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Polypeptide N-acetylgalactosaminyltransferase 2 (EC 2.4.1.41) (Polypeptide GalNAc transferase 2) (GalNAc-T2) (pp-GaNTase 2) (Protein-UDP acetylgalactosaminyltransferase 2) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 2 soluble form]

 GALT2_MOUSE             Reviewed;         570 AA.
Q6PB93; Q7TSI5; Q8BL27; Q922K5; Q99ME1;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
07-JUN-2017, entry version 127.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 2;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 2;
Short=GalNAc-T2;
Short=pp-GaNTase 2;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 2;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2;
Contains:
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 2 soluble form;
Name=Galnt2;
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).
TISSUE=Colon adenocarcinoma;
Miyahara N., Kanoh A., Irimura T.;
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Adipose tissue;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 broad spectrum of substrates for peptides
such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked
glycosylation of the immunoglobulin A1 (IgA1) hinge region (By
similarity). {ECO:0000250}.
-!- 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, Golgi stack membrane;
Single-pass type II membrane protein. Secreted. Note=Resides
preferentially in the trans and medial parts of the Golgi stack. A
secreted form also exists.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6PB93-1; Sequence=Displayed;
Name=2;
IsoId=Q6PB93-2; Sequence=VSP_011201;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed at high level.
{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}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Polypeptide N-acetylgalactosaminyltransferase 2;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_511";
-----------------------------------------------------------------------
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EMBL; AF348968; AAK37548.1; -; mRNA.
EMBL; AK046567; BAC32790.1; -; mRNA.
EMBL; BC007172; AAH07172.1; -; mRNA.
EMBL; BC053063; AAH53063.1; -; mRNA.
EMBL; BC059818; AAH59818.1; -; mRNA.
CCDS; CCDS22769.1; -. [Q6PB93-1]
RefSeq; NP_644678.2; NM_139272.2. [Q6PB93-1]
UniGene; Mm.33808; -.
ProteinModelPortal; Q6PB93; -.
SMR; Q6PB93; -.
STRING; 10090.ENSMUSP00000034458; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
PhosphoSitePlus; Q6PB93; -.
SwissPalm; Q6PB93; -.
PaxDb; Q6PB93; -.
PeptideAtlas; Q6PB93; -.
PRIDE; Q6PB93; -.
Ensembl; ENSMUST00000034458; ENSMUSP00000034458; ENSMUSG00000089704. [Q6PB93-1]
Ensembl; ENSMUST00000127664; ENSMUSP00000118564; ENSMUSG00000092329. [Q6PB93-2]
GeneID; 108148; -.
KEGG; mmu:108148; -.
UCSC; uc009nwz.2; mouse. [Q6PB93-1]
CTD; 2590; -.
MGI; MGI:894694; Galnt2.
eggNOG; KOG3738; Eukaryota.
eggNOG; ENOG410XPRX; LUCA.
GeneTree; ENSGT00760000118828; -.
HOVERGEN; HBG051699; -.
InParanoid; Q6PB93; -.
KO; K00710; -.
OMA; GNQEWAL; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q6PB93; -.
TreeFam; TF313267; -.
Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-MMU-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
PRO; PR:Q6PB93; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000089704; -.
Genevisible; Q6PB93; MM.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0005796; C:Golgi lumen; TAS:MGI.
GO; GO:0005795; C:Golgi stack; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; ISS:UniProtKB.
GO; GO:0002378; P:immunoglobulin biosynthetic process; ISO:MGI.
GO; GO:0016266; P:O-glycan processing; ISO:MGI.
GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
GO; GO:0018242; P:protein O-linked glycosylation via serine; ISO:MGI.
GO; GO:0018243; P:protein O-linked glycosylation via threonine; ISO: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.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Secreted;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 570 Polypeptide N-
acetylgalactosaminyltransferase 2.
/FTId=PRO_0000223392.
CHAIN 51 570 Polypeptide N-
acetylgalactosaminyltransferase 2 soluble
form.
/FTId=PRO_0000012267.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 24 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 25 570 Lumenal. {ECO:0000255}.
DOMAIN 442 565 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 134 239 Catalytic subdomain A.
REGION 299 361 Catalytic subdomain B.
METAL 223 223 Manganese. {ECO:0000250}.
METAL 225 225 Manganese. {ECO:0000250}.
METAL 358 358 Manganese. {ECO:0000250}.
BINDING 142 142 Substrate. {ECO:0000250}.
BINDING 175 175 Substrate. {ECO:0000250}.
BINDING 200 200 Substrate. {ECO:0000250}.
BINDING 224 224 Substrate. {ECO:0000250}.
BINDING 330 330 Substrate. {ECO:0000250}.
BINDING 361 361 Substrate. {ECO:0000250}.
BINDING 364 364 Substrate. {ECO:0000250}.
BINDING 366 366 Substrate. {ECO:0000250}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000250|UniProtKB:Q10471}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 125 353 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 344 422 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 455 472 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 495 512 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 538 554 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 1 41 MRRRSRMLLCFALLWVLGIAYYMYSGGGSALAAGGGGAGRK
-> MALHNPQ (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011201.
CONFLICT 2 2 R -> L (in Ref. 1; AAK37548).
{ECO:0000305}.
CONFLICT 226 226 C -> Y (in Ref. 2; BAC32790).
{ECO:0000305}.
CONFLICT 516 518 DSR -> NSK (in Ref. 1; AAK37548).
{ECO:0000305}.
CONFLICT 564 564 F -> V (in Ref. 1; AAK37548).
{ECO:0000305}.
SEQUENCE 570 AA; 64514 MW; 90D5DC02C85A8EEA CRC64;
MRRRSRMLLC FALLWVLGIA YYMYSGGGSA LAAGGGGAGR KGDWNDIDSI KKKDLHHSRG
DEKAQGVETL PPGKVRWPDF NQEAYVGGTM VRSGQDPYAR NKFNQVESDK LHMDRGIPDT
RHDQCQRKQW RVDLPATSVV ITFHNEARSA LLRTVVSVLK RSPPHLIKEI ILVDDYSNDP
EDGALLGKIE KVRVLRNDRR EGLMRSRVRG ADAAQAKVLT FLDSHCECNE RWLEPLLERV
AEDRTRVVSP IIDVINMDNF QYVGASADLK GGFDWNLVFK WDYMTPEQRR SRQGNPVAPI
KTPMIAGGLF VMDKLYFEEL GKYDMMMDVW GGENLEISFR VWQCGGSLEI IPCSRVGHVF
RKQHPYTFPG GSGTVFARNT RRAAEVWMDE YKHFYYAAVP SARNVPYGNI QSRLELRKKL
GCKPFKWYLD NVYPELRVPD HQDIAFGALQ QGTNCLDTLG HFADGVVGIY ECHNAGGNQE
WALTKEKSVK HMDLCLTVVD RSPGSLIRLQ GCRENDSRQK WEQIEGNSKL RHVGSNLCLD
SRTAKSGGLS VEVCGPALSQ QWKFSLNLQQ


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