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   24-JAN-2024, entry version 167.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 3;
DE            EC=2.4.1.41 {ECO:0000269|PubMed:8912633};
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   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 (PubMed:8912633).
CC       Has activity toward HIV envelope glycoprotein gp120 (By similarity).
CC       Has activity towards EA2, MUC2 and MUC5 (PubMed:8912633). Probably
CC       glycosylates fibronectin in vivo (By similarity). Glycosylates FGF23
CC       (By similarity). {ECO:0000250|UniProtKB:Q14435,
CC       ECO:0000269|PubMed:8912633}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q14435};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250|UniProtKB:Q14435}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q14435}. Note=Resides preferentially in the
CC       trans and medial parts of the Golgi stack.
CC       {ECO:0000250|UniProtKB:Q14435}.
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|UniProtKB:O08912}.
CC   -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC       to the glycopeptide specificity (By similarity). Essential for
CC       glycosylation of FGF23 (By similarity). {ECO:0000250|UniProtKB:Q14435,
CC       ECO:0000250|UniProtKB:Q8N4A0}.
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   GlyCosmos; P70419; 2 sites, No reported glycans.
DR   GlyGen; P70419; 2 sites.
DR   iPTMnet; P70419; -.
DR   PhosphoSitePlus; P70419; -.
DR   SwissPalm; P70419; -.
DR   EPD; P70419; -.
DR   jPOST; P70419; -.
DR   MaxQB; P70419; -.
DR   PaxDb; 10090-ENSMUSP00000028378; -.
DR   PeptideAtlas; P70419; -.
DR   ProteomicsDB; 268841; -.
DR   Antibodypedia; 2358; 196 antibodies from 25 providers.
DR   DNASU; 14425; -.
DR   Ensembl; ENSMUST00000028378.4; ENSMUSP00000028378.4; ENSMUSG00000026994.10.
DR   GeneID; 14425; -.
DR   KEGG; mmu:14425; -.
DR   UCSC; uc008jwu.2; mouse.
DR   AGR; MGI:894695; -.
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; NPLFKMC; -.
DR   OrthoDB; 202750at2759; -.
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 76 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 155 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
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; 2.80.10.50; -; 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   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF33; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   Genevisible; P70419; MM.
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         277
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         279
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         415
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         519
FT                   /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:67138"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         522
FT                   /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:67138"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         536
FT                   /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:67138"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         541
FT                   /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:67138"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
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        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
//