GLT13_HUMAN
ID GLT13_HUMAN Reviewed; 556 AA.
AC Q8IUC8; Q08ER7; Q68VI8; Q6ZWG1; Q96PX0; Q9UIE5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 13;
DE EC=2.4.1.41 {ECO:0000269|PubMed:12407114, ECO:0000269|PubMed:22186971};
DE AltName: Full=Polypeptide GalNAc transferase 13;
DE Short=GalNAc-T13 {ECO:0000303|PubMed:22186971};
DE Short=pp-GaNTase 13;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 13;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13 {ECO:0000303|PubMed:12407114};
GN Name=GALNT13; Synonyms=KIAA1918;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORM 1), CATALYTIC
RP ACTIVITY (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES (ISOFORM 1), PATHWAY,
RP AND TISSUE SPECIFICITY.
RX PubMed=12407114; DOI=10.1074/jbc.m203094200;
RA Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T.,
RA Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H.,
RA Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.;
RT "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-
RT GalNAc-T13, that is specifically expressed in neurons and synthesizes
RT GalNAc alpha-serine/threonine antigen.";
RL J. Biol. Chem. 278:573-584(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=24722188; DOI=10.1038/ncomms4650;
RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M.,
RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I.,
RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A.,
RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D.,
RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.;
RT "Protein interaction network of alternatively spliced isoforms from brain
RT links genetic risk factors for autism.";
RL Nat. Commun. 5:3650-3650(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bennett E.P.;
RT "polypetide GalNAc-transferase 13, ppGalNAc-T13, GALNT13.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-556 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-556 (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP FUNCTION (ISOFORMS 1 AND 3), CATALYTIC ACTIVITY (ISOFORMS 1 AND 3),
RP BIOPHYSICOCHEMICAL PROPERTIES (ISOFORMS 1 AND 3), AND PATHWAY.
RX PubMed=22186971; DOI=10.1093/glycob/cwr183;
RA Raman J., Guan Y., Perrine C.L., Gerken T.A., Tabak L.A.;
RT "UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-
RT acetylgalactosaminyltransferases: completion of the family tree.";
RL Glycobiology 22:768-777(2012).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine (GalNAc)
CC residue from UDP-GalNAc to a serine or threonine residue on the protein
CC receptor (PubMed:12407114, PubMed:22186971). Generates GalNAc-O-Ser/Thr
CC structure also known as Tn antigen, which itself is immunogenic but
CC also serves as a precursor for the synthesis of different mucin-type O-
CC glycan core structures (PubMed:12407114). Contributes to the synthesis
CC of O-linked glycans on mucins and proteoglycans of the central nervous
CC system. May promote neurogenesis through glycosylation and
CC stabilization of PDPN (PubMed:12407114, PubMed:22186971) (By
CC similarity). {ECO:0000250|UniProtKB:Q8CF93,
CC ECO:0000269|PubMed:12407114, ECO:0000269|PubMed:22186971}.
CC -!- FUNCTION: [Isoform 1]: Can glycosylate both unmodified peptides and
CC glycopeptides that already contain an O-linked GalNAc sugar. Transfers
CC GalNAc to Thr-/Ser-rich tandem repeats GTTPSPVPTTSTTSAP of MUC5AC,
CC specifically on Thr-3 of non-glycosylated MUC5AC peptide, on Thr-12 and
CC Thr-13 of preglycosylated MUC5AC at Thr-3 (MUC5AC-3), on Thr-3 of
CC preglycosylated MUC5AC at Thr-13 (MUC5AC-13) and on Thr-12 of
CC preglycosylated MUC5AC at Thr-3 and Thr-13 (MUC5AC-3,13). Transfers
CC GalNAc to three consecutive serine/threonine residues on SDC3 forming a
CC triplet-Tn epitope expressed in Purkinje cells of the developing brain.
CC {ECO:0000269|PubMed:12407114, ECO:0000269|PubMed:22186971}.
CC -!- FUNCTION: [Isoform 3]: Can glycosylate both unmodified peptides and
CC glycopeptides that already contain an O-linked GalNAc sugar. Transfers
CC GalNAc to Thr-/Ser-rich tandem repeats GTTPSPVPTTSTTSAP of MUC5AC,
CC specifically on Thr-3 of non-glycosylated MUC5AC peptide, on Thr-12 and
CC Thr-13 of preglycosylated MUC5AC at Thr-3 (MUC5AC-3), on Thr-3 of
CC preglycosylated MUC5AC at Thr-13 (MUC5AC-13) and on Thr-12 of
CC preglycosylated MUC5AC at Thr-3 and Thr-13 (MUC5AC-3,13).
