MGT5A_MOUSE
ID MGT5A_MOUSE Reviewed; 740 AA.
AC Q8R4G6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A;
DE EC=2.4.1.155 {ECO:0000269|PubMed:10700233, ECO:0000269|PubMed:12122020};
DE AltName: Full=Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase;
DE AltName: Full=GlcNAc-T V;
DE Short=GNT-V;
DE AltName: Full=Mannoside acetylglucosaminyltransferase 5;
DE AltName: Full=N-acetylglucosaminyl-transferase V;
DE Contains:
DE RecName: Full=Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A {ECO:0000305};
DE AltName: Full=Secreted beta-1,6-N-acetylglucosaminyltransferase V {ECO:0000305};
DE Short=Secreted GNT-V {ECO:0000305};
DE Flags: Precursor;
GN Name=Mgat5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=12122020; DOI=10.1093/glycob/cwf040;
RA Alverez K., Haswell C., St Clair M., Perng G.S., Shorebah M., Pierce M.,
RA Fregien N.;
RT "Sequences of the mouse N-acetylglucosaminyltransferase V (Mgat5) mRNA and
RT an mRNA expressed by an Mgat5-deficient cell line.";
RL Glycobiology 12:389-394(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10700233; DOI=10.1038/73163;
RA Granovsky M., Fata J., Pawling J., Muller W.J., Khokha R., Dennis J.W.;
RT "Suppression of tumor growth and metastasis in Mgat5-deficient mice.";
RL Nat. Med. 6:306-312(2000).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11217864; DOI=10.1038/35055582;
RA Demetriou M., Granovsky M., Quaggin S., Dennis J.W.;
RT "Negative regulation of T-cell activation and autoimmunity by Mgat5 N-
RT glycosylation.";
RL Nature 409:733-739(2001).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14561752; DOI=10.1074/jbc.m308837200;
RA Guo H.B., Lee I., Kamar M., Pierce M.;
RT "N-acetylglucosaminyltransferase V expression levels regulate cadherin-
RT associated homotypic cell-cell adhesion and intracellular signaling
RT pathways.";
RL J. Biol. Chem. 278:52412-52424(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15459394; DOI=10.1126/science.1102109;
RA Partridge E.A., Le Roy C., Di Guglielmo G.M., Pawling J., Cheung P.,
RA Granovsky M., Nabi I.R., Wrana J.L., Dennis J.W.;
RT "Regulation of cytokine receptors by Golgi N-glycan processing and
RT endocytosis.";
RL Science 306:120-124(2004).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
RX PubMed=22715095; DOI=10.1074/jbc.m112.367565;
RA Lee J.K., Matthews R.T., Lim J.M., Swanier K., Wells L., Pierce J.M.;
RT "Developmental expression of the neuron-specific N-
RT acetylglucosaminyltransferase Vb (GnT-Vb/IX) and identification of its in
RT vivo glycan products in comparison with those of its paralog, GnT-V.";
RL J. Biol. Chem. 287:28526-28536(2012).
CC -!- FUNCTION: Catalyzes the addition of N-acetylglucosamine (GlcNAc) in
CC beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked
CC oligosaccharides (PubMed:10700233, PubMed:14561752, PubMed:22715095).
CC Catalyzes an important step in the biosynthesis of branched, complex-
CC type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor)
CC and CDH2 (PubMed:12122020, PubMed:10700233, PubMed:14561752,
CC PubMed:15459394, PubMed:22715095). Via its role in the biosynthesis of
CC complex N-glycans, plays an important role in the activation of
CC cellular signaling pathways, reorganization of the actin cytoskeleton,
CC cell-cell adhesion and cell migration (PubMed:10700233,
CC PubMed:14561752, PubMed:15459394). MGAT5-dependent EGFR N-glycosylation
CC enhances the interaction between EGFR and LGALS3 and thereby prevents
CC rapid EGFR endocytosis and prolongs EGFR signaling (PubMed:15459394).
CC Required for efficient interaction between TGFB1 and its receptor
CC (PubMed:15459394). Enhances activation of intracellular signaling
CC pathways by several types of growth factors, including FGF2, PDGF, IGF,
CC TGFB1 and EGF (PubMed:15459394). MGAT5-dependent CDH2 N-glycosylation
CC inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to
CC the regulation of downstream signaling pathways (PubMed:14561752).
