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   27-MAR-2024, entry version 171.
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; 40.
DR   IntAct; Q8IUC8; 5.
DR   STRING; 9606.ENSP00000387239; -.
DR   BindingDB; Q8IUC8; -.
DR   ChEMBL; CHEMBL4523392; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; Q8IUC8; 3 sites, No reported glycans.
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; 9606-ENSP00000376570; -.
DR   PeptideAtlas; Q8IUC8; -.
DR   ProteomicsDB; 58694; -.
DR   ProteomicsDB; 70545; -. [Q8IUC8-1]
DR   ProteomicsDB; 70546; -. [Q8IUC8-2]
DR   Antibodypedia; 33696; 168 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   AGR; HGNC:23242; -.
DR   CTD; 114805; -.
DR   DisGeNET; 114805; -.
DR   GeneCards; GALNT13; -.
DR   HGNC; HGNC:23242; GALNT13.
DR   HPA; ENSG00000144278; Tissue enhanced (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; NYTRMEV; -.
DR   OrthoDB; 202750at2759; -.
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 1141 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 134 other cell types or tissues.
DR   ExpressionAtlas; Q8IUC8; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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; 2.80.10.50; -; 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   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF47; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 13; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   Genevisible; Q8IUC8; HS.
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
//