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   27-MAR-2024, entry version 192.
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)-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: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; 148.
DR   IntAct; Q9NYU1; 16.
DR   MINT; Q9NYU1; -.
DR   STRING; 9606.ENSP00000365938; -.
DR   CAZy; GT24; Glycosyltransferase Family 24.
DR   GlyConnect; 1872; 3 N-Linked glycans (1 site).
DR   GlyCosmos; Q9NYU1; 4 sites, 3 glycans.
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; 9606-ENSP00000365938; -.
DR   PeptideAtlas; Q9NYU1; -.
DR   ProteomicsDB; 72070; -.
DR   ProteomicsDB; 83276; -. [Q9NYU1-1]
DR   Pumba; Q9NYU1; -.
DR   Antibodypedia; 24874; 159 antibodies from 21 providers.
DR   DNASU; 55757; -.
DR   Ensembl; ENST00000376714.7; ENSP00000365904.3; ENSG00000102595.22. [Q9NYU1-2]
DR   Ensembl; ENST00000376747.8; ENSP00000365938.3; ENSG00000102595.22. [Q9NYU1-1]
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   AGR; HGNC:15664; -.
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; FQTHQLF; -.
DR   OrthoDB; 1734at2759; -.
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; 11 hits in 1164 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 185 other cell types or tissues.
DR   ExpressionAtlas; Q9NYU1; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
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: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   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:SF1; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 2; 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; Q9NYU1; HS.
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
//