Probable). {ECO:0000269|PubMed:28490633, ECO:0000305|PubMed:28490633}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:11535823, ECO:0000269|PubMed:7729408}. Endoplasmic
CC reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:11535823}.
CC -!- DEVELOPMENTAL STAGE: Expressed in salivary glands (at protein level)
CC (PubMed:11535823). Is present at low but detectable levels in the
CC earliest embryos, increasing at 6-8 hours with a maximum at 10-12 hours
CC (PubMed:7729408). Levels decrease thereafter and are not detected in
CC 18-20 hours embryos and first instar larvae but is detected again at
CC second instar to pupation (PubMed:7729408).
CC {ECO:0000269|PubMed:11535823, ECO:0000269|PubMed:7729408}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13582.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U20554; AAA85850.1; -; mRNA.
DR EMBL; AE014296; AAF49220.1; -; Genomic_DNA.
DR EMBL; AY058353; AAL13582.1; ALT_FRAME; mRNA.
DR EMBL; BT044158; ACH92223.1; -; mRNA.
DR PIR; S54723; S54723.
DR RefSeq; NP_524151.2; NM_079427.3.
DR AlphaFoldDB; Q09332; -.
DR SMR; Q09332; -.
DR BioGRID; 65336; 13.
DR IntAct; Q09332; 3.
DR STRING; 7227.FBpp0074831; -.
DR CAZy; GT24; Glycosyltransferase Family 24.
DR GlyGen; Q09332; 3 sites.
DR PaxDb; Q09332; -.
DR PRIDE; Q09332; -.
DR EnsemblMetazoa; FBtr0075064; FBpp0074831; FBgn0014075.
DR GeneID; 40055; -.
DR KEGG; dme:Dmel_CG6850; -.
DR CTD; 40055; -.
DR FlyBase; FBgn0014075; Uggt.
DR VEuPathDB; VectorBase:FBgn0014075; -.
DR eggNOG; KOG1879; Eukaryota.
DR GeneTree; ENSGT00390000004600; -.
DR HOGENOM; CLU_002668_1_1_1; -.
DR InParanoid; Q09332; -.
DR OMA; EFAIDIR; -.
DR OrthoDB; 231263at2759; -.
DR PhylomeDB; Q09332; -.
DR SignaLink; Q09332; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 40055; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Ugt; fly.
DR GenomeRNAi; 40055; -.
DR PRO; PR:Q09332; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0014075; Expressed in embryonic/larval hemocyte (Drosophila) and 25 other tissues.
DR Genevisible; Q09332; DM.
DR GO; GO:0005737; C:cytoplasm; TAS:FlyBase.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IDA:FlyBase.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Reference proteome; Signal; Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:7729408"
FT CHAIN 23..1548
FT /note="UDP-glucose:glycoprotein glucosyltransferase"
FT /id="PRO_0000012270"
FT REGION 243..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1548
FT /note="Glucosyltransferase"
FT /evidence="ECO:0000250"
FT REGION 1512..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1545..1548
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 262..272
FT /note="Missing: Abolishes binding to human SELENOF/SEP15."
FT /evidence="ECO:0000269|PubMed:28490633"
FT MUTAGEN 274..282
FT /note="Missing: Reduces binding to human SELENOF/SEP15."
FT /evidence="ECO:0000269|PubMed:28490633"
FT MUTAGEN 285..295
FT /note="Missing: Reduces binding human SELENOF/SEP15."
FT /evidence="ECO:0000269|PubMed:28490633"
FT MUTAGEN 298..305
FT /note="Missing: Destabilizes protein structure and targets
FT it for degradation."
