LARG2_HUMAN
ID LARG2_HUMAN Reviewed; 721 AA.
AC Q8N3Y3; A6NN75; Q8N8Y6; Q8NAK3; Q8WY62;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Xylosyl- and glucuronyltransferase LARGE2 {ECO:0000305};
DE EC=2.4.-.- {ECO:0000250|UniProtKB:Q5XPT3};
DE AltName: Full=Glycosyltransferase-like 1B;
DE AltName: Full=LARGE xylosyl- and glucuronyltransferase 2 {ECO:0000312|HGNC:HGNC:16522};
DE Includes:
DE RecName: Full=Alpha-1,3-xylosyltransferase LARGE2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q5XPT3};
DE Includes:
DE RecName: Full=Beta-1,3-glucuronyltransferase LARGE2 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q5XPT3};
GN Name=LARGE2 {ECO:0000312|HGNC:HGNC:16522}; Synonyms=GYLTL1B;
GN ORFNames=PP5656;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
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], AND VARIANT LYS-37.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 356-721.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15752776; DOI=10.1016/j.bbrc.2005.02.082;
RA Fujimura K., Sawaki H., Sakai T., Hiruma T., Nakanishi N., Sato T.,
RA Ohkura T., Narimatsu H.;
RT "LARGE2 facilitates the maturation of alpha-dystroglycan more effectively
RT than LARGE.";
RL Biochem. Biophys. Res. Commun. 329:1162-1171(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15958417; DOI=10.1093/glycob/cwi094;
RA Grewal P.K., McLaughlan J.M., Moore C.J., Browning C.A., Hewitt J.E.;
RT "Characterization of the LARGE family of putative glycosyltransferases
RT associated with dystroglycanopathies.";
RL Glycobiology 15:912-923(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15661757; DOI=10.1093/hmg/ddi062;
RA Brockington M., Torelli S., Prandini P., Boito C., Dolatshad N.F.,
RA Longman C., Brown S.C., Muntoni F.;
RT "Localization and functional analysis of the LARGE family of
RT glycosyltransferases: significance for muscular dystrophy.";
RL Hum. Mol. Genet. 14:657-665(2005).
RN [9]
RP INTERACTION WITH B4GAT1.
RX PubMed=19587235; DOI=10.1073/pnas.0904515106;
RA Bao X., Kobayashi M., Hatakeyama S., Angata K., Gullberg D., Nakayama J.,
RA Fukuda M.N., Fukuda M.;
RT "Tumor suppressor function of laminin-binding alpha-dystroglycan requires a
RT distinct beta3-N-acetylglucosaminyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12109-12114(2009).
RN [10]
RP FUNCTION, AND COFACTOR.
RX PubMed=25138275; DOI=10.1074/jbc.m114.597831;
RA Inamori K., Willer T., Hara Y., Venzke D., Anderson M.E., Clarke N.F.,
RA Guicheney P., Bonnemann C.G., Moore S.A., Campbell K.P.;
RT "Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for
RT functional modification of alpha-dystroglycan in cells and tissues.";
RL J. Biol. Chem. 289:28138-28148(2014).
