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Polypeptide N-acetylgalactosaminyltransferase 13 (EC 2.4.1.41) (Polypeptide GalNAc transferase 13) (GalNAc-T13) (pp-GaNTase 13) (Protein-UDP acetylgalactosaminyltransferase 13) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13)

 GLT13_MOUSE             Reviewed;         556 AA.
Q8CF93; Q8BLE4; Q8BYT3;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
07-JUN-2017, entry version 126.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 13;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 13;
Short=GalNAc-T13;
Short=pp-GaNTase 13;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 13;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13;
Name=Galnt13;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=12407114; DOI=10.1074/jbc.M203094200;
Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T.,
Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M.,
Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D.,
Narimatsu H.;
"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-
galactosamine:polypeptide N-acetylgalactosaminyltransferase,
designated pp-GalNAc-T13, that is specifically expressed in neurons
and synthesizes GalNAc alpha-serine/threonine antigen.";
J. Biol. Chem. 278:573-584(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Hypothalamus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8618846; DOI=10.1073/pnas.92.26.12070;
Hennet T., Hagen F.K., Tabak L.A., Marth J.D.;
"T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-
transferase gene by site-directed recombination.";
Proc. Natl. Acad. Sci. U.S.A. 92:12070-12074(1995).
[4]
TISSUE SPECIFICITY.
PubMed=12651884; DOI=10.1093/glycob/cwg062;
Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A.;
"Expression of UDP-GalNAc:polypeptide N-
acetylgalactosaminyltransferase isoforms in murine tissues determined
by real-time PCR: a new view of a large family.";
Glycobiology 13:549-557(2003).
-!- FUNCTION: Catalyzes the initial reaction in O-linked
oligosaccharide biosynthesis, the transfer of an N-acetyl-D-
galactosamine residue to a serine or threonine residue on the
protein receptor. Has a much stronger activity than GALNT1 to
transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able
to glycosylate SDC3. Probably responsible for the synthesis of Tn
antigen in neuronal cells. {ECO:0000269|PubMed:12407114,
ECO:0000269|PubMed:8618846}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8CF93-1; Sequence=Displayed;
Name=2;
IsoId=Q8CF93-2; Sequence=VSP_011220;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Specifically expressed in neuronal cells. Not
expressed in glial cells such as astrocytes. Expressed at low
level. {ECO:0000269|PubMed:12407114, ECO:0000269|PubMed:12651884}.
-!- DOMAIN: There are two conserved domains in the glycosyltransferase
region: the N-terminal domain (domain A, also called GT1 motif),
which is probably involved in manganese coordination and substrate
binding and the C-terminal domain (domain B, also called
Gal/GalNAc-T motif), which is probably involved in catalytic
reaction and UDP-Gal binding. {ECO:0000250}.
-!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
contributes to the glycopeptide specificity. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. It however abolishes
Tn antigen in neuronal cells. {ECO:0000269|PubMed:8618846}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- CAUTION: Was initially wrongly assigned as Galnt8. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Polypeptide N-acetylgalactosaminyltransferase 13;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_521";
-----------------------------------------------------------------------
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EMBL; AB082928; BAC54546.1; -; mRNA.
EMBL; AK038387; BAC29981.1; -; mRNA.
EMBL; AK045417; BAC32353.1; -; mRNA.
CCDS; CCDS16041.1; -. [Q8CF93-1]
RefSeq; NP_766618.2; NM_173030.2. [Q8CF93-1]
RefSeq; XP_006498154.1; XM_006498091.2. [Q8CF93-1]
RefSeq; XP_006498155.1; XM_006498092.2. [Q8CF93-1]
UniGene; Mm.330227; -.
ProteinModelPortal; Q8CF93; -.
SMR; Q8CF93; -.
STRING; 10090.ENSMUSP00000063464; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q8CF93; -.
PhosphoSitePlus; Q8CF93; -.
PaxDb; Q8CF93; -.
PRIDE; Q8CF93; -.
Ensembl; ENSMUST00000068595; ENSMUSP00000063464; ENSMUSG00000060988. [Q8CF93-1]
Ensembl; ENSMUST00000112634; ENSMUSP00000108253; ENSMUSG00000060988. [Q8CF93-2]
Ensembl; ENSMUST00000112635; ENSMUSP00000108254; ENSMUSG00000060988. [Q8CF93-1]
Ensembl; ENSMUST00000112636; ENSMUSP00000108255; ENSMUSG00000060988. [Q8CF93-1]
GeneID; 271786; -.
KEGG; mmu:271786; -.
UCSC; uc008jrq.1; mouse. [Q8CF93-1]
UCSC; uc012bvm.1; mouse. [Q8CF93-2]
CTD; 114805; -.
MGI; MGI:2139447; Galnt13.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
HOVERGEN; HBG051699; -.
InParanoid; Q8CF93; -.
KO; K00710; -.
OMA; ETFEYMA; -.
OrthoDB; EOG091G085O; -.
TreeFam; TF313267; -.
Reactome; R-MMU-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
ChiTaRS; Galnt13; mouse.
PRO; PR:Q8CF93; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000060988; -.
ExpressionAtlas; Q8CF93; baseline and differential.
Genevisible; Q8CF93; MM.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:MGI.
GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
Metal-binding; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 556 Polypeptide N-
acetylgalactosaminyltransferase 13.
/FTId=PRO_0000059131.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 556 Lumenal. {ECO:0000255}.
DOMAIN 428 550 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 114 224 Catalytic subdomain A.
REGION 284 346 Catalytic subdomain B.
METAL 208 208 Manganese. {ECO:0000250}.
METAL 210 210 Manganese. {ECO:0000250}.
METAL 343 343 Manganese. {ECO:0000250}.
BINDING 155 155 Substrate. {ECO:0000250}.
BINDING 185 185 Substrate. {ECO:0000250}.
BINDING 315 315 Substrate. {ECO:0000250}.
BINDING 346 346 Substrate. {ECO:0000250}.
BINDING 351 351 Substrate. {ECO:0000250}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 105 338 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 329 407 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 441 458 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 481 496 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 522 539 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 466 466 V -> VHDLCLSAPSLGVGAEECCSNHPLYGLVYTPTINEQ
V (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_011220.
CONFLICT 457 457 N -> K (in Ref. 2; BAC32353).
{ECO:0000305}.
SEQUENCE 556 AA; 63983 MW; 593934CFD0AED148 CRC64;
MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI SRNQEGPGEM
GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV RLEGCKTKVY PDELPNTSVV
IVFHNEAWST LLRTVYSVIN RSPHYLLSEV ILVDDASERD FLKLTLENYV KTLEVPVKII
RMEERSGLIR ARLRGAAASK GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI
SDDTFEYMAG SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN
YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP YTFPGGTGHV
INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT LRENLKCKPF SWYLENIYPD
SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL
CLDVSRLSGP VIMLKCHHMR GNQLWEYDAE RLTLRHANSN QCLDEPSEED KMVPTMQDCS
GSRSQQWLLR NMTLGT


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