GALT4_MOUSE
ID GALT4_MOUSE Reviewed; 578 AA.
AC O08832; Q3U681;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 4;
DE EC=2.4.1.41 {ECO:0000269|PubMed:9153242};
DE AltName: Full=Polypeptide GalNAc transferase 4;
DE Short=GalNAc-T4;
DE Short=pp-GaNTase 4;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 4;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4;
GN Name=Galnt4;
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=9153242; DOI=10.1074/jbc.272.21.13843;
RA Hagen F.K., Ten Hagen K.G., Beres T.M., Balys M.M., VanWuyckhuyse B.C.,
RA Tabak L.A.;
RT "cDNA cloning and expression of a novel UDP-N-acetyl-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase.";
RL J. Biol. Chem. 272:13843-13848(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Colon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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).
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 a highest
CC activity toward EA2 peptide substrate and a much lower activity with
CC EPO-T, Muc2, Muc1a, Muc1b. {ECO:0000269|PubMed:9153242}.
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 Evidence={ECO:0000269|PubMed:9153242};
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 Evidence={ECO:0000269|PubMed:9153242};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8N4A0};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:9153242}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in sublingual gland, stomach,
CC colon, small intestine and cervix. Expressed at intermediate levels in
CC kidney, ovary, lung and uterus. Weakly expressed in spleen, liver,
CC heart and brain. Not expressed in submandibular and parotid glands,
CC skeletal muscle and testis. {ECO:0000269|PubMed:9153242}.
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 directs the glycopeptide
CC specificity. It is required in the glycopeptide specificity of enzyme
CC activity but not for activity with naked peptide substrates, suggesting
CC that it triggers the catalytic domain to act on GalNAc-glycopeptide
CC substrates. {ECO:0000250|UniProtKB:Q8N4A0}.
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 4;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_513";
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DR EMBL; U73819; AAB58301.1; -; mRNA.
DR EMBL; AK033494; BAC28317.1; -; mRNA.
DR EMBL; AK148036; BAE28303.1; -; mRNA.
DR EMBL; AK153253; BAE31844.1; -; mRNA.
DR EMBL; BC057882; AAH57882.1; -; mRNA.
DR CCDS; CCDS48679.1; -.
DR RefSeq; NP_056552.1; NM_015737.4.
DR AlphaFoldDB; O08832; -.
DR SMR; O08832; -.
DR STRING; 10090.ENSMUSP00000125315; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; O08832; 1 site.
DR iPTMnet; O08832; -.
DR PhosphoSitePlus; O08832; -.
DR EPD; O08832; -.
DR MaxQB; O08832; -.
DR PaxDb; O08832; -.
DR PeptideAtlas; O08832; -.
DR PRIDE; O08832; -.
DR ProteomicsDB; 268842; -.
DR DNASU; 14426; -.
DR Ensembl; ENSMUST00000161240; ENSMUSP00000125315; ENSMUSG00000090035.
DR GeneID; 14426; -.
DR KEGG; mmu:14426; -.
DR UCSC; uc007gxj.2; mouse.
DR CTD; 8693; -.
DR MGI; MGI:894692; Galnt4.
DR VEuPathDB; HostDB:ENSMUSG00000090035; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000163607; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; O08832; -.
DR OMA; WHSVPKH; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; O08832; -.
DR TreeFam; TF352660; -.
DR BRENDA; 2.4.1.41; 3474.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14426; 1 hit in 70 CRISPR screens.
DR PRO; PR:O08832; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O08832; protein.
DR Bgee; ENSMUSG00000090035; Expressed in right colon and 221 other tissues.
DR Genevisible; O08832; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISS:UniProtKB.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..578
FT /note="Polypeptide N-acetylgalactosaminyltransferase 4"
FT /id="PRO_0000059109"
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..578
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 444..577
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 134..243
FT /note="Catalytic subdomain A"
FT REGION 303..365
FT /note="Catalytic subdomain B"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 362
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT SITE 459
FT /note="Interaction with glycopeptide substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N4A0"
FT SITE 478
FT /note="Interaction with glycopeptide substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N4A0"
FT SITE 483
FT /note="Interaction with glycopeptide substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N4A0"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 348..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 457..477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 503..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 547..565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 578 AA; 66555 MW; 10ADC0D8B8B30835 CRC64;
MAVRWTWAGK SCLLLALLTL AYILVEFSVS TLYASPGAGG ARELGPRRLP DLDTREEDLS
QPLYIKPPAD SHALGEWGRA SKLQLNEGEL KQQEELIERY AINIYLSDRI SLHRHIEDKR
MYECKAKKFH YRSLPTTSVI IAFYNEAWST LLRTIHSVLE TSPAVLLKEI ILVDDLSDRI
YLKAQLETYI SNLERVRLIR TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNTGWLEPL
LERISRDETA IVCPVIDTID WNTFEFYMQT GEPMIGGFDW RLTFQWHSVP KHERDRRTSR
IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG KLEIHPCSHV
GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP ARKEAYGDLS ERKLLRERLK
CKSFDWYLKN VFSNLHVPED RPGWHGAIRS MGISSECLDY NAPDNNPTGA NLSLFGCHGQ
GGNQFFEYTS NKEIRFNSVT ELCAEVPQQK DYVGMQNCPK DGLPVPVNII WHFKEDGTIF
HPHTRLCLSA YRTAEGRPSV HMKTCDALDK NQLWRFEK
