LARG2_MOUSE
ID LARG2_MOUSE Reviewed; 690 AA.
AC Q5XPT3; A2AHG9; Q5XPT2; Q8BJZ8; Q8K253;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Xylosyl- and glucuronyltransferase LARGE2 {ECO:0000305};
DE EC=2.4.-.- {ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544};
DE AltName: Full=Glycosyltransferase-like 1B;
DE AltName: Full=LARGE xylosyl- and glucuronyltransferase 2 {ECO:0000312|MGI:MGI:2443769};
DE Includes:
DE RecName: Full=Alpha-1,3-xylosyltransferase LARGE2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544};
DE Includes:
DE RecName: Full=Beta-1,3-glucuronyltransferase LARGE2 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544};
GN Name=Large2 {ECO:0000312|MGI:MGI:2443769}; Synonyms=Gyltl1b;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Lung, and Mammary tumor;
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 FUNCTION, PATHWAY, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23125099; DOI=10.1093/glycob/cws152;
RA Inamori K., Hara Y., Willer T., Anderson M.E., Zhu Z.,
RA Yoshida-Moriguchi T., Campbell K.P.;
RT "Xylosyl- and glucuronyltransferase functions of LARGE in alpha-
RT dystroglycan modification are conserved in LARGE2.";
RL Glycobiology 23:295-302(2013).
RN [6]
RP FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=23135544; DOI=10.1093/glycob/cws153;
RA Ashikov A., Buettner F.F., Tiemann B., Gerardy-Schahn R., Bakker H.;
RT "LARGE2 generates the same xylose- and glucuronic acid-containing glycan
RT structures as LARGE.";
RL Glycobiology 23:303-309(2013).
RN [7]
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).
RN [8]
RP FUNCTION.
RX PubMed=27496765; DOI=10.1093/glycob/cww075;
RA Inamori K.I., Beedle A.M., de Bernabe D.B., Wright M.E., Campbell K.P.;
RT "LARGE2-dependent glycosylation confers laminin-binding ability on
RT proteoglycans.";
RL Glycobiology 26:1284-1296(2016).
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:15958417, PubMed:23125099, PubMed:23135544, PubMed:25138275).
CC Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer
CC structure by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-]
CC to produce a heteropolysaccharide (PubMed:23125099, PubMed:23135544,
CC PubMed:25138275). Supports the maturation of DAG1 more effectively than
CC LARGE1 (By similarity). In addition, can modify both heparan sulfate
CC (HS)- and chondroitin/dermatan sulfate (CS/DS)-proteoglycans (PGs),
CC namely GPC4, with a glycosaminoglycan (GAG)-like polysaccharide
CC composed of xylose and glucuronic acid to confer laminin binding
CC (PubMed:27496765). {ECO:0000250|UniProtKB:Q8N3Y3,
CC ECO:0000269|PubMed:15958417, ECO:0000269|PubMed:23125099,
CC ECO:0000269|PubMed:23135544, ECO:0000269|PubMed:25138275,
CC ECO:0000269|PubMed:27496765}.
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:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57337;
CC Evidence={ECO:0000305|PubMed:23125099, ECO:0000305|PubMed:23135544};
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:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67925;
CC Evidence={ECO:0000305|PubMed:23125099, ECO:0000305|PubMed:23135544};
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:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68369;
CC Evidence={ECO:0000305|PubMed:23125099, ECO:0000305|PubMed:23135544};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|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:0000269|PubMed:25138275};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is from 5.5 to 9.0 for xylosyltransferase activity.
CC Optimum pH is 5.5 for Beta-1,3-glucuronyltransferase activity.
CC {ECO:0000269|PubMed:23125099};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544}.
CC -!- SUBUNIT: Interacts with B4GAT1. {ECO:0000250|UniProtKB:Q8N3Y3}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15958417}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5XPT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XPT3-2; Sequence=VSP_017489;
CC Name=3;
CC IsoId=Q5XPT3-3; Sequence=VSP_041607, VSP_041608;
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis and kidney, but
CC weakly expressed in the heart and brain. Expressed during embryogenesis
CC from 7 dpc. {ECO:0000269|PubMed:15958417}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36913.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AY742914; AAU95213.1; -; mRNA.
DR EMBL; AY742915; AAU95214.1; -; mRNA.
DR EMBL; AK077630; BAC36913.1; ALT_SEQ; mRNA.
DR EMBL; AL731709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033922; AAH33922.1; -; mRNA.
DR EMBL; BC096655; AAH96655.1; -; mRNA.
DR CCDS; CCDS16443.2; -. [Q5XPT3-1]
DR CCDS; CCDS50646.1; -. [Q5XPT3-2]
DR RefSeq; NP_001160105.1; NM_001166633.2. [Q5XPT3-2]
DR RefSeq; NP_001277702.1; NM_001290773.1.
DR RefSeq; NP_001277703.1; NM_001290774.1.
