UGGG2_HUMAN
ID UGGG2_HUMAN Reviewed; 1516 AA.
AC Q9NYU1; A6NKL4; Q08AD0; Q5JQR8; Q8N5K0; Q9UFC4;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase 2;
DE Short=UGT2;
DE Short=hUGT2;
DE EC=2.4.1.- {ECO:0000269|PubMed:24415556};
DE AltName: Full=UDP--Glc:glycoprotein glucosyltransferase 2;
DE AltName: Full=UDP-glucose ceramide glucosyltransferase-like 1;
DE Flags: Precursor;
GN Name=UGGT2; Synonyms=UGCGL2, UGT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP THR-323; ALA-328; THR-821 AND LEU-994.
RC TISSUE=Fetal liver;
RX PubMed=10694380; DOI=10.1021/bi9916473;
RA Arnold S.M., Fessler L.I., Fessler J.H., Kaufman R.J.;
RT "Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase
RT differ in mRNA expression and enzymatic activity.";
RL Biochemistry 39:2149-2163(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ALA-328 AND LEU-994.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-1516 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12913004; DOI=10.1074/jbc.m305800200;
RA Arnold S.M., Kaufman R.J.;
RT "The noncatalytic portion of human UDP-glucose: glycoprotein
RT glucosyltransferase I confers UDP-glucose binding and transferase function
RT to the catalytic domain.";
RL J. Biol. Chem. 278:43320-43328(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INTERACTION WITH METTL23.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, INTERACTION
RP WITH SELENOF, AND MUTAGENESIS OF ASP-1333.
RX PubMed=24415556; DOI=10.1093/glycob/cwt163;
RA Takeda Y., Seko A., Hachisu M., Daikoku S., Izumi M., Koizumi A.,
RA Fujikawa K., Kajihara Y., Ito Y.;
RT "Both isoforms of human UDP-glucose:glycoprotein glucosyltransferase are
RT enzymatically active.";
RL Glycobiology 24:344-350(2014).
RN [10]
RP VARIANT ALA-328.
RX PubMed=28686597; DOI=10.1371/journal.pgen.1006897;
RA Klar J., Piontek J., Milatz S., Tariq M., Jameel M., Breiderhoff T.,
RA Schuster J., Fatima A., Asif M., Sher M., Maebert K., Fromm A., Baig S.M.,
RA Guenzel D., Dahl N.;
RT "Altered paracellular cation permeability due to a rare CLDN10B variant
RT causes anhidrosis and kidney damage.";
RL PLoS Genet. 13:E1006897-E1006897(2017).
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:24415556}.
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:24415556};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q09140};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q09140};
CC -!- ACTIVITY REGULATION: Ethylenediaminetetraacetic acid completely
CC abolishes catalytic activity (PubMed:24415556). Catalytic activity is
CC enhanced by complex formation with SELENOF (PubMed:24415556).
CC {ECO:0000269|PubMed:24415556}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:24415556}.
CC -!- SUBUNIT: Interacts with METTL23 (PubMed:23349634). Interacts with
CC SELENOF (PubMed:24415556). {ECO:0000269|PubMed:23349634,
CC ECO:0000269|PubMed:24415556}.
CC -!- INTERACTION:
CC Q9NYU1; Q92624: APPBP2; NbExp=3; IntAct=EBI-1054215, EBI-743771;
CC Q9NYU1; P0DTC6: 6; Xeno; NbExp=3; IntAct=EBI-1054215, EBI-25475897;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:12913004}. Endoplasmic reticulum-
CC Golgi intermediate compartment {ECO:0000255|PROSITE-ProRule:PRU10138,
CC ECO:0000269|PubMed:12913004}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYU1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYU1-2; Sequence=VSP_056319, VSP_056320;
CC -!- TISSUE SPECIFICITY: Higher levels in kidney, pancreas, heart, and
CC skeletal muscle. {ECO:0000269|PubMed:10694380}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC -!- CAUTION: Has no enzymatic activity towards unfolded RNase B or
CC thyroglobulin. {ECO:0000305|PubMed:10694380}.
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DR EMBL; AF227906; AAF66233.2; -; mRNA.
DR EMBL; AL136104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL607038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032302; AAH32302.1; -; mRNA.
DR EMBL; BC125233; AAI25234.1; -; mRNA.
DR EMBL; AL133051; CAB61378.1; -; mRNA.
DR CCDS; CCDS9480.1; -. [Q9NYU1-1]
DR PIR; T42654; T42654.
