GLT15_MOUSE
ID GLT15_MOUSE Reviewed; 638 AA.
AC Q9D2N8; A3KN88;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 15;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase-like protein 2;
DE Short=GalNAc-T-like protein 2;
DE Short=pp-GaNTase-like protein 2;
DE AltName: Full=Polypeptide N-acetylgalactosaminyltransferase-like protein 2;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase-like protein 2;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2;
GN Name=Galnt15; Synonyms=Galntl2;
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=Skin;
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].
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12651884; DOI=10.1093/glycob/cwg062;
RA Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A.;
RT "Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
RT isoforms in murine tissues determined by real-time PCR: a new view of a
RT large family.";
RL Glycobiology 13:549-557(2003).
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. Although it
CC displays a much weaker activity toward all substrates tested compared
CC to GALNT2, it is able to transfer up to seven GalNAc residues to the
CC Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in
CC cooperation with other GALNT proteins. Prefers Muc1a as substrate (By
CC 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 -!- TISSUE SPECIFICITY: Specifically expressed in testis.
CC {ECO:0000269|PubMed:12651884}.
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-like protein 2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_527";
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DR EMBL; AK019470; BAB31741.1; -; mRNA.
DR EMBL; BC133711; AAI33712.1; -; mRNA.
DR CCDS; CCDS36859.1; -.
DR RefSeq; NP_084442.1; NM_030166.3.
DR AlphaFoldDB; Q9D2N8; -.
DR SMR; Q9D2N8; -.
DR STRING; 10090.ENSMUSP00000022460; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q9D2N8; 1 site.
DR iPTMnet; Q9D2N8; -.
DR PhosphoSitePlus; Q9D2N8; -.
DR PaxDb; Q9D2N8; -.
DR PRIDE; Q9D2N8; -.
DR ProteomicsDB; 271231; -.
DR Antibodypedia; 2430; 71 antibodies from 18 providers.
DR DNASU; 78754; -.
DR Ensembl; ENSMUST00000022460; ENSMUSP00000022460; ENSMUSG00000021903.
DR GeneID; 78754; -.
DR KEGG; mmu:78754; -.
DR UCSC; uc007syb.1; mouse.
DR CTD; 117248; -.
DR MGI; MGI:1926004; Galnt15.
DR VEuPathDB; HostDB:ENSMUSG00000021903; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000160808; -.
DR HOGENOM; CLU_013477_0_3_1; -.
DR InParanoid; Q9D2N8; -.
DR OMA; APERDWG; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q9D2N8; -.
DR TreeFam; TF313267; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 78754; 6 hits in 75 CRISPR screens.
DR PRO; PR:Q9D2N8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9D2N8; protein.
DR Bgee; ENSMUSG00000021903; Expressed in hindlimb stylopod muscle and 96 other tissues.
DR ExpressionAtlas; Q9D2N8; baseline and differential.
DR Genevisible; Q9D2N8; 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:0030133; C:transport vesicle; ISO:MGI.
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; 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 2: Evidence at transcript 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..638
FT /note="Polypeptide N-acetylgalactosaminyltransferase 15"
FT /id="PRO_0000059138"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..638
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 503..630
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 134..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..299
FT /note="Catalytic subdomain A"
FT REGION 357..419
FT /note="Catalytic subdomain B"
FT COMPBIAS 134..150
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 181..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 402..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 516..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 561..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 602..619
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 638 AA; 72321 MW; 421617F0C8556976 CRC64;
MLPRKRPRSG RSRLQFLLLF LTLGCVLMMV ILLHPPPPTL HQAVTAQASK HSPDTGYRLD
FGDSQEWVLE AETEGDEYSL LDGLPSFISL QEDQLLVAVA SPRARRSQSQ GRRQGSYQFI
KHRSRRWDEE ALEKDWRTEE DGEESEEVLT PLGPDSDGLN KPLSARLPLR RVLPEVRHPL
CLQQHPTSGL PTASVILCFH DEAWPTLLRT VHSILDTAPR ALLQEIILVD DLSQQELLKS
ALSEYVARLE AVKLLRSNRR LGTIGARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI
ADDRSRVVSP VIDVIDWKTL QYSASKLHRG TLDWKLDFRW KPLGEQEQKA LPSPISPVRS
PVVPREVVAV DRHYFQNTGA YDPLLSLGDS ENLEMSFKAW LCGGSVEILP CSRVGHIYRS
QDASSRPDPE VALKNKIIIA ETWLSSFKET FYRHIPEAFT LSKVAKPDCT ERLKLQRRLG
CRTFHWFLAN VYPELYPSDH RPRFSGKLHN TGFGLCADCQ ADGDILGCPM TLAPCSNNRQ
QQNLEHTGRK EILFGGPQRL CFDVRGGRVI LQNCTEEGPA IHQQHWDFQE DGMIIHVLSG
KCMEAGVQPS NKDLYLRQCD GKTSQLWRFD QIHPVDER
