GALT5_MOUSE
ID GALT5_MOUSE Reviewed; 930 AA.
AC Q8C102; A2AS75;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 5;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 5;
DE Short=GalNAc-T5;
DE Short=pp-GaNTase 5;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 5;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5;
GN Name=Galnt5;
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=Head;
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 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 [3]
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=11159923; DOI=10.1093/glycob/10.12.1317;
RA Kingsley P.D., Hagen K.G., Maltby K.M., Zara J., Tabak L.A.;
RT "Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-
RT acetylgalactosaminyl-transferase family member mRNAs during mouse
RT development.";
RL Glycobiology 10:1317-1323(2000).
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 EA2 peptide substrate, but has a weak activity toward Muc2 or
CC Muc1b substrates (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 -!- SUBUNIT: Interacts with EXT2. Does not interact with EXT1, EXTL1 or
CC EXTL3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at low level. Not expressed before E7.5
CC during embryogenesis. Expressed in dental mesenchyme and tongue.
CC Accumulates in a subset of mesenchymal cells at the ventral-most
CC portions of the 12.5 dpc maxilla and mandible underlying the dental
CC lamina. {ECO:0000269|PubMed:11159923}.
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 5;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_514";
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DR EMBL; AK029323; BAC26396.1; -; mRNA.
DR EMBL; AL928564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL26932.1; -; Genomic_DNA.
DR CCDS; CCDS38125.1; -.
DR RefSeq; NP_766443.2; NM_172855.3.
DR RefSeq; XP_006498111.1; XM_006498048.3.
DR RefSeq; XP_006498112.1; XM_006498049.2.
DR AlphaFoldDB; Q8C102; -.
DR SMR; Q8C102; -.
DR BioGRID; 232310; 1.
DR STRING; 10090.ENSMUSP00000108235; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8C102; 12 sites.
DR iPTMnet; Q8C102; -.
DR PhosphoSitePlus; Q8C102; -.
DR MaxQB; Q8C102; -.
DR PaxDb; Q8C102; -.
DR PRIDE; Q8C102; -.
DR ProteomicsDB; 268843; -.
DR Antibodypedia; 2453; 110 antibodies from 21 providers.
DR DNASU; 241391; -.
DR Ensembl; ENSMUST00000112616; ENSMUSP00000108235; ENSMUSG00000026828.
DR Ensembl; ENSMUST00000166729; ENSMUSP00000131362; ENSMUSG00000026828.
DR GeneID; 241391; -.
DR KEGG; mmu:241391; -.
DR UCSC; uc012bvo.1; mouse.
DR CTD; 11227; -.
DR MGI; MGI:2179403; Galnt5.
DR VEuPathDB; HostDB:ENSMUSG00000026828; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000159241; -.
DR HOGENOM; CLU_013477_1_0_1; -.
DR InParanoid; Q8C102; -.
DR OMA; VQPDQMK; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8C102; -.
DR TreeFam; TF313267; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 241391; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q8C102; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C102; protein.
DR Bgee; ENSMUSG00000026828; Expressed in lumbar dorsal root ganglion and 83 other tissues.
DR Genevisible; Q8C102; 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; ISO:MGI.
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; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..930
FT /note="Polypeptide N-acetylgalactosaminyltransferase 5"
FT /id="PRO_0000059111"
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..930
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 794..925
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 190..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..594
FT /note="Catalytic subdomain A"
FT REGION 654..716
FT /note="Catalytic subdomain B"
FT COMPBIAS 191..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 578
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 580
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 713
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 716
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7M9"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 902
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 476..708
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 699..779
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 812..825
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 848..863
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 898..913
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 705
FT /note="I -> L (in Ref. 1; BAC26396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 930 AA; 105780 MW; C5851F6E13CDF5D7 CRC64;
MNKIRKFFRG SGRVLAFIFA ASVIWLLFDM AALRLSFSEI NAGLLKEDII RREHTGFRVE
PDQVKVLYTS IRGMGLPRNG AWGKENFRKA ENHELKVEEN MDQVQRKGKM QNLLGRRKAV
PLWHLAHLQT LPVTIPMQKT QGRDSKPEVS SQYMMSKWMT VLESEKTPFT ASRGVPLTKI
AGRTETFDKK QEAPQNYNVS SDTSKQASER TLNMTISVKT DRSKQKSQTV TKLRMHFASP
PILKSEEVTV IKKAEAQSKD LKHEALKALP LLKFIADMGH LKNQSTNETQ LGRLPEDDAA
KVAPGKKLNF SESHVVIITK EEELKTDTKE VPNSKTQTVF PKLLGGSPHK QIPRNQSKTS
SSPPALKKAV SQSKPTISGG LHTARSNLTA KAPTVGYQQS HANIPENPGM HHVFRIDVTL
SPRDLNAPGQ FGRPVVVPPE KKKEAEQRWK EGNFNVYLSD LIPVDRAIED TRPAGCAEQL
VHNDLPTTSI IMCFVDEVWS ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK EYLKADLDKY
MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK
KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWKTIP PDVVAKNGIK ETDIIRCPVM
AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG GEIEIIPCSR VGHIFRNDNP
YSFPKDRMKT VERNLVRVAE VWLDDYRELF YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK
SFKWYLDNVF PDLKAPVVRA SGVLINMALG KCVSIENITV TLEDCDGSSQ LQQFNYTWVR
LIKHGEWCVA PIPEKGSLTL YHCDNRNNRL KWLHKSASAF HPELVDHIVF ENYQQLLCME
GNFSQKTLKL AACNPMELQQ KWKFEKYYEV
