ID   GLT12_MOUSE             Reviewed;         576 AA.
AC   Q8BGT9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 12;
DE            EC=2.4.1.41;
DE   AltName: Full=Polypeptide GalNAc transferase 12;
DE            Short=GalNAc-T12;
DE            Short=pp-GaNTase 12;
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 12;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12;
GN   Name=Galnt12;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, and Thymus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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: 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 non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no
CC       detectable activity with Muc2 and Muc7. Displays enzymatic activity
CC       toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to
CC       mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. May play an
CC       important role in the initial step of mucin-type oligosaccharide
CC       biosynthesis in digestive organs (By similarity). {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   -!- 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
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 12;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_520";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK033638; BAC28401.1; -; mRNA.
DR   EMBL; AK042133; BAC31179.1; -; mRNA.
DR   EMBL; BC056425; AAH56425.1; -; mRNA.
DR   CCDS; CCDS18158.1; -.
DR   RefSeq; NP_766281.1; NM_172693.3.
DR   AlphaFoldDB; Q8BGT9; -.
DR   SMR; Q8BGT9; -.
DR   STRING; 10090.ENSMUSP00000045721; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   iPTMnet; Q8BGT9; -.
DR   PhosphoSitePlus; Q8BGT9; -.
DR   SwissPalm; Q8BGT9; -.
DR   EPD; Q8BGT9; -.
DR   jPOST; Q8BGT9; -.
DR   MaxQB; Q8BGT9; -.
DR   PaxDb; 10090-ENSMUSP00000045721; -.
DR   ProteomicsDB; 263372; -.
DR   Antibodypedia; 29005; 106 antibodies from 15 providers.
DR   DNASU; 230145; -.
DR   Ensembl; ENSMUST00000045041.12; ENSMUSP00000045721.6; ENSMUSG00000039774.13.
DR   GeneID; 230145; -.
DR   KEGG; mmu:230145; -.
DR   UCSC; uc008suk.1; mouse.
DR   AGR; MGI:2444664; -.
DR   CTD; 79695; -.
DR   MGI; MGI:2444664; Galnt12.
DR   VEuPathDB; HostDB:ENSMUSG00000039774; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000157173; -.
DR   HOGENOM; CLU_013477_0_3_1; -.
DR   InParanoid; Q8BGT9; -.
DR   OMA; FSIDRAF; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; Q8BGT9; -.
DR   TreeFam; TF352660; -.
DR   Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 230145; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Galnt12; mouse.
DR   PRO; PR:Q8BGT9; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8BGT9; Protein.
DR   Bgee; ENSMUSG00000039774; Expressed in molar tooth and 163 other cell types or tissues.
DR   ExpressionAtlas; Q8BGT9; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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:SF18; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 12; 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; Q8BGT9; MM.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycosyltransferase; Golgi apparatus; Lectin; Manganese;
KW   Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..576
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 12"
FT                   /id="PRO_0000059129"
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..576
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          440..572
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          38..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..239
FT                   /note="Catalytic subdomain A"
FT   REGION          299..361
FT                   /note="Catalytic subdomain B"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        120..353
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        344..417
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        453..474
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        501..516
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        542..561
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ   SEQUENCE   576 AA;  66541 MW;  706310A99FCDACD5 CRC64;
     MWGRAVRRRC PRGLRRGREA LLALLALAGL GALLRARSRS GTVDPGPPRT PLPGRHEPVL
     PRPPLPADAL GAHGEAVRLQ LQGEELRLQE ESVKQHQINI YLSDRISLHR RLPERWNPLC
     REVKYDYDNL PKTSVVIAFY NEAWSTLLRT VYSVLETSPD ILLEEVILVD DYSDREHLKE
     RLANELSQLP KVRLIRASRR EGLVRARLLG ASAARGEVLT FLDCHCECHE GWLEPLLQRI
     HEKESAVVCP VIDVIDWNTF EYLGNSGEPQ IGGFDWRLVF TWHVVPQRER QSMRSPIDVI
     RSPTMAGGLF AVSKRYFDYL GSYDTGMEVW GGENLEFSFR IWQCGGTLET HPCSHVGHVF
     PKQAPYSRSK ALANSVRAAE VWMDEFKELY YHRNPQARLE PFGDVTERKK LRAKLQCKDF
     KWFLDTVYPE LHVPEDRPGF FGMLQNRGLR GYCLDYNPPN ENHVEGHQVL LYLCHGMGQN
     QFFEYTTRKE IRYNTRQPEA CITVEDGKDT LVMDLCRETV PENQEFILQE DGTLVHKHSR
     KCVEATEKVL DNGFAPYLRD CTNSDNQRWF FKERMS
//