GENTAUR Molecular Products.

 CGAT1_HUMAN             Reviewed;         532 AA.
 Q8TDX6; B2RBE4; Q6P9G6; Q8IUF9; Q9NSQ7; Q9NUM9;
 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
 05-OCT-2010, sequence version 2.
 13-FEB-2019, entry version 144.
 RecName: Full=Chondroitin sulfate N-acetylgalactosaminyltransferase 1 {ECO:0000305};
          Short=CsGalNAcT-1 {ECO:0000305};
          EC=2.4.1.174 {ECO:0000269|PubMed:21160489, ECO:0000269|PubMed:27599773};
 AltName: Full=Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1;
          Short=Beta4GalNAcT-1;
 Name=CSGALNACT1 {ECO:0000312|HGNC:HGNC:24290};
 Synonyms=CHGN, GALNACT1; ORFNames=UNQ656/PRO1287;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, GLYCOSYLATION,
 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT ASN-193.
 TISSUE=Melanoma;
 PubMed=11788602; DOI=10.1074/jbc.M111434200;
 Uyama T., Kitagawa H., Tamura J., Sugahara K.;
 "Molecular cloning and expression of human chondroitin N-
 acetylgalactosaminyltransferase: key enzyme for chain initiation and
 elongation of chondroitin/dermatan sulfate on the protein linkage
 region tetrasaccharide shared by heparin/heparan sulfate.";
 J. Biol. Chem. 277:8841-8846(2002).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
 AND VARIANT ASN-193.
 PubMed=12163485; DOI=10.1074/jbc.M203619200;
 Gotoh M., Sato T., Akashima T., Iwasaki H., Kameyama A., Mochizuki H.,
 Yada T., Inaba N., Zhang Y., Kikuchi N., Kwon Y.-D., Togayachi A.,
 Kudo T., Nishihara S., Watanabe H., Kimata K., Narimatsu H.;
 "Enzymatic synthesis of chondroitin with a novel chondroitin sulfate
 N-acetylgalactosaminyltransferase that transfers N-acetylgalactosamine
 to glucuronic acid in initiation and elongation of chondroitin sulfate
 synthesis.";
 J. Biol. Chem. 277:38189-38196(2002).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
 ASN-193.
 PubMed=12975309; DOI=10.1101/gr.1293003;
 Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
 Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
 Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
 Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
 Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
 Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
 Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
 Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
 Wood W.I., Godowski P.J., Gray A.M.;
 "The secreted protein discovery initiative (SPDI), a large-scale
 effort to identify novel human secreted and transmembrane proteins: a
 bioinformatics assessment.";
 Genome Res. 13:2265-2270(2003).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
 TISSUE=Placenta, and Thalamus;
 PubMed=14702039; DOI=10.1038/ng1285;
 Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
 Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
 Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
 Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
 Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
 Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
 Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
 Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
 Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
 Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
 Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
 Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
 Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
 Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
 Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
 Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
 Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
 Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
 Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
 Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
 Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
 Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
 Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
 Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
 Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
 Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
 Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
 Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
 "Complete sequencing and characterization of 21,243 full-length human
 cDNAs.";
 Nat. Genet. 36:40-45(2004).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16421571; DOI=10.1038/nature04406;
 Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
 Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
 Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
 Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
 Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
 DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
 Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
 Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
 Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
 Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
 O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
 Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
 Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
 Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
 Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
 Lander E.S.;
 "DNA sequence and analysis of human chromosome 8.";
 Nature 439:331-335(2006).
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
 ASN-193.
 TISSUE=Placenta;
 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).
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-532, AND VARIANT
 ASN-193.
 TISSUE=Melanoma;
 PubMed=17974005; DOI=10.1186/1471-2164-8-399;
 Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
 Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
 Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
 Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
 "The full-ORF clone resource of the German cDNA consortium.";
 BMC Genomics 8:399-399(2007).
 [8]
 FUNCTION, AND TISSUE SPECIFICITY.
 PubMed=12446672; DOI=10.1074/jbc.M208886200;
 Sato T., Gotoh M., Kiyohara K., Akashima T., Iwasaki H., Kameyama A.,
 Mochizuki H., Yada T., Inaba N., Togayachi A., Kudo T., Asada M.,
 Watanabe H., Imamura T., Kimata K., Narimatsu H.;
 "Differential roles of two N-acetylgalactosaminyltransferases,
 CSGalNAcT-1, and a novel enzyme, CSGalNAcT-2. Initiation and
 elongation in synthesis of chondroitin sulfate.";
 J. Biol. Chem. 278:3063-3071(2003).
 [9]
 FUNCTION.