DR RefSeq; NP_001277704.1; NM_001290775.1.
DR RefSeq; NP_766258.2; NM_172670.3. [Q5XPT3-1]
DR AlphaFoldDB; Q5XPT3; -.
DR SMR; Q5XPT3; -.
DR STRING; 10090.ENSMUSP00000064128; -.
DR CAZy; GT49; Glycosyltransferase Family 49.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyGen; Q5XPT3; 3 sites.
DR iPTMnet; Q5XPT3; -.
DR PhosphoSitePlus; Q5XPT3; -.
DR PaxDb; Q5XPT3; -.
DR PRIDE; Q5XPT3; -.
DR ProteomicsDB; 264833; -. [Q5XPT3-1]
DR ProteomicsDB; 264834; -. [Q5XPT3-2]
DR Antibodypedia; 64472; 15 antibodies from 8 providers.
DR DNASU; 228366; -.
DR Ensembl; ENSMUST00000068586; ENSMUSP00000064128; ENSMUSG00000040434. [Q5XPT3-1]
DR Ensembl; ENSMUST00000090582; ENSMUSP00000088070; ENSMUSG00000040434. [Q5XPT3-2]
DR Ensembl; ENSMUST00000176289; ENSMUSP00000135118; ENSMUSG00000040434. [Q5XPT3-3]
DR GeneID; 228366; -.
DR KEGG; mmu:228366; -.
DR UCSC; uc008kxn.3; mouse. [Q5XPT3-1]
DR UCSC; uc008kxp.3; mouse. [Q5XPT3-2]
DR CTD; 120071; -.
DR MGI; MGI:2443769; Large2.
DR VEuPathDB; HostDB:ENSMUSG00000040434; -.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000158758; -.
DR InParanoid; Q5XPT3; -.
DR OMA; RTACPKQ; -.
DR TreeFam; TF319168; -.
DR BRENDA; 2.4.1.B80; 3474.
DR BRENDA; 2.4.2.B18; 3474.
DR Reactome; R-MMU-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 228366; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Gyltl1b; mouse.
DR PRO; PR:Q5XPT3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q5XPT3; protein.
DR Bgee; ENSMUSG00000040434; Expressed in nasolacrimal duct and 119 other tissues.
DR ExpressionAtlas; Q5XPT3; baseline and differential.
DR Genevisible; Q5XPT3; MM.
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:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
DR GO; GO:0002162; F:dystroglycan binding; IDA:MGI.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042285; F:xylosyltransferase activity; IDA:UniProtKB.
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 Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Multifunctional enzyme;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..690
FT /note="Xylosyl- and glucuronyltransferase LARGE2"
FT /id="PRO_0000226812"
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..690
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 68..343
FT /note="Xylosyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT REGION 344..686
FT /note="Glucuronyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT BINDING 492
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT BINDING 494
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 67..76
FT /note="MLHVAIVCAG -> EKSAAPPPDN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041607"
FT VAR_SEQ 77..690
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041608"
FT VAR_SEQ 193..227
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15958417"
FT /id="VSP_017489"
FT CONFLICT 144
FT /note="K -> N (in Ref. 2; BAC36913)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="S -> R (in Ref. 4; AAH33922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 79514 MW; 76AE2A4E8B87930E CRC64;
MLPRGRPRAM GAAVLLLLLL LVVGFFLFGR DPDYGLGTTA TLDEDPYRSR NLSASSPQLL
LPPKCEMLHV AIVCAGYNSS REIITLTKSL LFYRKNPLHL HLITDAVARN ILETLFRTWM
VPAVVVSFYD AEELKPLVSW IPNKHYSGLY GLMKLVLPSI LPPSLARVIV LDTDVTFSSD
IVELWALFDH FSDKQVVGLV ENQSDWYLGN LWKNHRPWPA LGRGFNTGVI LLWLDRLQQT
GWEQMWKVTA KRELLTLMAT SLADQDIFNA VIKEHPHLVH PLPCVWNVQL SDHTRAERCY
LEAADLKVIH WNSPKKLRVK NKHAEFFRNL HLTFLGYDGK LLRRELFGCP NQFPPGAEQL
QQALTQLDEE EPCFEFRQQQ LTVHRVHITF LPHQPPPPQP HDVTLVAQLS MDRLQMLEAL
CRHWPGPMSL ALYLTDEEAQ QFLHFVETSP VLSMRKDVAY HVVYRDGPLY PVNQLRNVAL
AQALTPYVFL SDIDFLPAYS LYDYLRASIE QLELDSRRKT ALVVPAFETL HYRFSFPNSK
AELLTLLDAG SLHTFRYHEW PQGHSSTDYS RWREAQAPYS VQWSADYEPY VVVPRDCPRY
DPRFVGFGWN KVAHIIELDA QEYEFLVLPE AFSIHLPHAP SLDISRFRSS PTYRNCLQAL
KEEFHQDLSR RYGSAALKYL TALQQARSRA
