MGT5B_HUMAN
ID MGT5B_HUMAN Reviewed; 792 AA.
AC Q3V5L5; Q6P3S8; Q6P6B3; Q766X5; Q76D04; Q96LS2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B;
DE EC=2.4.1.- {ECO:0000269|PubMed:19846580};
DE EC=2.4.1.155 {ECO:0000269|PubMed:12941944, ECO:0000269|PubMed:14623122, ECO:0000269|PubMed:19846580};
DE AltName: Full=Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase B;
DE AltName: Full=GlcNAc-T Vb {ECO:0000303|PubMed:19846580};
DE Short=GNT-Vb {ECO:0000303|PubMed:16857188, ECO:0000303|PubMed:19846580};
DE Short=hGnTVb;
DE AltName: Full=Mannoside acetylglucosaminyltransferase 5B;
DE AltName: Full=N-acetylglucosaminyl-transferase Vb;
DE AltName: Full=N-acetylglucosaminyltransferase IX {ECO:0000303|PubMed:14617637};
DE Short=GNT-IX {ECO:0000303|PubMed:19846580};
GN Name=MGAT5B; Synonyms=KIAA2008;
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 2), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=14623122; DOI=10.1016/s0014-5793(03)01234-1;
RA Kaneko M., Alvarez-Manilla G., Kamar M., Lee I., Lee J.-K., Troupe K.,
RA Zhang W., Osawa M., Pierce M.;
RT "A novel beta(1,6)-N-acetylglucosaminyltransferase V (GnT-VB).";
RL FEBS Lett. 554:515-519(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, FUNCTION,
RP PATHWAY, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12941944; DOI=10.1074/jbc.m308255200;
RA Inamori K., Endo T., Ide Y., Fujii S., Gu J., Honke K., Taniguchi N.;
RT "Molecular cloning and characterization of human GnT-IX, a novel beta1,6-N-
RT acetylglucosaminyltransferase that is specifically expressed in the
RT brain.";
RL J. Biol. Chem. 278:43102-43109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-341 (ISOFORMS 1/3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 616-792.
RC TISSUE=PNS, and Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-306.
RC TISSUE=Brain;
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 [7]
RP FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=14617637; DOI=10.1074/jbc.c300480200;
RA Inamori K., Endo T., Gu J., Matsuo I., Ito Y., Fujii S., Iwasaki H.,
RA Narimatsu H., Miyoshi E., Honke K., Taniguchi N.;
RT "N-Acetylglucosaminyltransferase IX acts on the GlcNAc beta 1,2-Man alpha
RT 1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl
RT glycan.";
RL J. Biol. Chem. 279:2337-2340(2004).
RN [8]
RP FUNCTION.
RX PubMed=16857188; DOI=10.1016/j.yexcr.2006.05.022;
RA Abbott K.L., Troupe K., Lee I., Pierce M.;
RT "Integrin-dependent neuroblastoma cell adhesion and migration on laminin is
RT regulated by expression levels of two enzymes in the O-mannosyl-linked
RT glycosylation pathway, PomGnT1 and GnT-Vb.";
RL Exp. Cell Res. 312:2837-2850(2006).
RN [9]
RP FUNCTION.
RX PubMed=16606368; DOI=10.1111/j.1471-4159.2006.03785.x;
RA Lee I., Guo H.-B., Kamar M., Abbott K., Troupe K., Lee J.-K.,
RA Alvarez-Manilla G., Pierce M.;
RT "N-acetylglucosaminyltransferase VB expression enhances beta1 integrin-
RT dependent PC12 neurite outgrowth on laminin and collagen.";
RL J. Neurochem. 97:947-956(2006).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=19846580; DOI=10.1093/glycob/cwp158;
RA Alvarez-Manilla G., Troupe K., Fleming M., Martinez-Uribe E., Pierce M.;
RT "Comparison of the substrate specificities and catalytic properties of the
RT sister N-acetylglucosaminyltransferases, GnT-V and GnT-Vb (IX).";
RL Glycobiology 20:166-174(2010).
CC -!- FUNCTION: Glycosyltransferase that acts on alpha-linked mannose of N-
CC glycans and O-mannosyl glycans. Catalyzes the transfer of N-
CC acetylglucosamine (GlcNAc) to the beta 1-6 linkage of the mannose
CC residue of GlcNAc-beta1,2-Man-alpha on both the alpha1,3- and alpha1,6-
CC linked mannose arms in the core structure of N-glycan. Also acts on the
CC GlcNAc-beta1,2-Man-alpha1-Ser/Thr moiety, forming a 2,6-branched
CC structure in brain O-mannosyl glycan. Plays an active role in
CC modulating integrin and laminin-dependent adhesion and migration of
CC neuronal cells via its activity in the O-mannosyl glycan pathway.
CC {ECO:0000269|PubMed:12941944, ECO:0000269|PubMed:14617637,
CC ECO:0000269|PubMed:14623122, ECO:0000269|PubMed:16606368,
CC ECO:0000269|PubMed:16857188, ECO:0000269|PubMed:19846580}.