DR RefSeq; NP_064506.3; NM_020121.3. [Q9NYU1-1]
DR AlphaFoldDB; Q9NYU1; -.
DR SMR; Q9NYU1; -.
DR BioGRID; 120875; 139.
DR IntAct; Q9NYU1; 14.
DR MINT; Q9NYU1; -.
DR STRING; 9606.ENSP00000365938; -.
DR CAZy; GT24; Glycosyltransferase Family 24.
DR GlyConnect; 1872; 3 N-Linked glycans (1 site).
DR GlyGen; Q9NYU1; 5 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9NYU1; -.
DR PhosphoSitePlus; Q9NYU1; -.
DR BioMuta; UGGT2; -.
DR DMDM; 311033544; -.
DR EPD; Q9NYU1; -.
DR jPOST; Q9NYU1; -.
DR MassIVE; Q9NYU1; -.
DR MaxQB; Q9NYU1; -.
DR PaxDb; Q9NYU1; -.
DR PeptideAtlas; Q9NYU1; -.
DR PRIDE; Q9NYU1; -.
DR ProteomicsDB; 72070; -.
DR ProteomicsDB; 83276; -. [Q9NYU1-1]
DR Antibodypedia; 24874; 135 antibodies from 21 providers.
DR DNASU; 55757; -.
DR Ensembl; ENST00000376714.7; ENSP00000365904.3; ENSG00000102595.21. [Q9NYU1-2]
DR Ensembl; ENST00000376747.8; ENSP00000365938.3; ENSG00000102595.21. [Q9NYU1-1]
DR Ensembl; ENST00000621375.5; ENSP00000482021.2; ENSG00000102595.21. [Q9NYU1-2]
DR GeneID; 55757; -.
DR KEGG; hsa:55757; -.
DR MANE-Select; ENST00000376747.8; ENSP00000365938.3; NM_020121.4; NP_064506.3.
DR UCSC; uc001vmt.5; human. [Q9NYU1-1]
DR CTD; 55757; -.
DR DisGeNET; 55757; -.
DR GeneCards; UGGT2; -.
DR HGNC; HGNC:15664; UGGT2.
DR HPA; ENSG00000102595; Low tissue specificity.
DR MIM; 605898; gene.
DR neXtProt; NX_Q9NYU1; -.
DR OpenTargets; ENSG00000102595; -.
DR PharmGKB; PA38015; -.
DR VEuPathDB; HostDB:ENSG00000102595; -.
DR eggNOG; KOG1879; Eukaryota.
DR GeneTree; ENSGT00390000004600; -.
DR HOGENOM; CLU_002668_1_1_1; -.
DR InParanoid; Q9NYU1; -.
DR OMA; PQGLQFT; -.
DR OrthoDB; 231263at2759; -.
DR PhylomeDB; Q9NYU1; -.
DR TreeFam; TF300320; -.
DR PathwayCommons; Q9NYU1; -.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR SignaLink; Q9NYU1; -.
DR SIGNOR; Q9NYU1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 55757; 8 hits in 1082 CRISPR screens.
DR ChiTaRS; UGGT2; human.
DR GenomeRNAi; 55757; -.
DR Pharos; Q9NYU1; Tbio.
DR PRO; PR:Q9NYU1; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9NYU1; protein.
DR Bgee; ENSG00000102595; Expressed in calcaneal tendon and 183 other tissues.
DR ExpressionAtlas; Q9NYU1; baseline and differential.