CC Promotes cell migration (PubMed:14561752, PubMed:15459394). Contributes
CC to the regulation of the inflammatory response (PubMed:11217864,
CC PubMed:15459394). MGAT5-dependent TCR N-glycosylation enhances the
CC interaction between TCR and LGALS3, limits agonist-induced TCR
CC clustering, and thereby dampens TCR-mediated responses to antigens
CC (PubMed:11217864). Required for normal leukocyte evasation and
CC accumulation at sites of inflammation (PubMed:15459394). Inhibits
CC attachment of monocytes to the vascular endothelium and subsequent
CC monocyte diapedesis (By similarity). {ECO:0000250|UniProtKB:Q09328,
CC ECO:0000269|PubMed:10700233, ECO:0000269|PubMed:11217864,
CC ECO:0000269|PubMed:12122020, ECO:0000269|PubMed:14561752,
CC ECO:0000269|PubMed:15459394, ECO:0000269|PubMed:22715095}.
CC -!- FUNCTION: [Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-
CC acetylglucosaminyltransferase A]: Promotes proliferation of umbilical
CC vein endothelial cells and angiogenesis, at least in part by promoting
CC the release of the growth factor FGF2 from the extracellular matrix.
CC {ECO:0000250|UniProtKB:Q09328}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-
CC GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-
CC (1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:16921, Rhea:RHEA-COMP:14374, Rhea:RHEA-COMP:14377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:139507, ChEBI:CHEBI:139510; EC=2.4.1.155;
CC Evidence={ECO:0000269|PubMed:10700233, ECO:0000269|PubMed:12122020};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:10700233, ECO:0000269|PubMed:12122020,
CC ECO:0000269|PubMed:22715095}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P97259}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q09328}. Perikaryon
CC {ECO:0000269|PubMed:10700233}.
CC -!- SUBCELLULAR LOCATION: [Secreted alpha-1,6-mannosylglycoprotein 6-beta-
CC N-acetylglucosaminyltransferase A]: Secreted
CC {ECO:0000250|UniProtKB:Q09328}.
CC -!- TISSUE SPECIFICITY: Detected in cerebellum.
CC {ECO:0000269|PubMed:10700233}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q09328}.
CC -!- PTM: A secreted form is released from the membrane after cleavage by
CC gamma-secretase. {ECO:0000250|UniProtKB:Q09328}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate and
CC have no visible phenotype at birth. Adult mice display abnormal
CC leukocyte recruitment to inflamed tissues, hypersensitivity of T cells
CC to agonists that activate T cell receptors, an age-related decrease in
CC the cellularity of kidney glomeruli and a tendency to develop
CC proliferative glomerulonephritis, plus defective nurturing behavior
CC (PubMed:10700233, PubMed:11217864). Mutant mice show increased
CC responsiveness to treatments that cause delayed-type hypersensitivity
CC (PubMed:11217864). Mice show increased incidence of autoimmune
CC encephalomyelitis in response to injections with MBP (PubMed:11217864).
CC Transgenic mice that express polyomavirus middle T antigen develop
CC mammary tumors; 50% of female wild-type mice have detectable tumors
CC after 16 weeks, but it takes 24 weeks until 50% of the female mice that
CC lack Mgat5 develop mammary tumors. Male mice that express polyomavirus
CC middle T antigen develop mammary tumors after 6 to 9 months; males that
CC lack Mgat5 develop tumors after 10 to 13 months. Formation of lung
CC metastases is about 5% of wild-type (PubMed:10700233). Tumor initiation
CC is not decreased in mice that lack Mgat5, but tumor growth is strongly
CC decreased (PubMed:10700233). Tumor cells from mutant mice show impaired
CC membrane ruffling, probably due to decreased activation of
CC phosphoinositide-3-kinase (PI3K) (PubMed:10700233). Embryonic
CC fibroblasts from Mgat5-deficient mice display increased Cdh2-mediated
CC cell-cell adhesion (PubMed:14561752). Mutant mice that lack both Mgat5
CC and Mgat5b display no visible changes in brain anatomy, but their
CC brains display defective biosynthesis of both O-mannosyl glycans and N-
CC linked glycans (PubMed:22715095). {ECO:0000269|PubMed:10700233,
CC ECO:0000269|PubMed:11217864, ECO:0000269|PubMed:14561752,
CC ECO:0000269|PubMed:22715095}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 18 family.
CC {ECO:0000305}.
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DR EMBL; AF474154; AAL83249.1; -; mRNA.
DR EMBL; AK030402; BAC26946.1; -; mRNA.
DR CCDS; CCDS15245.1; -.
DR RefSeq; NP_660110.2; NM_145128.3.
DR RefSeq; XP_006529118.1; XM_006529055.3.
DR RefSeq; XP_006529119.1; XM_006529056.3.
DR RefSeq; XP_006529120.1; XM_006529057.3.
DR AlphaFoldDB; Q8R4G6; -.
DR SMR; Q8R4G6; -.
DR STRING; 10090.ENSMUSP00000038359; -.
DR CAZy; GT18; Glycosyltransferase Family 18.
