GLT14_MOUSE
ID GLT14_MOUSE Reviewed; 550 AA.
AC Q8BVG5; Q60GT2; Q8BTI6; Q9DCJ2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 14;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 14;
DE Short=GalNAc-T14;
DE Short=pp-GaNTase 14;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 14;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14;
GN Name=Galnt14;
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).
RA Zhang Y., Kwon Y., Kikuchi N., Narimatsu H.;
RT "Mouse UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-
RT acetylgalactosaminyltransferase, mpp-GalNAc-T14.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Olfactory bulb;
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).
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. Displays activity
CC toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and
CC Muc13 (-58). May be involved in O-glycosylation in kidney (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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BVG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BVG5-2; Sequence=VSP_011225, VSP_011226;
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 14;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_522";
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DR EMBL; AB175681; BAD52069.1; -; mRNA.
DR EMBL; AK002747; BAB22325.1; -; mRNA.
DR EMBL; AK078292; BAC37208.1; -; mRNA.
DR CCDS; CCDS28965.1; -. [Q8BVG5-1]
DR RefSeq; NP_082140.2; NM_027864.2.
DR RefSeq; XP_006525002.1; XM_006524939.3.
DR AlphaFoldDB; Q8BVG5; -.
DR SMR; Q8BVG5; -.
DR STRING; 10090.ENSMUSP00000024858; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR PhosphoSitePlus; Q8BVG5; -.
DR MaxQB; Q8BVG5; -.
DR PaxDb; Q8BVG5; -.
DR PRIDE; Q8BVG5; -.
DR ProteomicsDB; 263373; -. [Q8BVG5-1]
DR ProteomicsDB; 263374; -. [Q8BVG5-2]
DR Antibodypedia; 2530; 227 antibodies from 24 providers.
DR DNASU; 71685; -.
DR Ensembl; ENSMUST00000112591; ENSMUSP00000108210; ENSMUSG00000024064. [Q8BVG5-2]
DR GeneID; 71685; -.
DR KEGG; mmu:71685; -.
DR CTD; 79623; -.
DR MGI; MGI:1918935; Galnt14.
DR VEuPathDB; HostDB:ENSMUSG00000024064; -.
DR eggNOG; KOG3738; Eukaryota.
DR GeneTree; ENSGT00940000158182; -.
DR HOGENOM; CLU_013477_0_0_1; -.
DR InParanoid; Q8BVG5; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8BVG5; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 71685; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Galnt14; mouse.
DR PRO; PR:Q8BVG5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BVG5; protein.
DR Bgee; ENSMUSG00000024064; Expressed in right kidney and 50 other tissues.
DR ExpressionAtlas; Q8BVG5; baseline and differential.
DR Genevisible; Q8BVG5; 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: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 Alternative splicing; Disulfide bond; Glycosyltransferase; Golgi apparatus;
KW Lectin; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..550
FT /note="Polypeptide N-acetylgalactosaminyltransferase 14"
FT /id="PRO_0000059134"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..550
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 415..548
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 110..215
FT /note="Catalytic subdomain A"
FT REGION 274..336
FT /note="Catalytic subdomain B"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 101..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 319..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 430..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 474..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 515..536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 385..429
FT /note="IENRLNLRKNLHCQTFKWNLENVYPELRVPPDSSIQKGNIRQRQK -> SHV
FT TQCCRRRILIRGTSFRGVVPPTNLPVESPTDPSSPYYLSSSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011225"
FT VAR_SEQ 430..550
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011226"
FT CONFLICT 112
FT /note="P -> H (in Ref. 2; BAC37208)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="N -> H (in Ref. 1; BAD52069)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="L -> I (in Ref. 2; BAB22325)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="P -> H (in Ref. 2; BAC37208)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="N -> Y (in Ref. 1; BAD52069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 63989 MW; D67054CFE6F332E1 CRC64;
MRRLTRRLAL PIFGVLWITV LLFFWVTKRK LEVPLGPEVQ TPKPSDADWD DLWEQFDERR
YLNAKKWRVG DDPYKLYAFN QRESERISSN RAVPDTRHKR CSLLVYCTDL PPTSIIITFH
NEARSTLLRT IRSVLNRTPM HLIQEIILVD DFSNDPEDCK QLIKLPKVKC LRNNERQGLV
RSRMRGADIA QGTTLTFLDS HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFNYIE
SASELRGGFD WSLHFQWEQL SLEQKALRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDV
DMDIWGGENF EISFRVWMCG GGLEIIPCSR VGHVFRKKHP YVFPDGNANT YIKNTKRTAE
VWMDEYKQYY YAARPFALER PFGNIENRLN LRKNLHCQTF KWNLENVYPE LRVPPDSSIQ
KGNIRQRQKC LESQKQKKQE ILRLSPCAKV KGDGAKSQVW AFTYTQQIIQ EELCLSVVTL
FPGAPVVLAL CKNGDERQLW TKTGARIEHI ASHLCLDTDM FGDSTEDGKE VVVNPCESSL
MSQHWDIVSS