DR Genevisible; Q9NYU1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
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 Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1516
FT /note="UDP-glucose:glycoprotein glucosyltransferase 2"
FT /id="PRO_0000012274"
FT REGION 1220..1516
FT /note="Glucosyltransferase"
FT MOTIF 1513..1516
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT MOD_RES 1289
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 950
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 278
FT /note="E -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056319"
FT VAR_SEQ 279..1516
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056320"
FT VARIANT 323
FT /note="A -> T (in dbSNP:rs12863903)"
FT /evidence="ECO:0000269|PubMed:10694380"
FT /id="VAR_030006"
FT VARIANT 328
FT /note="S -> A (in dbSNP:rs816142)"
FT /evidence="ECO:0000269|PubMed:10694380,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:28686597"
FT /id="VAR_030007"
FT VARIANT 821
FT /note="A -> T (in dbSNP:rs33949518)"
FT /evidence="ECO:0000269|PubMed:10694380"
FT /id="VAR_055849"
FT VARIANT 865
FT /note="K -> R (in dbSNP:rs35060832)"
FT /id="VAR_061196"
FT VARIANT 924
FT /note="F -> I (in dbSNP:rs35780499)"
FT /id="VAR_055850"
FT VARIANT 994
FT /note="M -> L (in dbSNP:rs12876018)"
FT /evidence="ECO:0000269|PubMed:10694380,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_030008"
FT VARIANT 1274
FT /note="F -> L (in dbSNP:rs9525072)"
FT /id="VAR_055851"
FT VARIANT 1285
FT /note="Y -> F (in dbSNP:rs35123499)"
FT /id="VAR_061197"
FT MUTAGEN 1333
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24415556"
SQ SEQUENCE 1516 AA; 174735 MW; BD216896ECA54E4F CRC64;
MAPAKATNVV RLLLGSTALW LSQLGSGTVA ASKSVTAHLA AKWPETPLLL EASEFMAEES
NEKFWQFLET VQELAIYKQT ESDYSYYNLI LKKAGQFLDN LHINLLKFAF SIRAYSPAIQ
MFQQIAADEP PPDGCNAFVV IHKKHTCKIN EIKKLLKKAA SRTRPYLFKG DHKFPTNKEN
LPVVILYAEM GTRTFSAFHK VLSEKAQNEE ILYVLRHYIQ KPSSRKMYLS GYGVELAIKS
TEYKALDDTQ VKTVTNTTVE DETETNEVQG FLFGKLKEIY SDLRDNLTAF QKYLIESNKQ
MMPLKVWELQ DLSFQAASQI MSAPVYDSIK LMKDISQNFP IKARSLTRIA VNQHMREEIK
ENQKDLQVRF KIQPGDARLF INGLRVDMDV YDAFSILDML KLEGKMMNGL RNLGINGEDM
SKFLKLNSHI WEYTYVLDIR HSSIMWINDL ENDDLYITWP TSCQKLLKPV FPGSVPSIRR
NFHNLVLFID PAQEYTLDFI KLADVFYSHE VPLRIGFVFI LNTDDEVDGA NDAGVALWRA
FNYIAEEFDI SEAFISIVHM YQKVKKDQNI LTVDNVKSVL QNTFPHANIW DILGIHSKYD
EERKAGASFY KMTGLGPLPQ ALYNGEPFKH EEMNIKELKM AVLQRMMDAS VYLQREVFLG
TLNDRTNAID FLMDRNNVVP RINTLILRTN QQYLNLISTS VTADVEDFST FFFLDSQDKS
AVIAKNMYYL TQDDESIISA VTLWIIADFD KPSGRKLLFN ALKHMKTSVH SRLGIIYNPT
SKINEENTAI SRGILAAFLT QKNMFLRSFL GQLAKEEIAT AIYSGDKIKT FLIEGMDKNA
FEKKYNTVGV NIFRTHQLFC QDVLKLRPGE MGIVSNGRFL GPLDEDFYAE DFYLLEKITF
SNLGEKIKGI VENMGINANN MSDFIMKVDA LMSSVPKRAS RYDVTFLREN HSVIKTNPQE
NDMFFNVIAI VDPLTREAQK MAQLLVVLGK IINMKIKLFM NCRGRLSEAP LESFYRFVLE
PELMSGANDV SSLGPVAKFL DIPESPLLIL NMITPEGWLV ETVHSNCDLD NIHLKDTEKT
VTAEYELEYL LLEGQCFDKV TEQPPRGLQF TLGTKNKPAV VDTIVMAHHG YFQLKANPGA
WILRLHQGKS EDIYQIVGHE GTDSQADLED IIVVLNSFKS KILKVKVKKE TDKIKEDILT
DEDEKTKGLW DSIKSFTVSL HKENKKEKDV LNIFSVASGH LYERFLRIMM LSVLRNTKTP
VKFWLLKNYL SPTFKEVIPH MAKEYGFRYE LVQYRWPRWL RQQTERQRII WGYKILFLDV
LFPLAVDKII FVDADQIVRH DLKELRDFDL DGAPYGYTPF CDSRREMDGY RFWKTGYWAS
HLLRRKYHIS ALYVVDLKKF RRIGAGDRLR SQYQALSQDP NSLSNLDQDL PNNMIYQVAI
KSLPQDWLWC ETWCDDESKQ RAKTIDLCNN PKTKESKLKA AARIVPEWVE YDAEIRQLLD
HLENKKQDTI LTHDEL