CC -!- FUNCTION: Bifunctional glycosyltransferase with both alpha-1,3-
CC xylosyltransferase and beta-1,3-glucuronyltransferase activities
CC involved in the maturation of alpha-dystroglycan (DAG1) by
CC glycosylation leading to DAG1 binding to laminin G-like domain-
CC containing extracellular proteins with high affinity and in a
CC phosphorylated-O-mannosyl trisaccharide dependent manner
CC (PubMed:15661757, PubMed:15752776, PubMed:25138275). Elongates the
CC glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding
CC repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a
CC heteropolysaccharide (By similarity). Supports the maturation of DAG1
CC more effectively than LARGE1 (PubMed:15752776). In addition, can modify
CC both heparan sulfate (HS)- and chondroitin/dermatan sulfate (CS/DS)-
CC proteoglycans (PGs), namely GPC4, with a glycosaminoglycan (GAG)-like
CC polysaccharide composed of xylose and glucuronic acid to confer laminin
CC binding (By similarity). {ECO:0000250|UniProtKB:Q5XPT3,
CC ECO:0000269|PubMed:15661757, ECO:0000269|PubMed:15752776,
CC ECO:0000269|PubMed:25138275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-
CC beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-
CC [protein] + UDP-alpha-D-xylose = 3-O-[alpha-D-Xyl-(1->3)-beta-D-GlcA-
CC (1->4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-
CC beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:57336, Rhea:RHEA-COMP:17482, Rhea:RHEA-COMP:17483,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:177336, ChEBI:CHEBI:177352;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57337;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-
CC D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-
CC (1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + UDP-alpha-D-glucuronate =
CC 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-
CC beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-
CC GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:67924, Rhea:RHEA-COMP:17484, Rhea:RHEA-COMP:17486,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:177354, ChEBI:CHEBI:177355;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67925;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-
CC (1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-
CC (1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + UDP-
CC alpha-D-xylose = 3-O-{(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-
CC (1->](n+1)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-
CC (1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + H(+)
CC + UDP; Xref=Rhea:RHEA:68368, Rhea:RHEA-COMP:17485, Rhea:RHEA-
CC COMP:17486, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:177354, ChEBI:CHEBI:177355;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68369;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:25138275};
CC Note=Binds 2 Mn(2+) ions per subunit. The xylosyltransferase part binds
CC one Mn(2+) and the beta-1,3-glucuronyltransferase part binds one
CC Mn(2+). {ECO:0000305|PubMed:25138275};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:15661757, ECO:0000269|PubMed:15752776,
CC ECO:0000269|PubMed:25138275}.
CC -!- SUBUNIT: Interacts with B4GAT1. {ECO:0000269|PubMed:19587235}.
CC -!- INTERACTION:
CC Q8N3Y3; O43505: B4GAT1; NbExp=3; IntAct=EBI-2839174, EBI-6138697;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15661757}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in
CC placenta, pancreas and kidney compared to LARGE. Not expressed in
CC brain. {ECO:0000269|PubMed:15752776, ECO:0000269|PubMed:15958417}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC glycosyltransferase 49 family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23791.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC03909.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Glycosyltransferase-like protein LARGE2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_550";
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; AK092526; BAC03909.1; ALT_SEQ; mRNA.
DR EMBL; AK096021; BAC04675.1; -; mRNA.
DR EMBL; AC068385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68021.1; -; Genomic_DNA.
DR EMBL; BC037291; AAH37291.1; -; mRNA.
DR EMBL; AF258588; AAG23791.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31473.1; -.
DR RefSeq; NP_001287650.1; NM_001300721.1.
DR RefSeq; NP_001287651.1; NM_001300722.1.
DR RefSeq; NP_689525.3; NM_152312.4.
DR AlphaFoldDB; Q8N3Y3; -.
DR SMR; Q8N3Y3; -.
DR BioGRID; 125666; 102.
DR DIP; DIP-48923N; -.
DR IntAct; Q8N3Y3; 19.
DR STRING; 9606.ENSP00000432869; -.
DR CAZy; GT49; Glycosyltransferase Family 49.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyConnect; 1278; 1 N-Linked glycan (1 site).
DR GlyGen; Q8N3Y3; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8N3Y3; -.
DR PhosphoSitePlus; Q8N3Y3; -.
DR BioMuta; LARGE2; -.
DR DMDM; 146345450; -.
DR EPD; Q8N3Y3; -.
DR jPOST; Q8N3Y3; -.
DR MassIVE; Q8N3Y3; -.
DR MaxQB; Q8N3Y3; -.
DR PaxDb; Q8N3Y3; -.
DR PeptideAtlas; Q8N3Y3; -.
DR PRIDE; Q8N3Y3; -.
DR ProteomicsDB; 71849; -.
DR Antibodypedia; 64472; 15 antibodies from 8 providers.
DR DNASU; 120071; -.
DR Ensembl; ENST00000325468.9; ENSP00000324570.5; ENSG00000165905.18.
DR Ensembl; ENST00000401752.6; ENSP00000385235.1; ENSG00000165905.18.
DR Ensembl; ENST00000531526.5; ENSP00000432869.1; ENSG00000165905.18.
DR GeneID; 120071; -.
DR KEGG; hsa:120071; -.
DR MANE-Select; ENST00000401752.6; ENSP00000385235.1; NM_001300721.2; NP_001287650.1.
DR UCSC; uc001nbv.1; human.
DR CTD; 120071; -.
DR DisGeNET; 120071; -.
DR GeneCards; LARGE2; -.