 PubMed=17145758; DOI=10.1074/jbc.M606870200;
 Sakai K., Kimata K., Sato T., Gotoh M., Narimatsu H., Shinomiya K.,
 Watanabe H.;
 "Chondroitin sulfate N-acetylgalactosaminyltransferase-1 plays a
 critical role in chondroitin sulfate synthesis in cartilage.";
 J. Biol. Chem. 282:4152-4161(2007).
 [10]
 VARIANTS ARG-234 AND ARG-509, CHARACTERIZATION OF VARIANTS ARG-234 AND
 ARG-509, FUNCTION, AND CATALYTIC ACTIVITY.
 PubMed=21160489; DOI=10.1038/jhg.2010.148;
 Saigoh K., Izumikawa T., Koike T., Shimizu J., Kitagawa H.,
 Kusunoki S.;
 "Chondroitin beta-1,4-N-acetylgalactosaminyltransferase-1 missense
 mutations are associated with neuropathies.";
 J. Hum. Genet. 56:143-146(2011).
 [11]
 INVOLVEMENT IN DISEASE, VARIANT ARG-384, CHARACTERIZATION OF VARIANT
 ARG-384, FUNCTION, AND CATALYTIC ACTIVITY.
 PubMed=27599773; DOI=10.1002/humu.23070;
 Vodopiutz J., Mizumoto S., Lausch E., Rossi A., Unger S., Janocha N.,
 Costantini R., Seidl R., Greber-Platzer S., Yamada S., Mueller T.,
 Jilma B., Ganger R., Superti-Furga A., Ikegawa S., Sugahara K.,
 Janecke A.R.;
 "Chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1)
 deficiency results in a mild skeletal dysplasia and joint laxity.";
 Hum. Mutat. 38:34-38(2017).
 -!- FUNCTION: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-
     GalNAc to the non-reducing end of glucuronic acid (GlcUA).
     Required for addition of the first GalNAc to the core
     tetrasaccharide linker and for elongation of chondroitin chains.
     Important role in chondroitin chain biosynthesis in cartilage
     formation and subsequent endochondral ossification
     (PubMed:11788602, PubMed:12163485, PubMed:12446672,
     PubMed:17145758). Moreover, is involved in the metabolism of
     aggrecan (By similarity). {ECO:0000250|UniProtKB:Q8BJQ9,
     ECO:0000269|PubMed:11788602, ECO:0000269|PubMed:12163485,
     ECO:0000269|PubMed:12446672, ECO:0000269|PubMed:17145758,
     ECO:0000269|PubMed:21160489, ECO:0000269|PubMed:27599773}.
 -!- CATALYTIC ACTIVITY:
     Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-
       (1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-
       galactosamine = 3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-
       beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
       [protein] + H(+) + UDP; Xref=Rhea:RHEA:23464, Rhea:RHEA-
       COMP:12573, Rhea:RHEA-COMP:12575, ChEBI:CHEBI:15378,
       ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:132093,
       ChEBI:CHEBI:132105; EC=2.4.1.174;
       Evidence={ECO:0000269|PubMed:21160489,
       ECO:0000269|PubMed:27599773};
 -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
     {ECO:0000305|PubMed:11788602}; Single-pass type II membrane
     protein {ECO:0000305|PubMed:11788602}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=3;
     Name=1;
       IsoId=Q8TDX6-1; Sequence=Displayed;
     Name=2;
       IsoId=Q8TDX6-2; Sequence=VSP_012726, VSP_012727;
       Note=No experimental confirmation available.;
     Name=3;
       IsoId=Q8TDX6-3; Sequence=VSP_012728;
       Note=No experimental confirmation available.;
 -!- TISSUE SPECIFICITY: Ubiquitous, with the highest levels in
     placenta, thyroid, bladder, prostate and adrenal gland. Detected
     at low levels in the other tissues examined.
     {ECO:0000269|PubMed:11788602, ECO:0000269|PubMed:12163485,
     ECO:0000269|PubMed:12446672}.
 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11788602}.
 -!- SIMILARITY: Belongs to the chondroitin N-
     acetylgalactosaminyltransferase family. {ECO:0000305}.
 -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
     Note=Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1;
     URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_477";
 -----------------------------------------------------------------------
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 EMBL; AB071403; BAB85992.1; -; mRNA.
 EMBL; AB081516; BAC16217.1; -; mRNA.
 EMBL; AY358441; AAQ88806.1; -; mRNA.
