MGAT2_HUMAN
ID MGAT2_HUMAN Reviewed; 447 AA.
AC Q10469; B3KPC5; B3KQM0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.143 {ECO:0000269|PubMed:29666272, ECO:0000269|PubMed:7635144, ECO:0000269|PubMed:8808595};
DE AltName: Full=Beta-1,2-N-acetylglucosaminyltransferase II;
DE AltName: Full=GlcNAc-T II;
DE Short=GNT-II;
DE AltName: Full=Mannoside acetylglucosaminyltransferase 2;
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II;
GN Name=MGAT2;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RC TISSUE=Leukocyte;
RX PubMed=7635144; DOI=10.1111/j.1432-1033.1995.tb20703.x;
RA Tan J., D'Agostaro A.F., Bendiak B., Reck F., Sarkar M., Squire J.A.,
RA Leong P., Schachter H.;
RT "The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2-N-
RT acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA,
RT localization to chromosome 14q21, expression in insect cells and
RT purification of the recombinant protein.";
RL Eur. J. Biochem. 231:317-328(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
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 [6] {ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR, ECO:0007744|PDB:5VCS}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 29-447 IN COMPLEXES WITH
RP MANGANESE AND UDP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY,
RP GLYCOSYLATION AT ASN-86, DISULFIDE BONDS, AND MUTAGENESIS OF ARG-198;
RP ASP-217; GLU-259; TYR-294; ASN-318; TYR-344; TRP-346 AND ASP-347.
RX PubMed=29666272; DOI=10.1073/pnas.1716988115;
RA Kadirvelraj R., Yang J.Y., Sanders J.H., Liu L., Ramiah A., Prabhakar P.K.,
RA Boons G.J., Wood Z.A., Moremen K.W.;
RT "Human N-acetylglucosaminyltransferase II substrate recognition uses a
RT modular architecture that includes a convergent exosite.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:4637-4642(2018).
RN [7]
RP VARIANTS CDG2A ARG-262 AND PHE-290, FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND CHARACTERIZATION OF VARIANTS CDG2A ARG-262 AND PHE-290.
RX PubMed=8808595;
RA Tan J., Dunn J., Jaeken J., Schachter H.;
RT "Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause
RT carbohydrate-deficient glycoprotein syndrome type II, an autosomal
RT recessive disease with defective brain development.";
RL Am. J. Hum. Genet. 59:810-817(1996).
RN [8]
RP VARIANT CDG2A ASP-318, FUNCTION, AND PATHWAY.
RX PubMed=11228641; DOI=10.1136/jmg.37.11.875;
RA Cormier-Daire V., Amiel J., Vuillaumier-Barrot S., Tan J., Durand G.,
RA Munnich A., Le Merrer M., Seta N.;
RT "Congenital disorders of glycosylation IIa cause growth retardation, mental
RT retardation, and facial dysmorphism.";
RL J. Med. Genet. 37:875-877(2000).
CC -!- FUNCTION: Plays an essential role in protein N-glycosylation. Catalyzes
CC the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal
CC mannose moiety in the core structure of the nascent N-linked glycan
CC chain, giving rise to the second branch in complex glycans.
CC {ECO:0000269|PubMed:11228641, ECO:0000269|PubMed:29666272,
CC ECO:0000269|PubMed:8808595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-
CC asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-
CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:12941,
CC Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:14369, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615,
CC ChEBI:CHEBI:60651; EC=2.4.1.143;
CC Evidence={ECO:0000269|PubMed:29666272, ECO:0000269|PubMed:7635144,
CC ECO:0000269|PubMed:8808595};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:29666272};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11228641, ECO:0000269|PubMed:29666272,
CC ECO:0000269|PubMed:7635144, ECO:0000269|PubMed:8808595}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20378551}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- DISEASE: Congenital disorder of glycosylation 2A (CDG2A) [MIM:212066]:
CC A multisystem disorder caused by a defect in glycoprotein biosynthesis
CC and characterized by under-glycosylated serum glycoproteins. Congenital
CC disorders of glycosylation result in a wide variety of clinical
CC features, such as defects in the nervous system development,
CC psychomotor retardation, dysmorphic features, hypotonia, coagulation
CC disorders, and immunodeficiency. The broad spectrum of features
CC reflects the critical role of N-glycoproteins during embryonic
CC development, differentiation, and maintenance of cell functions.
