GALT3_MOUSE
ID GALT3_MOUSE Reviewed; 633 AA.
AC P70419; Q3UXL2; Q80V55;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 3;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 3;
DE Short=GalNAc-T3;
DE Short=pp-GaNTase 3;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 3;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3;
GN Name=Galnt3;
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], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=8912633; DOI=10.1006/bbrc.1996.1613;
RA Zara J., Hagen F.K., Ten Hagen K.G., Van Wuyckhuyse B.C., Tabak L.A.;
RT "Cloning and expression of mouse UDP-GalNAc:polypeptide N-
RT acetylgalactosaminyltransferase-T3.";
RL Biochem. Biophys. Res. Commun. 228:38-44(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Muellerian duct;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. Has activity
CC toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5.
CC Glycosylates FGF23 (By similarity). Probably glycosylates fibronectin
CC in vivo. May be involved in phosphate homeostasis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:8912633};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:8912633};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Resides preferentially in the trans and medial parts of the Golgi
CC stack. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the reproductive tract,
CC principally in the testis and uterus, and to a lesser degree in the
CC cervix with only trace levels in the ovary. Also expressed at high
CC level in sublingual gland, stomach and colon, with more moderate
CC amounts present in the submandibular and parotid gland as well as the
CC kidney. {ECO:0000269|PubMed:8912633}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 3;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_512";
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DR EMBL; U70538; AAB09579.1; -; mRNA.
DR EMBL; AK135489; BAE22551.1; -; mRNA.
DR EMBL; AL928586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27008.1; -; Genomic_DNA.
DR EMBL; BC043331; AAH43331.1; -; mRNA.
DR CCDS; CCDS16075.1; -.
DR PIR; JC5247; JC5247.
DR RefSeq; NP_056551.2; NM_015736.2.
DR AlphaFoldDB; P70419; -.
DR SMR; P70419; -.
DR STRING; 10090.ENSMUSP00000028378; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; P70419; 2 sites.
DR iPTMnet; P70419; -.
DR PhosphoSitePlus; P70419; -.
DR EPD; P70419; -.
DR jPOST; P70419; -.
DR MaxQB; P70419; -.
DR PaxDb; P70419; -.
DR PeptideAtlas; P70419; -.
DR PRIDE; P70419; -.
DR ProteomicsDB; 268841; -.
DR Antibodypedia; 2358; 171 antibodies from 24 providers.
DR DNASU; 14425; -.
DR Ensembl; ENSMUST00000028378; ENSMUSP00000028378; ENSMUSG00000026994.
DR GeneID; 14425; -.
DR KEGG; mmu:14425; -.
DR UCSC; uc008jwu.2; mouse.
DR CTD; 2591; -.
DR MGI; MGI:894695; Galnt3.
DR VEuPathDB; HostDB:ENSMUSG00000026994; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000156609; -.
DR HOGENOM; CLU_013477_0_3_1; -.
DR InParanoid; P70419; -.
DR OMA; NGEHPNL; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; P70419; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 3474.
DR Reactome; R-MMU-190372; FGFR3c ligand binding and activation.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14425; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Galnt3; mouse.
DR PRO; PR:P70419; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P70419; protein.
DR Bgee; ENSMUSG00000026994; Expressed in parotid gland and 152 other tissues.
DR Genevisible; P70419; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; ISO:MGI.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; ISO:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:MGI.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISO:MGI.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..633
FT /note="Polypeptide N-acetylgalactosaminyltransferase 3"
FT /id="PRO_0000059107"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..633
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 504..630
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 112..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..293
FT /note="Catalytic subdomain A"
FT REGION 356..418
FT /note="Catalytic subdomain B"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 173..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 401..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 517..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 561..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 605..618
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 324
FT /note="S -> N (in Ref. 5; AAH43331)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="D -> E (in Ref. 1; AAB09579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 72932 MW; 8BEE7CDDBCF56428 CRC64;
MAHLKRLVKL HIKRHYHRKF WKLGAVIFFF LVVLILMQRE VSVQYSKEES KMERNLKNKN
KMLDFMLEAV NNIKDAMPKM QIGAPIKENI DVRERPCLQG YYTAAELKPV FDRPPQDSNA
PGASGKPFKI THLSPEEQKE KERGETKHCF NAFASDRISL HRDLGPDTRP PECIEQKFKR
CPPLPTTSVI IVFHNEAWST LLRTVHSVLY SSPAILLKEI ILVDDASVDD YLHEKLEEYI
KQFSIVKIVR QQERKGLITA RLLGAAVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA
VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR KDETYPIKTP
TFAGGLFSIS KKYFEHIGSY DEEMEIWGGE NIEMSFRVWQ CGGQLEIMPC SVVGHVFRSK
SPHTFPKGTQ VIARNQVRLA EVWMDEYKEI FYRRNTDAAK IVKQKSFGDL SKRFEIKKRL
QCKNFTWYLN TIYPEAYVPD LNPVISGYIK SVGQPLCLDV GENNQGGKPL ILYTCHGLGG
NQYFEYSAQR EIRHNIQKEL CLHATQGVVQ LKACVYKGHR TIAPGEQIWE IRKDQLLYNP
LFKMCLSSNG EHPNLVPCDA TDLLQKWIFS QND
