B3GL2_MOUSE
ID B3GL2_MOUSE Reviewed; 504 AA.
AC Q8BG28; Q5U4F9; Q8BXL0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2;
DE Short=Beta-1,3-GalNAc-T2;
DE EC=2.4.1.313 {ECO:0000250|UniProtKB:Q8NCR0};
DE AltName: Full=Beta-1,3-N-acetylgalactosaminyltransferase II;
GN Name=B3galnt2;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=14724282; DOI=10.1074/jbc.m310614200;
RA Hiruma T., Togayachi A., Okamura K., Sato T., Kikuchi N., Kwon Y.D.,
RA Nakamura A., Fujimura K., Gotoh M., Tachibana K., Ishizuka Y., Noce T.,
RA Nakanishi H., Narimatsu H.;
RT "A novel human beta1,3-N-acetylgalactosaminyltransferase that synthesizes a
RT unique carbohydrate structure, GalNAcbeta1-3GlcNAc.";
RL J. Biol. Chem. 279:14087-14095(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Aorta, Bone marrow, Eye, Placenta, Retina, Urinary bladder, and
RC Vein;
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 MRNA] (ISOFORM 1).
RC TISSUE=Trophoblast stem cell;
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).
CC -!- FUNCTION: Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a
CC unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-
CC glycans. Has no galactose nor galactosaminyl transferase activity
CC toward any acceptor substrate. Involved in alpha-dystroglycan (DAG1)
CC glycosylation: acts coordinately with GTDC2/POMGnT2 to synthesize a
CC GalNAc-beta3-GlcNAc-beta-terminus at the 4-position of protein O-
CC mannose in the biosynthesis of the phosphorylated O-mannosyl
CC trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-
CC (phosphate-6-)mannose), a carbohydrate structure present in alpha-
CC dystroglycan, which is required for binding laminin G-like domain-
CC containing extracellular proteins with high affinity (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl)-L-
CC threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[beta-
CC D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-alpha-D-Man]-L-Thr-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:37667, Rhea:RHEA-COMP:13308, Rhea:RHEA-
CC COMP:13618, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:136709, ChEBI:CHEBI:137540; EC=2.4.1.313;
CC Evidence={ECO:0000250|UniProtKB:Q8NCR0};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BG28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BG28-2; Sequence=VSP_020253, VSP_020254;
CC -!- TISSUE SPECIFICITY: Present in testis (at protein level). In testis, it
CC is mainly detected in the middle layers of seminiferous tubules at
CC stages XII to II. Strongly expressed in primary and secondary
CC spermatocytes and early round spermatids, but not in spermatogonia,
CC elongating or elongated spermatids, or in Leydig or Sertoli cells.
CC {ECO:0000269|PubMed:14724282}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AB116655; BAD13421.1; -; mRNA.
DR EMBL; AK035259; BAC29004.1; -; mRNA.
DR EMBL; AK041022; BAC30784.1; -; mRNA.
DR EMBL; AK044785; BAC32091.1; -; mRNA.
DR EMBL; AK084275; BAC39153.1; -; mRNA.
DR EMBL; AK151677; BAE30602.1; -; mRNA.
DR EMBL; AK153362; BAE31934.1; -; mRNA.
DR EMBL; AK167635; BAE39686.1; -; mRNA.
DR EMBL; BC085110; AAH85110.1; -; mRNA.
DR CCDS; CCDS26246.1; -. [Q8BG28-1]
DR RefSeq; NP_848755.1; NM_178640.2. [Q8BG28-1]
DR AlphaFoldDB; Q8BG28; -.
DR SMR; Q8BG28; -.
DR STRING; 10090.ENSMUSP00000097336; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q8BG28; 2 sites.
DR iPTMnet; Q8BG28; -.
DR PhosphoSitePlus; Q8BG28; -.
DR EPD; Q8BG28; -.
DR MaxQB; Q8BG28; -.
DR PaxDb; Q8BG28; -.
DR PRIDE; Q8BG28; -.
DR ProteomicsDB; 277094; -. [Q8BG28-1]
DR ProteomicsDB; 277095; -. [Q8BG28-2]
DR Antibodypedia; 1593; 119 antibodies from 22 providers.
DR Ensembl; ENSMUST00000099747; ENSMUSP00000097336; ENSMUSG00000039242. [Q8BG28-1]
DR Ensembl; ENSMUST00000221300; ENSMUSP00000152755; ENSMUSG00000039242. [Q8BG28-1]
DR Ensembl; ENSMUST00000221974; ENSMUSP00000152397; ENSMUSG00000039242. [Q8BG28-1]
DR GeneID; 97884; -.
DR KEGG; mmu:97884; -.
DR UCSC; uc007pmm.1; mouse. [Q8BG28-2]
DR UCSC; uc007pmn.1; mouse. [Q8BG28-1]
DR CTD; 148789; -.
DR MGI; MGI:2145517; B3galnt2.
DR VEuPathDB; HostDB:ENSMUSG00000039242; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000156562; -.
DR HOGENOM; CLU_591287_0_0_1; -.
DR InParanoid; Q8BG28; -.
DR OMA; EKTCESG; -.
DR OrthoDB; 640360at2759; -.
DR PhylomeDB; Q8BG28; -.
DR TreeFam; TF314311; -.
DR Reactome; R-MMU-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 97884; 5 hits in 70 CRISPR screens.
DR ChiTaRS; B3galnt2; mouse.
DR PRO; PR:Q8BG28; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BG28; protein.
DR Bgee; ENSMUSG00000039242; Expressed in muscle of arm and 256 other tissues.
DR ExpressionAtlas; Q8BG28; baseline and differential.
DR Genevisible; Q8BG28; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0019276; P:UDP-N-acetylgalactosamine metabolic process; ISO:MGI.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..504
FT /note="UDP-GalNAc:beta-1,3-N-
FT acetylgalactosaminyltransferase 2"
FT /id="PRO_0000248363"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..504
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 188..209
FT /note="EALFIARFSPPSCGVQVNKLWY -> VCTGMDRIFLLLKQLFFVVPID (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020253"
FT VAR_SEQ 210..504
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020254"
FT CONFLICT 60
FT /note="S -> P (in Ref. 3; AAH85110)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="S -> G (in Ref. 3; AAH85110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 57219 MW; CF23C733C84AC6C0 CRC64;
MRNWLVLLCP CVLGAALHLW HLWLRSPPDP HNTGPSAADQ SALFPHWKFS HYDVVVGVLS
ARNNHELRNV IRNTWLKNLL HHPTLSQRVL VKFIIGARGC EVPVEDREDP YSCRLLNITN
PVLNQEIEAF SFPEDASSSR LSEDRVVSVS FRVLYPIVIT SLGVFYDASD VGFQRNITVK
LYQTEQEEAL FIARFSPPSC GVQVNKLWYK PVEQFILPES FEGTIVWESQ DLHGLVSRNL
HRVTVNDGGG VLRVLAAGEG ALPHEFMEGV EGVAGGFIYT VQEGDALLRS LYSRPQRLAD
HIQDLQVEDA LLQEESSVHD DIVFVDVVDT YRNVPAKLLN FYRWTVESTS FDLLLKTDDD
CYIDLEAVFN RIAQKNLDGP NFWWGNFRLN WAVDRTGKWQ ELEYPSPAYP AFACGSGYVI
SKDIVDWLAG NSRRLKTYQG EDVSMGIWMA AIGPKRHQDS LWLCEKTCET GMLSSPQYSP
EELSKLWELK ELCGDPCQCE AKVR
