MGAT1_HUMAN
ID MGAT1_HUMAN Reviewed; 445 AA.
AC P26572; A8K404; B3KRU8; D3DWR1; Q6IBE3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.101 {ECO:0000269|PubMed:1702225};
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I {ECO:0000303|PubMed:1702225};
DE Short=GNT-I;
DE Short=GlcNAc-T I {ECO:0000303|PubMed:1702225};
GN Name=MGAT1; Synonyms=GGNT1, GLCT1, GLYT1, MGAT;
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP COFACTOR.
RX PubMed=1702225; DOI=10.1073/pnas.87.24.9948;
RA Kumar R., Yang J., Larsen R.D., Stanley P.;
RT "Cloning and expression of N-acetylglucosaminyltransferase I, the medial
RT Golgi transferase that initiates complex N-linked carbohydrate formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9948-9952(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-435.
RC TISSUE=Myeloid leukemia cell;
RX PubMed=1827260; DOI=10.1016/s0006-291x(05)80227-x;
RA Hull E., Sarkar M., Spruijt M.P.N., Hoeppener J.W.M., Dunn R.,
RA Schachter H.;
RT "Organization and localization to chromosome 5 of the human UDP-N-
RT acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-
RT acetylglucosaminyltransferase I gene.";
RL Biochem. Biophys. Res. Commun. 176:608-615(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-435.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-435.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-435.
RC TISSUE=Kidney;
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=20378551; DOI=10.1074/jbc.m110.103184;
RA Hassinen A., Rivinoja A., Kauppila A., Kellokumpu S.;
RT "Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme
RT complexes in live cells.";
RL J. Biol. Chem. 285:17771-17777(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP INTERACTION WITH BRI3, AND SUBCELLULAR LOCATION.
RX PubMed=30983867; DOI=10.3906/biy-1805-47;
RA Akiva I., Birguel Iyison N.;
RT "Identification of IFITM3 and MGAT1 as novel interaction partners of BRI3
RT by yeast two-hybrid screening.";
RL Turk. J. Biol. 42:463-470(2018).
CC -!- FUNCTION: Initiates complex N-linked carbohydrate formation. Essential
CC for the conversion of high-mannose to hybrid and complex N-glycans.
CC {ECO:0000269|PubMed:1702225}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer
CC 5A1,2) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-
CC GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:11456,
CC Rhea:RHEA-COMP:14367, Rhea:RHEA-COMP:14368, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:59087,
CC ChEBI:CHEBI:60625; EC=2.4.1.101;
CC Evidence={ECO:0000269|PubMed:1702225};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:1702225};
CC Note=The cofactor is mostly bound to the substrate.
CC {ECO:0000250|UniProtKB:P27115};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:1702225}.
CC -!- SUBUNIT: Interacts with MGAT4D. Interacts with BRI3 (isoforms 1 and 2);
CC the interaction with isoform 2 is weaker than with isoform 1
CC (PubMed:30983867). {ECO:0000250|UniProtKB:P27808,
CC ECO:0000269|PubMed:30983867}.
CC -!- INTERACTION:
CC P26572; O95415: BRI3; NbExp=6; IntAct=EBI-7211952, EBI-2874789;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein
CC {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:30983867}. Note=Co-localizes with BRI3 isoform 1 at
CC the perinuclear region. {ECO:0000269|PubMed:30983867}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Alpha-
CC 1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_535";
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DR EMBL; M55621; AAA52563.1; -; mRNA.
DR EMBL; M61829; AAA75523.1; -; Genomic_DNA.
DR EMBL; AK092256; BAG52510.1; -; mRNA.
DR EMBL; AK094130; BAG52821.1; -; mRNA.
DR EMBL; AK290769; BAF83458.1; -; mRNA.
DR EMBL; CR456861; CAG33142.1; -; mRNA.
DR EMBL; AC022413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471165; EAW53739.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53740.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53741.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53742.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53743.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53744.1; -; Genomic_DNA.
DR EMBL; BC003575; AAH03575.1; -; mRNA.
DR CCDS; CCDS4458.1; -.
DR PIR; JH0397; XUHUMB.
DR RefSeq; NP_001108089.1; NM_001114617.1.
DR RefSeq; NP_001108090.1; NM_001114618.1.
DR RefSeq; NP_001108091.1; NM_001114619.1.
DR RefSeq; NP_001108092.1; NM_001114620.1.
DR RefSeq; NP_002397.2; NM_002406.3.
DR RefSeq; XP_005265972.1; XM_005265915.1.
DR RefSeq; XP_005265973.1; XM_005265916.1.
DR RefSeq; XP_006714929.1; XM_006714866.1.
DR RefSeq; XP_011532861.1; XM_011534559.1.
DR RefSeq; XP_011532862.1; XM_011534560.1.
DR RefSeq; XP_011532863.1; XM_011534561.1.
DR RefSeq; XP_011532864.1; XM_011534562.1.
DR RefSeq; XP_011532865.1; XM_011534563.2.
DR RefSeq; XP_016864975.1; XM_017009486.1.
DR RefSeq; XP_016864976.1; XM_017009487.1.
DR AlphaFoldDB; P26572; -.
DR SMR; P26572; -.
DR BioGRID; 110401; 38.
DR CORUM; P26572; -.
DR IntAct; P26572; 14.
DR MINT; P26572; -.