CC {ECO:0000269|PubMed:11228641, ECO:0000269|PubMed:8808595}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 16 (GT16) protein
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Alpha-
CC 1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_534";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U15128; AAA86956.1; -; Genomic_DNA.
DR EMBL; AK056167; BAG51637.1; -; mRNA.
DR EMBL; AK075199; BAG52082.1; -; mRNA.
DR EMBL; CH471078; EAW65758.1; -; Genomic_DNA.
DR EMBL; BC006390; AAH06390.1; -; mRNA.
DR CCDS; CCDS9690.1; -.
DR PIR; S66256; S66256.
DR RefSeq; NP_002399.1; NM_002408.3.
DR PDB; 5VCM; X-ray; 1.60 A; A/B=29-447.
DR PDB; 5VCR; X-ray; 1.99 A; A/B=29-447.
DR PDB; 5VCS; X-ray; 2.80 A; A/B=29-447.
DR PDBsum; 5VCM; -.
DR PDBsum; 5VCR; -.
DR PDBsum; 5VCS; -.
DR AlphaFoldDB; Q10469; -.
DR SMR; Q10469; -.
DR BioGRID; 110403; 29.
DR CORUM; Q10469; -.
DR IntAct; Q10469; 7.
DR STRING; 9606.ENSP00000307423; -.
DR BindingDB; Q10469; -.
DR ChEMBL; CHEMBL2321630; -.
DR CAZy; GT16; Glycosyltransferase Family 16.
DR GlyGen; Q10469; 4 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q10469; -.
DR PhosphoSitePlus; Q10469; -.
DR BioMuta; MGAT2; -.
DR DMDM; 1708004; -.
DR EPD; Q10469; -.
DR jPOST; Q10469; -.
DR MassIVE; Q10469; -.
DR MaxQB; Q10469; -.
DR PaxDb; Q10469; -.
DR PeptideAtlas; Q10469; -.
DR PRIDE; Q10469; -.
DR ProteomicsDB; 58853; -.
DR Antibodypedia; 10266; 161 antibodies from 23 providers.
DR DNASU; 4247; -.
DR Ensembl; ENST00000305386.4; ENSP00000307423.2; ENSG00000168282.6.
DR GeneID; 4247; -.
DR KEGG; hsa:4247; -.
DR MANE-Select; ENST00000305386.4; ENSP00000307423.2; NM_002408.4; NP_002399.1.
DR UCSC; uc001wwr.4; human.
DR CTD; 4247; -.
DR DisGeNET; 4247; -.
DR GeneCards; MGAT2; -.
DR GeneReviews; MGAT2; -.
DR HGNC; HGNC:7045; MGAT2.
DR HPA; ENSG00000168282; Low tissue specificity.
DR MalaCards; MGAT2; -.
DR MIM; 212066; phenotype.
DR MIM; 602616; gene.
DR neXtProt; NX_Q10469; -.
DR OpenTargets; ENSG00000168282; -.
DR Orphanet; 79329; MGAT2-CDG.
DR PharmGKB; PA30780; -.
DR VEuPathDB; HostDB:ENSG00000168282; -.
DR eggNOG; KOG2791; Eukaryota.
DR GeneTree; ENSGT00390000007341; -.
DR HOGENOM; CLU_032753_2_1_1; -.
DR InParanoid; Q10469; -.
DR OMA; MHHKKTC; -.
DR OrthoDB; 647764at2759; -.
DR PhylomeDB; Q10469; -.
DR TreeFam; TF314772; -.
DR BioCyc; MetaCyc:HS09725-MON; -.
DR BRENDA; 2.4.1.143; 2681.
DR PathwayCommons; Q10469; -.
DR Reactome; R-HSA-4793952; Defective MGAT2 causes CDG-2a.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR SignaLink; Q10469; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 4247; 57 hits in 1076 CRISPR screens.
DR ChiTaRS; MGAT2; human.
DR GeneWiki; MGAT2; -.
DR GenomeRNAi; 4247; -.
DR Pharos; Q10469; Tchem.
DR PRO; PR:Q10469; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q10469; protein.
DR Bgee; ENSG00000168282; Expressed in jejunal mucosa and 200 other tissues.
DR Genevisible; Q10469; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008455; F:alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IEA:InterPro.