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:12941944, ECO:0000269|PubMed:14623122,
CC ECO:0000269|PubMed:19846580};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl]-L-
CC seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + O(3)-{N-
CC acetyl-beta-D-glucosaminyl-(1->2)-[N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-alpha-D-mannosyl}-L-seryl-[protein] + UDP;
CC Xref=Rhea:RHEA:56252, Rhea:RHEA-COMP:14438, Rhea:RHEA-COMP:14440,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:140080, ChEBI:CHEBI:140085;
CC Evidence={ECO:0000269|PubMed:12941944, ECO:0000269|PubMed:14617637,
CC ECO:0000269|PubMed:14623122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl]-L-
CC threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC O(3)-{N-acetyl-beta-D-glucosaminyl-(1->2)-[N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-alpha-D-mannosyl}-L-threonyl-[protein] + UDP;
CC Xref=Rhea:RHEA:56256, Rhea:RHEA-COMP:14439, Rhea:RHEA-COMP:14441,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:140083, ChEBI:CHEBI:140087;
CC Evidence={ECO:0000269|PubMed:12941944, ECO:0000269|PubMed:14617637,
CC ECO:0000269|PubMed:14623122, ECO:0000269|PubMed:19846580};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:14623122, ECO:0000269|PubMed:19846580};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.56 mM for UDP-GlcNAc {ECO:0000269|PubMed:19846580};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:19846580};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:12941944, ECO:0000269|PubMed:14617637,
CC ECO:0000269|PubMed:14623122, ECO:0000269|PubMed:19846580}.
CC -!- INTERACTION:
CC Q3V5L5; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-3957727, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q765H6}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q765H6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3V5L5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3V5L5-2; Sequence=VSP_025731, VSP_025734;
CC Name=3;
CC IsoId=Q3V5L5-5; Sequence=VSP_025734;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Expressed in all
CC areas of the adult and fetal brain. Also expressed at much lower levels
CC in testis, spleen and thymus. {ECO:0000269|PubMed:12941944,
CC ECO:0000269|PubMed:14623122}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 18 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH62354.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAH63862.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAB71598.1; Type=Miscellaneous discrepancy; Note=Chimeric sequence.; Evidence={ECO:0000305};
CC Sequence=BAD02406.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE44474.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB114297; BAD02406.1; ALT_INIT; mRNA.
DR EMBL; AB109185; BAC84969.1; -; mRNA.
DR EMBL; AB235153; BAE44474.1; ALT_INIT; mRNA.
DR EMBL; AC016168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062354; AAH62354.1; ALT_SEQ; mRNA.
DR EMBL; BC063862; AAH63862.1; ALT_SEQ; mRNA.
DR EMBL; AK057861; BAB71598.1; ALT_SEQ; mRNA.
DR CCDS; CCDS11751.1; -. [Q3V5L5-5]
DR CCDS; CCDS45788.1; -. [Q3V5L5-2]
DR CCDS; CCDS59299.1; -. [Q3V5L5-1]
DR RefSeq; NP_001186101.1; NM_001199172.1. [Q3V5L5-1]
DR RefSeq; NP_653278.2; NM_144677.2. [Q3V5L5-5]
DR RefSeq; NP_945193.1; NM_198955.1. [Q3V5L5-2]
DR AlphaFoldDB; Q3V5L5; -.
DR SMR; Q3V5L5; -.
DR BioGRID; 127000; 117.
DR IntAct; Q3V5L5; 5.
DR MINT; Q3V5L5; -.
DR STRING; 9606.ENSP00000391227; -.
DR CAZy; GT18; Glycosyltransferase Family 18.
DR GlyGen; Q3V5L5; 1 site.
DR iPTMnet; Q3V5L5; -.
DR PhosphoSitePlus; Q3V5L5; -.
DR BioMuta; MGAT5B; -.
DR DMDM; 152040009; -.
DR jPOST; Q3V5L5; -.
DR MassIVE; Q3V5L5; -.
DR MaxQB; Q3V5L5; -.
DR PaxDb; Q3V5L5; -.
DR PeptideAtlas; Q3V5L5; -.
DR PRIDE; Q3V5L5; -.
DR ProteomicsDB; 61881; -. [Q3V5L5-1]
DR ProteomicsDB; 61882; -. [Q3V5L5-2]
DR ProteomicsDB; 61885; -. [Q3V5L5-5]
DR Antibodypedia; 46175; 61 antibodies from 18 providers.
DR DNASU; 146664; -.
DR Ensembl; ENST00000301618.8; ENSP00000301618.4; ENSG00000167889.13. [Q3V5L5-5]
DR Ensembl; ENST00000428789.6; ENSP00000391227.2; ENSG00000167889.13. [Q3V5L5-2]
DR Ensembl; ENST00000569840.7; ENSP00000456037.2; ENSG00000167889.13. [Q3V5L5-1]
DR GeneID; 146664; -.