FT /evidence="ECO:0000269|PubMed:28490633"
FT CONFLICT 166
FT /note="S -> P (in Ref. 1; AAA85850)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="G -> E (in Ref. 1; AAA85850)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="A -> T (in Ref. 1; AAA85850)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="N -> K (in Ref. 1; AAA85850)"
FT /evidence="ECO:0000305"
FT CONFLICT 1233
FT /note="T -> S (in Ref. 1; AAA85850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1548 AA; 174354 MW; 87D782E7B27E0EE9 CRC64;
MLRAVALCVS VVLIALYTPT SGESSQSYPI TTLINAKWTQ TPLYLEIAEY LADEQAGLFW
DYVSGVTKLD TVLNEYDTES QQYNAALELV KSHVSSPQLP LLRLVVSMHS LTPRIQTHFQ
LAEELRSSGS CQSFTFAQVG SELACSFNEL QKKLEVPLAK DSLDASVVTY SFDHIFPGSE
NNTRTVVLYG DLGSSQFRTY HKLLEKEANA GRIRYILRHQ LAKKDKRPVR LSGYGVELHL
KSTEYKSQDD APKPEAGSTS DEDLANESDV QGFDFKVLKQ KHPTLKRALD QLRQRLLQGN
DEIAQLKAWE FQDLGLQAAA AIAEIQGDET LQILQYTAHN FPMLARTLLA HKVTDGLRAE
VKHNTEAFGR SLNVAPPDGA LFINGLFFDA DTMDLYSLIE TLRSEMRVLE SLHSNNVRGS
LASSLLALDL TASSKKEFAI DIRDTAVQWV NDIENDVQYR RWPSSVMDLL RPTFPGMLRN
IRKNVFNLVL VVDALQPTAR SVIKLSESFV IHQAPIRLGL VFDARDANED NLADYVAITC
AYNYVSQKKD ARAALSFLTD IYAAVGETKV VTKKDIVKQL TKEFTSLSFA KAEEFLEEDS
TYDYGRELAA EFIQRLGFGD KGQPQALLNG VPMPSNVVTA DSDFEEAIFT EIMTHTSNLQ
KAVYKGELTD NDVAIDYLMN QPHVMPRLNQ RILSQEDVKY LDINGVAYKN LGNVGVLNRL
SNRDMTATLM DNLKYFGGKK STELIGRASL QFLTIWVFAD LETDQGRDLL THALDYVQSG
ESVRVAFIPN TESSSASSRR NLNRLVWAAM QSLPPTQATE QVLKWLKKPK EKIEIPTQLE
DILGSTELHL KMLRVYSQRV LGLNKSQRLV IGNGRLYGPL SSDESFDSAD FALLARFSSL
QYSDKVRQVL KESAQDVNEE FNSDTLLKLY ASLLPRQTKT RFKLPTDLKT DHSVVKLPPK
QENLPHFDVA AVLDPASRAA QKLTPILILL RQVLNCQLNL YLIPVPQHSD MPVKNFYRYV
VEPEVQFEAN GGRSDGPLAK FSGLPANPLL TQQLQVPENW LVEAVRAVYD LDNIKLTDIG
GPVHSEFDLE YLLLEGHCFD AASGAPPRGL QLVLGTQSQP TLVDTIVMAN LGYFQLKANP
GAWSLRLREG KSADIYAISH IEGTNTHHSA GSSEVQVLIT SLRSHVVKLR VSKKPGMQQA
ELLSDDNEQA AQSGMWNSIA SSFGGGSANQ AATDEDTETI NIFSVASGHL YERLLRIMMV
SLLKHTKSPV KFWFLKNYLS PQFTDFLPHM ASEYNFQYEL VQYKWPRWLH QQTEKQRTIW
GYKILFLDVL FPLNVRKIIF VDADAIVRTD IKELYDMDLG GAPYAYTPFC DSRKEMEGFR
FWKQGYWRSH LMGRRYHISA LYVVDLKRFR KIAAGDRLRG QYQALSQDPN SLSNLDQDLP
NNMIHQVAIK SLPDDWLWCQ TWCSDSNFKT AKVIDLCNNP QTKEAKLTAA QRIVPEWKDY
DAELKTLMSR IEDHENSHSR DSAVDDSVDD SVEVTTVTPS HEPKHGEL