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:0019082; P:viral protein processing; TAS:Reactome.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR007754; GlcNAc_II.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12871; PTHR12871; 1.
DR Pfam; PF05060; MGAT2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Congenital disorder of glycosylation;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..447
FT /note="Alpha-1,6-mannosyl-glycoprotein 2-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000080517"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..447
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 123..127
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM"
FT BINDING 229..233
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM"
FT BINDING 261
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM"
FT BINDING 374
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT ECO:0007744|PDB:5VCS"
FT DISULFID 196..210
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT ECO:0007744|PDB:5VCS"
FT DISULFID 283..286
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT ECO:0007744|PDB:5VCS"
FT DISULFID 334..357
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT ECO:0007744|PDB:5VCS"
FT DISULFID 339..440
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT ECO:0007744|PDB:5VCS"
FT DISULFID 378..386
FT /evidence="ECO:0000269|PubMed:29666272,
FT ECO:0007744|PDB:5VCM"
FT VARIANT 262
FT /note="H -> R (in CDG2A; strongly reduced protein levels;
FT loss of enzyme activity; dbSNP:rs104894447)"
FT /evidence="ECO:0000269|PubMed:8808595"
FT /id="VAR_003415"
FT VARIANT 290
FT /note="S -> F (in CDG2A; strongly reduced protein levels;
FT loss of enzyme activity; dbSNP:rs104894446)"
FT /evidence="ECO:0000269|PubMed:8808595"
FT /id="VAR_003416"
FT VARIANT 318
FT /note="N -> D (in CDG2A; dbSNP:rs104894448)"
FT /evidence="ECO:0000269|PubMed:11228641"
FT /id="VAR_012343"
FT MUTAGEN 198
FT /note="R->A: Strongly decreased catalytic activity and
FT affinity for UDP-GlcNAc."
FT /evidence="ECO:0000269|PubMed:29666272"
FT MUTAGEN 217
FT /note="D->A: Nearly abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29666272"
FT MUTAGEN 259
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29666272"
FT MUTAGEN 294
FT /note="Y->A: Strongly decreased catalytic activity and
FT affinity for UDP-GlcNAc."
FT /evidence="ECO:0000269|PubMed:29666272"
FT MUTAGEN 318
FT /note="N->A: Strongly decreased catalytic activity and
FT affinity for UDP-GlcNAc."
FT /evidence="ECO:0000269|PubMed:29666272"
FT MUTAGEN 344
FT /note="Y->A: Nearly abolishes catalytic activity and
FT strongly decreases affinity for UDP-GlcNAc."
FT /evidence="ECO:0000269|PubMed:29666272"
FT MUTAGEN 346
FT /note="W->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29666272"
FT MUTAGEN 347
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29666272"
FT CONFLICT 299
FT /note="S -> R (in Ref. 2; BAG52082)"
FT /evidence="ECO:0000305"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5VCM"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5VCS"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:5VCM"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 225..243
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 268..282
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:5VCM"
FT TURN 301..305
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:5VCM"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 388..401
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:5VCM"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:5VCM"
FT HELIX 434..442
FT /evidence="ECO:0007829|PDB:5VCM"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:5VCM"
SQ SEQUENCE 447 AA; 51550 MW; 533B76D08BD8A572 CRC64;
MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKNEALAPP LLDAEPARGA GGRGGDHPSV
AVGIRRVSNV SAASLVPAVP QPEADNLTLR YRSLVYQLNF DQTLRNVDKA GTWAPRELVL
VVQVHNRPEY LRLLLDSLRK AQGIDNVLVI FSHDFWSTEI NQLIAGVNFC PVLQVFFPFS
IQLYPNEFPG SDPRDCPRDL PKNAALKLGC INAEYPDSFG HYREAKFSQT KHHWWWKLHF
VWERVKILRD YAGLILFLEE DHYLAPDFYH VFKKMWKLKQ QECPECDVLS LGTYSASRSF
YGMADKVDVK TWKSTEHNMG LALTRNAYQK LIECTDTFCT YDDYNWDWTL QYLTVSCLPK
FWKVLVPQIP RIFHAGDCGM HHKKTCRPST QSAQIESLLN NNKQYMFPET LTISEKFTVV
AISPPRKNGG WGDIRDHELC KSYRRLQ