DR KEGG; hsa:146664; -.
DR MANE-Select; ENST00000569840.7; ENSP00000456037.2; NM_001199172.2; NP_001186101.1.
DR UCSC; uc002jth.4; human. [Q3V5L5-1]
DR CTD; 146664; -.
DR DisGeNET; 146664; -.
DR GeneCards; MGAT5B; -.
DR HGNC; HGNC:24140; MGAT5B.
DR HPA; ENSG00000167889; Tissue enriched (brain).
DR MIM; 612441; gene.
DR neXtProt; NX_Q3V5L5; -.
DR OpenTargets; ENSG00000167889; -.
DR PharmGKB; PA134987427; -.
DR VEuPathDB; HostDB:ENSG00000167889; -.
DR eggNOG; ENOG502QWJG; Eukaryota.
DR GeneTree; ENSGT00940000153470; -.
DR HOGENOM; CLU_016749_0_0_1; -.
DR InParanoid; Q3V5L5; -.
DR OMA; ASIWKFQ; -.
DR OrthoDB; 179031at2759; -.
DR PhylomeDB; Q3V5L5; -.
DR TreeFam; TF313714; -.
DR BioCyc; MetaCyc:HS15606-MON; -.
DR PathwayCommons; Q3V5L5; -.
DR SignaLink; Q3V5L5; -.
DR SIGNOR; Q3V5L5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 146664; 20 hits in 1073 CRISPR screens.
DR ChiTaRS; MGAT5B; human.
DR GeneWiki; MGAT5B; -.
DR GenomeRNAi; 146664; -.
DR Pharos; Q3V5L5; Tbio.
DR PRO; PR:Q3V5L5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q3V5L5; protein.
DR Bgee; ENSG00000167889; Expressed in right frontal lobe and 127 other tissues.
DR ExpressionAtlas; Q3V5L5; baseline and differential.
DR Genevisible; Q3V5L5; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030144; F:alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:UniProtKB.
DR InterPro; IPR026116; GlyclTrfase_18.
DR Pfam; PF15024; Glyco_transf_18; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..792
FT /note="Alpha-1,6-mannosylglycoprotein 6-beta-N-
FT acetylglucosaminyltransferase B"
FT /id="PRO_0000288611"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..792
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 157..195
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 168..208
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 184..353
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 387..644
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 700..775
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 704..777
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 711..764
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 732..753
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 788..791
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT VAR_SEQ 1..22
FT /note="MITVNPDGKIMVRRCLVTLRPF -> MHSFVKHLCSRYVVERQGTMALPALL
FT TRLLPLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14623122"
FT /id="VSP_025731"
FT VAR_SEQ 475..476
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14623122"
FT /id="VSP_025734"
FT VARIANT 70
FT /note="V -> I (in dbSNP:rs571264)"
FT /id="VAR_032452"
SQ SEQUENCE 792 AA; 89535 MW; C2EB9445FDBE9429 CRC64;
MITVNPDGKI MVRRCLVTLR PFRLFVLGIG FFTLCFLMTS LGGQFSARRL GDSPFTIRTE
VMGGPESRGV LRKMSDLLEL MVKRMDALAR LENSSELHRA GGDLHFPADR MPPGAGLMER
IQAIAQNVSD IAVKVDQILR HSLLLHSKVS EGRRDQCEAP SDPKFPDCSG KVEWMRARWT
SDPCYAFFGV DGTECSFLIY LSEVEWFCPP LPWRNQTAAQ RAPKPLPKVQ AVFRSNLSHL
LDLMGSGKES LIFMKKRTKR LTAQWALAAQ RLAQKLGATQ RDQKQILVHI GFLTEESGDV
FSPRVLKGGP LGEMVQWADI LTALYVLGHG LRVTVSLKEL QSNLGVPPGR GSCPLTMPLP
FDLIYTDYHG LQQMKRHMGL SFKKYRCRIR VIDTFGTEPA YNHEEYATLH GYRTNWGYWN
LNPKQFMTMF PHTPDNSFMG FVSEELNETE KRLIKGGKAS NMAVVYGKEA SIWKLQGKEK
FLGILNKYME IHGTVYYESQ RPPEVPAFVK NHGLLPQPEF QQLLRKAKLF IGFGFPYEGP
APLEAIANGC IFLQSRFSPP HSSLNHEFFR GKPTSREVFS QHPYAENFIG KPHVWTVDYN
NSEEFEAAIK AIMRTQVDPY LPYEYTCEGM LERIHAYIQH QDFCRAPDPA LPEAHAPQSP
FVLAPNATHL EWARNTSLAP GAWPPAHALR AWLAVPGRAC TDTCLDHGLI CEPSFFPFLN
SQDAFLKLQV PCDSTESEMN HLYPAFAQPG QECYLQKEPL LFSCAGSNTK YRRLCPCRDF
RKGQVALCQG CL
