GLT16_MOUSE
ID GLT16_MOUSE Reviewed; 558 AA.
AC Q9JJ61; Q60GT0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 16;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 16;
DE Short=GalNAc-T16;
DE AltName: Full=Polypeptide GalNAc transferase-like protein 1;
DE Short=GalNAc-T-like protein 1;
DE Short=pp-GaNTase-like protein 1;
DE AltName: Full=Polypeptide N-acetylgalactosaminyltransferase-like protein 1;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase-like protein 1;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1;
GN Name=Galnt16; Synonyms=Galntl1;
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].
RC TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang Y., Kwon Y., Kikuchi N., Narimatsu H.;
RT "Mouse UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-
RT acetylgalactosaminyltransferase, mpp-GalNAc-T16.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [4]
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=15018805; DOI=10.1016/s1567-133x(01)00019-9;
RA Nelson P.A., Sutcliffe J.G., Thomas E.A.;
RT "A new UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase mRNA
RT exhibits predominant expression in the hypothalamus, thalamus and amygdala
RT of mouse forebrain.";
RL Gene Expr. Patterns 1:95-99(2002).
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. {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: In the CNS, it is predominantly expressed in
CC several distinct hypothalamic, thalamic and amygdaloid nuclei. The most
CC abundant level of expression is in the paraventricular, ventromedial
CC and arcuate nuclei of the hypothalamus, the anterodorsal and
CC parafascicular nuclei of the thalamus and the central, basomedial and
CC medial nuclei of the amygdala. Also expressed in cerebral cortex,
CC lateral septum, habenula and hippocampus.
CC {ECO:0000269|PubMed:15018805}.
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 -!- CAUTION: Was originally termed Galnt10/pp-GaNTase 10.
CC {ECO:0000305|PubMed:15018805}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Putative
CC polypeptide N-acetylgalactosaminyltransferase-like protein 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_524";
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; AB045325; BAA97985.1; -; mRNA.
DR EMBL; AB175683; BAD52071.1; -; mRNA.
DR EMBL; AK138883; BAE23810.1; -; mRNA.
DR EMBL; BC110634; AAI10635.1; -; mRNA.
DR EMBL; BC125015; AAI25016.1; -; mRNA.
DR CCDS; CCDS36482.1; -.
DR RefSeq; NP_001074890.1; NM_001081421.1.
DR AlphaFoldDB; Q9JJ61; -.
DR SMR; Q9JJ61; -.
DR BioGRID; 224406; 1.
DR STRING; 10090.ENSMUSP00000021558; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR iPTMnet; Q9JJ61; -.
DR PhosphoSitePlus; Q9JJ61; -.
DR MaxQB; Q9JJ61; -.
DR PaxDb; Q9JJ61; -.
DR PRIDE; Q9JJ61; -.
DR ProteomicsDB; 263375; -.
DR Antibodypedia; 25033; 69 antibodies from 17 providers.
DR Ensembl; ENSMUST00000021558; ENSMUSP00000021558; ENSMUSG00000021130.
DR Ensembl; ENSMUST00000218943; ENSMUSP00000151619; ENSMUSG00000021130.
DR Ensembl; ENSMUST00000219993; ENSMUSP00000151829; ENSMUSG00000021130.
DR GeneID; 108760; -.
DR KEGG; mmu:108760; -.
DR UCSC; uc007oaw.1; mouse.
DR CTD; 57452; -.
DR MGI; MGI:1917754; Galnt16.
DR VEuPathDB; HostDB:ENSMUSG00000021130; -.
DR eggNOG; KOG3738; Eukaryota.
DR GeneTree; ENSGT00940000158846; -.
DR HOGENOM; CLU_013477_0_2_1; -.
DR InParanoid; Q9JJ61; -.
DR OMA; VCNPREG; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q9JJ61; -.
DR TreeFam; TF313267; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 108760; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Galnt16; mouse.
DR PRO; PR:Q9JJ61; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9JJ61; protein.
DR Bgee; ENSMUSG00000021130; Expressed in ventromedial nucleus of hypothalamus and 166 other tissues.
DR ExpressionAtlas; Q9JJ61; baseline and differential.
DR Genevisible; Q9JJ61; 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 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 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; Glycosyltransferase; Golgi apparatus; Lectin; Manganese;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..558
FT /note="Polypeptide N-acetylgalactosaminyltransferase 16"
FT /id="PRO_0000059136"
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..558
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 428..555
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..227
FT /note="Catalytic subdomain A"
FT REGION 286..348
FT /note="Catalytic subdomain B"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 113..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 331..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 441..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 486..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 530..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 71
FT /note="K -> E (in Ref. 1; BAA97985)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="G -> R (in Ref. 1; BAA97985)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="P -> L (in Ref. 1; BAA97985)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="K -> R (in Ref. 1; BAA97985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 62875 MW; 1B59DBE8EDDD5C63 CRC64;
MRKIRANAIA ILTVAWILGT FYYLWQDNRA HAASSSGRGA QRAGGRPEQL REDRTIPLIV
TGTPSKGFDE KAYLSAKQLK PGEDPYRQHA FNQLESDKLS SDRPIRDTRH YSCPSLSYSS
DLPATSVIIT FHNEARSTLL RTVKSVLNRT PASLIQEIIL VDDFSSDPED CLLLTRIPKV
KCLRNDKREG LIRSRVRGAD VAGATVLTFL DSHCEVNVEW LQPMLQRVME DHTRVVSPII
DVISLDNFAY LAASADLRGG FDWSLHFKWE QIPLEQKMTR TDPTKPIRTP VIAGGIFVID
KSWFNHLGKY DAQMDIWGGE NFELSFRVWM CGGSLEIVPC SRVGHVFRKR HPYNFPEGNA
LTYIRNTKRT AEVWMDEYKQ YYYEARPSAI GKAFGSVATR IEQRKKMDCK SFRWYLENVY
PELTVPVKEV LPGVIKQGVN CLESQGQNTA GDLLLGMGIC RGSAKSPPPA QAWLFSDHLI
QQQGKCLAAT STLMSSPGSP VILQTCNPKE GKQKWRRKGS FIQHSVSGLC LETKPAQLVT
SKCQTDAQAQ QWQLLPHT