CC {ECO:0000269|PubMed:22186971}.
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:12407114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23957;
CC Evidence={ECO:0000305|PubMed:12407114};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:12407114, ECO:0000269|PubMed:22186971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52425;
CC Evidence={ECO:0000305|PubMed:12407114, ECO:0000305|PubMed:22186971};
CC -!- CATALYTIC ACTIVITY: [Isoform 3]:
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:22186971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52425;
CC Evidence={ECO:0000305|PubMed:22186971};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q10471};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC Kinetic parameters:
CC KM=111 uM for MUC5AC {ECO:0000269|PubMed:22186971};
CC KM=263 uM for MUC5AC-3 {ECO:0000269|PubMed:22186971};
CC KM=353 uM for MUC5AC-13 {ECO:0000269|PubMed:22186971};
CC KM=2000 uM for MUC5AC-3,13 {ECO:0000269|PubMed:22186971};
CC KM=0.11 mM for MUC1 {ECO:0000269|PubMed:12407114};
CC KM=0.046 mM for MUC7 {ECO:0000269|PubMed:12407114};
CC KM=1.33 mM for SDC3 (SDC106) {ECO:0000269|PubMed:12407114};
CC KM=0.63 mM for SDC3 (SDC155) {ECO:0000269|PubMed:12407114};
CC KM=0.38 mM for SDC3 (SDC165) {ECO:0000269|PubMed:12407114};
CC KM=0.07 mM for SDC3 (SDC284) {ECO:0000269|PubMed:12407114};
CC Vmax=0.65 nmol/min/ug enzyme toward MUC1
CC {ECO:0000269|PubMed:12407114};
CC Vmax=0.41 nmol/min/ug enzyme toward MUC7
CC {ECO:0000269|PubMed:12407114};
CC Vmax=2 nmol/min/ug enzyme toward SDC3 (SDC106)
CC {ECO:0000269|PubMed:12407114};
CC Vmax=1.17 nmol/min/ug enzyme toward SDC3 (SDC155)
CC {ECO:0000269|PubMed:12407114};
CC Vmax=0.711 nmol/min/ug enzyme toward SDC3 (SDC165)
CC {ECO:0000269|PubMed:12407114};
CC Vmax=0.212 nmol/min/ug enzyme toward SDC3 (SDC284)
CC {ECO:0000269|PubMed:12407114};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 3]:
CC Kinetic parameters:
CC KM=67 uM for MUC5AC {ECO:0000269|PubMed:22186971};
CC KM=35 uM for MUC5AC-3 {ECO:0000269|PubMed:22186971};
CC KM=130 uM for MUC5AC-13 {ECO:0000269|PubMed:22186971};
CC KM=2000 uM for MUC5AC-3,13 {ECO:0000269|PubMed:22186971};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:12407114, ECO:0000305|PubMed:22186971}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IUC8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IUC8-2; Sequence=VSP_011218, VSP_011219;
CC Name=3;
CC IsoId=Q8IUC8-3; Sequence=VSP_054411;
CC -!- TISSUE SPECIFICITY: Specifically expressed in neuronal cells. Expressed
CC in fetal brain, whole adult brain, cerebral cortex and cerebellum. Not
CC expressed in other tissues tested. {ECO:0000269|PubMed:12407114}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF19246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC85542.1; Type=Miscellaneous discrepancy; Note=Chimera. Chimeric at the N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 13;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_496";
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DR EMBL; AB078142; BAC54545.1; -; mRNA.
DR EMBL; KJ534843; AHW56483.1; -; mRNA.
DR EMBL; AJ505991; CAD44533.2; -; mRNA.
DR EMBL; AC008166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009227; AAF19246.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC009297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX11464.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11465.1; -; Genomic_DNA.
DR EMBL; BC101031; AAI01032.1; -; mRNA.
DR EMBL; BC101032; AAI01033.1; -; mRNA.
DR EMBL; BC101033; AAI01034.1; -; mRNA.
DR EMBL; BC101034; AAI01035.1; -; mRNA.
DR EMBL; AB067505; BAB67811.1; -; mRNA.
DR EMBL; AK123152; BAC85542.1; ALT_SEQ; mRNA.
DR CCDS; CCDS2199.1; -. [Q8IUC8-1]
DR CCDS; CCDS77472.1; -. [Q8IUC8-3]
DR RefSeq; NP_001288556.1; NM_001301627.1. [Q8IUC8-3]
DR RefSeq; NP_443149.2; NM_052917.3. [Q8IUC8-1]
DR RefSeq; XP_016858749.1; XM_017003260.1.