 EMBL; AK002126; BAA92093.1; -; mRNA.
 EMBL; AK314625; BAG37191.1; -; mRNA.
 EMBL; AC090541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC090786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC116376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC060772; AAH60772.1; -; mRNA.
 EMBL; AL157483; CAB75673.1; -; mRNA.
 CCDS; CCDS6010.1; -. [Q8TDX6-1]
 PIR; T46919; T46919.
 RefSeq; NP_001123990.1; NM_001130518.1. [Q8TDX6-1]
 RefSeq; NP_060841.5; NM_018371.4. [Q8TDX6-1]
 RefSeq; XP_006716421.1; XM_006716358.2.
 RefSeq; XP_006716422.1; XM_006716359.2.
 RefSeq; XP_006716423.1; XM_006716360.2. [Q8TDX6-1]
 RefSeq; XP_006716424.1; XM_006716361.2.
 RefSeq; XP_006716425.1; XM_006716362.2.
 RefSeq; XP_006716426.1; XM_006716363.1. [Q8TDX6-1]
 RefSeq; XP_006716427.1; XM_006716364.3. [Q8TDX6-1]
 RefSeq; XP_011542880.1; XM_011544578.1. [Q8TDX6-1]
 RefSeq; XP_011542881.1; XM_011544579.1. [Q8TDX6-1]
 RefSeq; XP_011542882.1; XM_011544580.1.
 RefSeq; XP_011542884.1; XM_011544582.1.
 RefSeq; XP_011542885.1; XM_011544583.1. [Q8TDX6-1]
 RefSeq; XP_011542886.1; XM_011544584.1. [Q8TDX6-1]
 RefSeq; XP_016869112.1; XM_017013623.1. [Q8TDX6-1]
 RefSeq; XP_016869113.1; XM_017013624.1. [Q8TDX6-1]
 RefSeq; XP_016869114.1; XM_017013625.1. [Q8TDX6-1]
 RefSeq; XP_016869115.1; XM_017013626.1.
 RefSeq; XP_016869116.1; XM_017013627.1. [Q8TDX6-1]
 RefSeq; XP_016869117.1; XM_017013628.1. [Q8TDX6-1]
 RefSeq; XP_016869118.1; XM_017013629.1. [Q8TDX6-1]
 RefSeq; XP_016869119.1; XM_017013630.1.
 RefSeq; XP_016869120.1; XM_017013631.1.
 RefSeq; XP_016869121.1; XM_017013632.1.
 RefSeq; XP_016869122.1; XM_017013633.1.
 RefSeq; XP_016869123.1; XM_017013634.1.
 RefSeq; XP_016869124.1; XM_017013635.1.
 RefSeq; XP_016869125.1; XM_017013636.1.
 RefSeq; XP_016869126.1; XM_017013637.1.
 RefSeq; XP_016869127.1; XM_017013638.1. [Q8TDX6-1]
 UniGene; Hs.613729; -.
 UniGene; Hs.721954; -.
 ProteinModelPortal; Q8TDX6; -.
 BioGrid; 120904; 13.
 IntAct; Q8TDX6; 2.
 STRING; 9606.ENSP00000310891; -.
 BindingDB; Q8TDX6; -.
 ChEMBL; CHEMBL2040705; -.
 CAZy; GT7; Glycosyltransferase Family 7.
 iPTMnet; Q8TDX6; -.
 PhosphoSitePlus; Q8TDX6; -.
 BioMuta; CSGALNACT1; -.
 DMDM; 308153425; -.
 EPD; Q8TDX6; -.
 jPOST; Q8TDX6; -.
 MaxQB; Q8TDX6; -.
 PaxDb; Q8TDX6; -.
 PeptideAtlas; Q8TDX6; -.
 PRIDE; Q8TDX6; -.
 ProteomicsDB; 74361; -.
 ProteomicsDB; 74362; -. [Q8TDX6-2]
 ProteomicsDB; 74363; -. [Q8TDX6-3]
 Ensembl; ENST00000332246; ENSP00000330805; ENSG00000147408. [Q8TDX6-1]
 Ensembl; ENST00000397998; ENSP00000381084; ENSG00000147408. [Q8TDX6-3]
 Ensembl; ENST00000454498; ENSP00000411816; ENSG00000147408. [Q8TDX6-1]
 Ensembl; ENST00000519222; ENSP00000428216; ENSG00000147408. [Q8TDX6-3]
 Ensembl; ENST00000522854; ENSP00000429809; ENSG00000147408. [Q8TDX6-1]
 GeneID; 55790; -.