DR GlyGen; Q8R4G6; 6 sites.
DR iPTMnet; Q8R4G6; -.
DR PhosphoSitePlus; Q8R4G6; -.
DR MaxQB; Q8R4G6; -.
DR PaxDb; Q8R4G6; -.
DR PRIDE; Q8R4G6; -.
DR ProteomicsDB; 295662; -.
DR Antibodypedia; 33554; 161 antibodies from 25 providers.
DR DNASU; 107895; -.
DR Ensembl; ENSMUST00000038361; ENSMUSP00000038359; ENSMUSG00000036155.
DR Ensembl; ENSMUST00000171405; ENSMUSP00000129166; ENSMUSG00000036155.
DR GeneID; 107895; -.
DR KEGG; mmu:107895; -.
DR UCSC; uc007ckq.1; mouse.
DR CTD; 4249; -.
DR MGI; MGI:894701; Mgat5.
DR VEuPathDB; HostDB:ENSMUSG00000036155; -.
DR eggNOG; ENOG502QTNG; Eukaryota.
DR GeneTree; ENSGT00940000153470; -.
DR HOGENOM; CLU_016749_1_0_1; -.
DR InParanoid; Q8R4G6; -.
DR OMA; DGRRKHC; -.
DR OrthoDB; 179031at2759; -.
DR PhylomeDB; Q8R4G6; -.
DR TreeFam; TF313714; -.
DR Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 107895; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Mgat5; mouse.
DR PRO; PR:Q8R4G6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8R4G6; protein.
DR Bgee; ENSMUSG00000036155; Expressed in paneth cell and 215 other tissues.
DR ExpressionAtlas; Q8R4G6; baseline and differential.
DR Genevisible; Q8R4G6; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IMP:MGI.
DR GO; GO:0030144; F:alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity; IMP:MGI.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; ISO:MGI.
DR GO; GO:1903614; P:negative regulation of protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:MGI.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
DR InterPro; IPR027833; DUF4525.
DR InterPro; IPR026116; GlyclTrfase_18.
DR Pfam; PF15027; DUF4525; 1.
DR Pfam; PF15024; Glyco_transf_18; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Secreted; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..740
FT /note="Alpha-1,6-mannosylglycoprotein 6-beta-N-
FT acetylglucosaminyltransferase A"
FT /id="PRO_0000080523"
FT CHAIN 31..740
FT /note="Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-
FT acetylglucosaminyltransferase A"
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT /id="PRO_0000445693"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..740
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 212..740
FT /note="Sufficient for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT BINDING 377..378
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT BINDING 525
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT BINDING 553
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 144..182
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 155..195
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 171..337
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 371..625
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 648..723
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 652..725
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 659..712
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 680..701
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 736..739
FT /evidence="ECO:0000250|UniProtKB:Q09328"
SQ SEQUENCE 740 AA; 84551 MW; E4D0A58BD6954C7A CRC64;
MAFFSPWKLS SQKLGFFLVT FGFIWGMMLL HFTIQQRTQP ESSSMLREQI LDLSKRYIKA
LAEENRDVVD GPYAGVMTAY DLKKTLAVLL DNILQRIGKL ESKVDNLVNG TGANSTNSTT
AVPSLVSLEK INVADIINGV QEKCVLPPMD GYPHCEGKIK WMKDMWRSDP CYADYGVDGT
SCSFFIYLSE VENWCPRLPW RAKNPYEEAD HNSLAEIRTD FNILYGMMKK HEEFRWMRLR
IRRMADAWIQ AIKSLAEKQN LEKRKRKKIL VHLGLLTKES GFKIAETAFS GGPLGELVQW
SDLITSLYLL GHDIRISASL AELKEIMKKV VGNRSGCPTV GDRIVELIYI DIVGLAQFKK
TLGPSWVHYQ CMLRVLDSFG TEPEFNHASY AQSKGHKTPW GKWNLNPQQF YTMFPHTPDN
SFLGFVVEQH LNSSDIHHIN EIKRQNQSLV YGKVDSFWKN KKIYLDIIHT YMEVHATVYG
SSTKNIPSYV KNHGILSGRD LQFLLRETKL FVGLGFPYEG PAPLEAIANG CAFLNPKFNP
PKSSKNTDFF IGKPTLRELT SQHPYAEVFI GRPHVWTVDL NNREEVEDAV KAILNQKIEP
YMPYEFTCEG MLQRINAFIE KQDFCHGQVM WPPLSALQVK LAEPGQSCKQ VCQESQLICE
PSFFQHLNKE KDLLKYKVTC QSSELYKDIL VPSFYPKSKH CVFQGDLLLF SCAGAHPTHQ
RICPCRDFIK GQVALCKDCL