DR RefSeq; XP_016858750.1; XM_017003261.1.
DR AlphaFoldDB; Q8IUC8; -.
DR SMR; Q8IUC8; -.
DR BioGRID; 125365; 36.
DR IntAct; Q8IUC8; 5.
DR STRING; 9606.ENSP00000376570; -.
DR BindingDB; Q8IUC8; -.
DR ChEMBL; CHEMBL4523392; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8IUC8; 3 sites.
DR iPTMnet; Q8IUC8; -.
DR PhosphoSitePlus; Q8IUC8; -.
DR BioMuta; GALNT13; -.
DR DMDM; 116242497; -.
DR EPD; Q8IUC8; -.
DR jPOST; Q8IUC8; -.
DR MassIVE; Q8IUC8; -.
DR MaxQB; Q8IUC8; -.
DR PaxDb; Q8IUC8; -.
DR PeptideAtlas; Q8IUC8; -.
DR PRIDE; Q8IUC8; -.
DR ProteomicsDB; 58694; -.
DR ProteomicsDB; 70545; -. [Q8IUC8-1]
DR ProteomicsDB; 70546; -. [Q8IUC8-2]
DR Antibodypedia; 33696; 156 antibodies from 20 providers.
DR DNASU; 114805; -.
DR Ensembl; ENST00000392825.8; ENSP00000376570.3; ENSG00000144278.15. [Q8IUC8-1]
DR Ensembl; ENST00000409237.5; ENSP00000387239.1; ENSG00000144278.15. [Q8IUC8-3]
DR GeneID; 114805; -.
DR KEGG; hsa:114805; -.
DR MANE-Select; ENST00000392825.8; ENSP00000376570.3; NM_052917.4; NP_443149.2.
DR UCSC; uc002tyr.5; human. [Q8IUC8-1]
DR CTD; 114805; -.
DR DisGeNET; 114805; -.
DR GeneCards; GALNT13; -.
DR HGNC; HGNC:23242; GALNT13.
DR HPA; ENSG00000144278; Group enriched (brain, retina).
DR MIM; 608369; gene.
DR neXtProt; NX_Q8IUC8; -.
DR OpenTargets; ENSG00000144278; -.
DR PharmGKB; PA134887166; -.
DR VEuPathDB; HostDB:ENSG00000144278; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000158904; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q8IUC8; -.
DR OMA; NSNQCLA; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8IUC8; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 2681.
DR PathwayCommons; Q8IUC8; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SABIO-RK; Q8IUC8; -.
DR SignaLink; Q8IUC8; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 114805; 10 hits in 1063 CRISPR screens.
DR ChiTaRS; GALNT13; human.
DR GeneWiki; GALNT13; -.
DR GenomeRNAi; 114805; -.
DR Pharos; Q8IUC8; Tbio.
DR PRO; PR:Q8IUC8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8IUC8; protein.
DR Bgee; ENSG00000144278; Expressed in cerebellar cortex and 133 other tissues.
DR ExpressionAtlas; Q8IUC8; baseline and differential.
DR Genevisible; Q8IUC8; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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; IDA:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:UniProtKB.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA: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 Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..556
FT /note="Polypeptide N-acetylgalactosaminyltransferase 13"
FT /id="PRO_0000059130"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..556
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 428..550
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 114..224
FT /note="Catalytic subdomain A"
FT REGION 284..346
FT /note="Catalytic subdomain B"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 210
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 343
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 329..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 441..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 481..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 522..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 466..486
FT /note="VFSYTADKEIRTDDLCLDVSR -> TQWTCNHVKMPPYERKSVMGI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011218"
FT VAR_SEQ 487..556
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011219"
FT VAR_SEQ 511..556
FT /note="RLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRNMTLGT -> SC
FT LSVNKVADGSQHPTVETCNDSTLQKWLLRNYTRMEIFRNIFGNSTDYIL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054411"
FT VARIANT 59
FT /note="E -> D (in dbSNP:rs34086479)"
FT /id="VAR_049242"
FT CONFLICT 4
FT /note="F -> S (in Ref. 1; BAC54545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 64051 MW; 00F3DCDDC4754D6F CRC64;
MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI SRNQEGPGEM
GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV RLEGCKTKVY PDELPNTSVV
IVFHNEAWST LLRTVYSVIN RSPHYLLSEV ILVDDASERD FLKLTLENYV KNLEVPVKII
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
CLDVSRLNGP VIMLKCHHMR GNQLWEYDAE RLTLRHVNSN QCLDEPSEED KMVPTMQDCS
GSRSQQWLLR NMTLGT