 KEGG; hsa:55790; -.
 UCSC; uc003wzg.4; human. [Q8TDX6-1]
 CTD; 55790; -.
 DisGeNET; 55790; -.
 EuPathDB; HostDB:ENSG00000147408.14; -.
 GeneCards; CSGALNACT1; -.
 H-InvDB; HIX0007349; -.
 HGNC; HGNC:24290; CSGALNACT1.
 HPA; HPA061336; -.
 MIM; 616615; gene.
 neXtProt; NX_Q8TDX6; -.
 OpenTargets; ENSG00000147408; -.
 PharmGKB; PA162382829; -.
 eggNOG; KOG3588; Eukaryota.
 eggNOG; ENOG410XNYM; LUCA.
 GeneTree; ENSGT00940000153626; -.
 HOGENOM; HOG000230628; -.
 HOVERGEN; HBG050930; -.
 InParanoid; Q8TDX6; -.
 KO; K00746; -.
 OMA; RMCMQSK; -.
 OrthoDB; 389974at2759; -.
 PhylomeDB; Q8TDX6; -.
 TreeFam; TF318303; -.
 BioCyc; MetaCyc:HS07428-MONOMER; -.
 BRENDA; 2.4.1.174; 2681.
 BRENDA; 2.4.1.175; 2681.
 Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
 ChiTaRS; CSGALNACT1; human.
 GeneWiki; ChGn; -.
 GenomeRNAi; 55790; -.
 PRO; PR:Q8TDX6; -.
 Proteomes; UP000005640; Chromosome 8.
 Bgee; ENSG00000147408; Expressed in 230 organ(s), highest expression level in thyroid gland.
 ExpressionAtlas; Q8TDX6; baseline and differential.
 Genevisible; Q8TDX6; HS.
 GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
 GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
 GO; GO:0030173; C:integral component of Golgi membrane; NAS:UniProtKB.
 GO; GO:0005622; C:intracellular; IC:UniProtKB.
 GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IDA:UniProtKB.
 GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
 GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
 GO; GO:0047237; F:glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
 GO; GO:0046872; F:metal ion binding; NAS:UniProtKB.
 GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:UniProtKB.
 GO; GO:0009653; P:anatomical structure morphogenesis; NAS:UniProtKB.
 GO; GO:0051216; P:cartilage development; IEA:Ensembl.
 GO; GO:0008283; P:cell population proliferation; NAS:UniProtKB.
 GO; GO:0008037; P:cell recognition; NAS:UniProtKB.
 GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:UniProtKB.
 GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
 GO; GO:0050653; P:chondroitin sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IDA:UniProtKB.
 GO; GO:0050651; P:dermatan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
 GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
 GO; GO:0030198; P:extracellular matrix organization; NAS:UniProtKB.
 GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; NAS:UniProtKB.
 GO; GO:0030210; P:heparin biosynthetic process; NAS:UniProtKB.
 GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
 GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:UniProtKB.
 GO; GO:0046398; P:UDP-glucuronate metabolic process; IDA:UniProtKB.
 GO; GO:0019276; P:UDP-N-acetylgalactosamine metabolic process; IDA:UniProtKB.
 Gene3D; 3.90.550.10; -; 1.
 InterPro; IPR008428; Chond_GalNAc.
 InterPro; IPR029044; Nucleotide-diphossugar_trans.
 Pfam; PF05679; CHGN; 1.
 SUPFAM; SSF53448; SSF53448; 1.
 1: Evidence at protein level;
 Alternative splicing; Coiled coil; Complete proteome;
 Disease mutation; Glycoprotein; Golgi apparatus; Membrane;
 Metal-binding; Polymorphism; Reference proteome; Signal-anchor;
 Transferase; Transmembrane; Transmembrane helix.
 CHAIN         1    532       Chondroitin sulfate N-
                              acetylgalactosaminyltransferase 1.
                              /FTId=PRO_0000189564.
 TOPO_DOM      1     14       Cytoplasmic. {ECO:0000255}.
 TRANSMEM     15     35       Helical; Signal-anchor for type II
                              membrane protein. {ECO:0000255}.
 TOPO_DOM     36    532       Lumenal. {ECO:0000255}.
 COILED       57    100       {ECO:0000255}.
 METAL       360    360       Divalent metal cation. {ECO:0000255}.
 METAL       477    477       Divalent metal cation. {ECO:0000255}.