DR STRING; 9606.ENSP00000404718; -.
DR BindingDB; P26572; -.
DR ChEMBL; CHEMBL2375207; -.
DR DrugBank; DB03397; Uridine-Diphosphate-N-Acetylglucosamine.
DR CAZy; GT13; Glycosyltransferase Family 13.
DR GlyGen; P26572; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P26572; -.
DR PhosphoSitePlus; P26572; -.
DR BioMuta; MGAT1; -.
DR DMDM; 311033399; -.
DR EPD; P26572; -.
DR jPOST; P26572; -.
DR MassIVE; P26572; -.
DR MaxQB; P26572; -.
DR PaxDb; P26572; -.
DR PeptideAtlas; P26572; -.
DR PRIDE; P26572; -.
DR ProteomicsDB; 54352; -.
DR Antibodypedia; 17878; 281 antibodies from 32 providers.
DR DNASU; 4245; -.
DR Ensembl; ENST00000307826.5; ENSP00000311888.4; ENSG00000131446.17.
DR Ensembl; ENST00000333055.8; ENSP00000332073.3; ENSG00000131446.17.
DR Ensembl; ENST00000393340.7; ENSP00000377010.3; ENSG00000131446.17.
DR Ensembl; ENST00000427865.2; ENSP00000402838.2; ENSG00000131446.17.
DR Ensembl; ENST00000446023.6; ENSP00000404718.2; ENSG00000131446.17.
DR GeneID; 4245; -.
DR KEGG; hsa:4245; -.
DR MANE-Select; ENST00000307826.5; ENSP00000311888.4; NM_002406.4; NP_002397.2.
DR UCSC; uc003mmg.5; human.
DR CTD; 4245; -.
DR DisGeNET; 4245; -.
DR GeneCards; MGAT1; -.
DR HGNC; HGNC:7044; MGAT1.
DR HPA; ENSG00000131446; Low tissue specificity.
DR MIM; 160995; gene.
DR neXtProt; NX_P26572; -.
DR OpenTargets; ENSG00000131446; -.
DR PharmGKB; PA30779; -.
DR VEuPathDB; HostDB:ENSG00000131446; -.
DR eggNOG; KOG1413; Eukaryota.
DR GeneTree; ENSGT00530000063632; -.
DR HOGENOM; CLU_022150_0_0_1; -.
DR InParanoid; P26572; -.
DR OMA; KGYDLSW; -.
DR OrthoDB; 1324622at2759; -.
DR PhylomeDB; P26572; -.
DR TreeFam; TF320555; -.
DR BioCyc; MetaCyc:HS05528-MON; -.
DR BRENDA; 2.4.1.101; 2681.
DR PathwayCommons; P26572; -.
DR Reactome; R-HSA-964739; N-glycan trimming and elongation in the cis-Golgi.
DR Reactome; R-HSA-9683686; Maturation of spike protein.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; P26572; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 4245; 191 hits in 1079 CRISPR screens.
DR ChiTaRS; MGAT1; human.
DR GeneWiki; MGAT1; -.
DR GenomeRNAi; 4245; -.
DR Pharos; P26572; Tchem.
DR PRO; PR:P26572; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P26572; protein.
DR Bgee; ENSG00000131446; Expressed in monocyte and 202 other tissues.
DR ExpressionAtlas; P26572; baseline and differential.
DR Genevisible; P26572; HS.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; TAS:Reactome.
DR GO; GO:0003827; F:alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR GO; GO:0006049; P:UDP-N-acetylglucosamine catabolic process; IEA:Ensembl.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004139; Glyco_trans_13.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF03071; GNT-I; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Glycosyltransferase; Golgi apparatus; Manganese;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..445
FT /note="Alpha-1,3-mannosyl-glycoprotein 2-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000191384"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..445
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT DISULFID 113..143
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT DISULFID 237..303
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT VARIANT 223
FT /note="R -> Q (in dbSNP:rs7726005)"
FT /id="VAR_028272"
FT VARIANT 435
FT /note="L -> P (in dbSNP:rs634501)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1827260,
FT ECO:0000269|Ref.4"
FT /id="VAR_028273"
FT CONFLICT 291
FT /note="W -> R (in Ref. 3; BAG52510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 50878 MW; 13402302ED69C302 CRC64;
MLKKQSAGLV LWGAILFVAW NALLLLFFWT RPAPGRPPSV SALDGDPASL TREVIRLAQD
AEVELERQRG LLQQIGDALS SQRGRVPTAA PPAQPRVPVT PAPAVIPILV IACDRSTVRR
CLDKLLHYRP SAELFPIIVS QDCGHEETAQ AIASYGSAVT HIRQPDLSSI AVPPDHRKFQ
GYYKIARHYR WALGQVFRQF RFPAAVVVED DLEVAPDFFE YFRATYPLLK ADPSLWCVSA
WNDNGKEQMV DASRPELLYR TDFFPGLGWL LLAELWAELE PKWPKAFWDD WMRRPEQRQG
RACIRPEISR TMTFGRKGVS HGQFFDQHLK FIKLNQQFVH FTQLDLSYLQ REAYDRDFLA
RVYGAPQLQV EKVRTNDRKE LGEVRVQYTG RDSFKAFAKA LGVMDDLKSG VPRAGYRGIV
TFQFRGRRVH LAPPLTWEGY DPSWN