DR HGNC; HGNC:16522; LARGE2.
DR HPA; ENSG00000165905; Tissue enhanced (placenta).
DR MIM; 609709; gene.
DR neXtProt; NX_Q8N3Y3; -.
DR OpenTargets; ENSG00000165905; -.
DR PharmGKB; PA142671704; -.
DR VEuPathDB; HostDB:ENSG00000165905; -.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000158758; -.
DR InParanoid; Q8N3Y3; -.
DR OMA; RTACPKQ; -.
DR OrthoDB; 729091at2759; -.
DR PhylomeDB; Q8N3Y3; -.
DR TreeFam; TF319168; -.
DR BioCyc; MetaCyc:ENSG00000165905-MON; -.
DR PathwayCommons; Q8N3Y3; -.
DR Reactome; R-HSA-5173105; O-linked glycosylation.
DR SignaLink; Q8N3Y3; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 120071; 12 hits in 1075 CRISPR screens.
DR GenomeRNAi; 120071; -.
DR Pharos; Q8N3Y3; Tbio.
DR PRO; PR:Q8N3Y3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8N3Y3; protein.
DR Bgee; ENSG00000165905; Expressed in lower esophagus mucosa and 140 other tissues.
DR ExpressionAtlas; Q8N3Y3; baseline and differential.
DR Genevisible; Q8N3Y3; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; TAS:UniProtKB.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; TAS:Reactome.
DR GO; GO:0042285; F:xylosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; TAS:Reactome.
DR GO; GO:0035269; P:protein O-linked mannosylation; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Multifunctional enzyme; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..721
FT /note="Xylosyl- and glucuronyltransferase LARGE2"
FT /id="PRO_0000226811"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..721
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 59..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..372
FT /note="Xylosyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT REGION 373..715
FT /note="Glucuronyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:25138275"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:25138275"
FT BINDING 521
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:25138275"
FT BINDING 523
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:25138275"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 37
FT /note="E -> K (in dbSNP:rs17853729)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031854"
FT VARIANT 546
FT /note="R -> W (in dbSNP:rs11038713)"
FT /id="VAR_031855"
FT VARIANT 677
FT /note="R -> C (in dbSNP:rs2271851)"
FT /id="VAR_025518"
FT CONFLICT 166
FT /note="Q -> R (in Ref. 1; BAC04675)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="E -> G (in Ref. 1; BAC03909)"
FT /evidence="ECO:0000305"
FT CONFLICT 473..474
FT /note="HF -> IS (in Ref. 5; AAG23791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 721 AA; 81787 MW; 7E9E208AAD872344 CRC64;
MLPRGRPRAL GAAALLLLLL LLGFLLFGGD LGCERREPGG RAGAPGCFPG PLMPRVPPDG
RLRRAAALDG DPGAGPGDHN RSDCGPQPPP PPKCELLHVA IVCAGHNSSR DVITLVKSML
FYRKNPLHLH LVTDAVARNI LETLFHTWMV PAVRVSFYHA DQLKPQVSWI PNKHYSGLYG
LMKLVLPSAL PAELARVIVL DTDVTFASDI SELWALFAHF SDTQAIGLVE NQSDWYLGNL
WKNHRPWPAL GRGFNTGVIL LRLDRLRQAG WEQMWRLTAR RELLSLPATS LADQDIFNAV
IKEHPGLVQR LPCVWNVQLS DHTLAERCYS EASDLKVIHW NSPKKLRVKN KHVEFFRNFY
LTFLEYDGNL LRRELFVCPS QPPPGAEQLQ QALAQLDEED PCFEFRQQQL TVHRVHVTFL
PHEPPPPRPH DVTLVAQLSM DRLQMLEALC RHWPGPMSLA LYLTDAEAQQ FLHFVEASPV
LAARQDVAYH VVYREGPLYP VNQLRNVALA QALTPYVFLS DIDFLPAYSL YDYLRASIEQ
LGLGSRRKAA LVVPAFETLR YRFSFPHSKV ELLALLDAGT LYTFRYHEWP RGHAPTDYAR
WREAQAPYRV QWAANYEPYV VVPRDCPRYD PRFVGFGWNK VAHIVELDAQ EYELLVLPEA
FTIHLPHAPS LDISRFRSSP TYRDCLQALK DEFHQDLSRH HGAAALKYLP ALQQPQSPAR
G