 CARBOHYD    315    315       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    324    324       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 VAR_SEQ       1    257       Missing (in isoform 2).
                              {ECO:0000303|PubMed:14702039}.
                              /FTId=VSP_012726.
 VAR_SEQ     258    282       MANTLINVIVPLAKRVDKFRQFMQN -> MESYSVTQAGVQ
                              WHELCSLQPSPPR (in isoform 2).
                              {ECO:0000303|PubMed:14702039}.
                              /FTId=VSP_012727.
 VAR_SEQ     285    532       EMCIEQDGRVHLTVVYFGKEEINEVKGILENTSKAANFRNF
                              TFIQLNGEFSRGKGLDVGARFWKGSNVLLFFCDVDIYFTSE
                              FLNTCRLNTQPGKKVFYPVLFSQYNPGIIYGHHDAVPPLEQ
                              QLVIKKETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWGG
                              EDVHLYRKYLHSNLIVVRTPVRGLFHLWHEKRCMDELTPEQ
                              YKMCMQSKAMNEASHGQLGMLVFRHEIEAHLRKQKQKTSSK
                              KT -> PADEVFRCVPLSP (in isoform 3).
                              {ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_012728.
 VARIANT     137    137       V -> I (in dbSNP:rs17128518).
                              /FTId=VAR_055647.
 VARIANT     193    193       S -> N (in dbSNP:rs7017776).
                              {ECO:0000269|PubMed:11788602,
                              ECO:0000269|PubMed:12163485,
                              ECO:0000269|PubMed:12975309,
                              ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:17974005}.
                              /FTId=VAR_060391.
 VARIANT     234    234       H -> R (found in a patient with
                              neuropathy; unknown pathological
                              significance; loss of GalNAc-transferase
                              activity; no effect on protein
                              expression; dbSNP:rs200092345).
                              {ECO:0000269|PubMed:21160489}.
                              /FTId=VAR_078123.
 VARIANT     384    384       P -> R (probable disease-associated
                              mutation found in a patient with a mild
                              skeletal dysplasia with shortness of long
                              bones of prenatal onset; loss of GalNAc-
                              transferase activity; dbSNP:rs746391651).
                              {ECO:0000269|PubMed:27599773}.
                              /FTId=VAR_078124.
 VARIANT     473    473       F -> Y (in dbSNP:rs17128366).
                              /FTId=VAR_055648.
 VARIANT     509    509       M -> R (found in a patient with
                              neuropathy; unknown pathological
                              significance; loss of GalNAc-transferase
                              activity; no effect on protein
                              expression; dbSNP:rs533235539).
                              {ECO:0000269|PubMed:21160489}.
                              /FTId=VAR_078125.
 CONFLICT    246    246       G -> S (in Ref. 1; BAB85992 and 3;
                              AAQ88806). {ECO:0000305}.
 CONFLICT    252    252       K -> E (in Ref. 6; AAH60772).
                              {ECO:0000305}.
 CONFLICT    312    312       I -> V (in Ref. 4; BAA92093).
                              {ECO:0000305}.
 SEQUENCE   532 AA;  61294 MW;  DB76B0FD6D74FD82 CRC64;
 MMMVRRGLLA WISRVVVLLV LLCCAISVLY MLACTPKGDE EQLALPRANS PTGKEGYQAV
 LQEWEEQHRN YVSSLKRQIA QLKEELQERS EQLRNGQYQA SDAAGLGLDR SPPEKTQADL
 LAFLHSQVDK AEVNAGVKLA TEYAAVPFDS FTLQKVYQLE TGLTRHPEEK PVRKDKRDEL
 VEAIESALET LNSPAENSPN HRPYTASDFI EGIYRTERDK GTLYELTFKG DHKHEFKRLI
 LFRPFGPIMK VKNEKLNMAN TLINVIVPLA KRVDKFRQFM QNFREMCIEQ DGRVHLTVVY
 FGKEEINEVK GILENTSKAA NFRNFTFIQL NGEFSRGKGL DVGARFWKGS NVLLFFCDVD
 IYFTSEFLNT CRLNTQPGKK VFYPVLFSQY NPGIIYGHHD AVPPLEQQLV IKKETGFWRD
 FGFGMTCQYR SDFINIGGFD LDIKGWGGED VHLYRKYLHS NLIVVRTPVR GLFHLWHEKR
 CMDELTPEQY KMCMQSKAMN EASHGQLGML VFRHEIEAHL RKQKQKTSSK KT

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