CGAT1_HUMAN
ID CGAT1_HUMAN Reviewed; 532 AA.
AC Q8TDX6; B2RBE4; Q6P9G6; Q8IUF9; Q9NSQ7; Q9NUM9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Chondroitin sulfate N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE Short=CsGalNAcT-1 {ECO:0000305};
DE EC=2.4.1.174 {ECO:0000269|PubMed:21160489, ECO:0000269|PubMed:27599773};
DE AltName: Full=Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1;
DE Short=Beta4GalNAcT-1;
GN Name=CSGALNACT1 {ECO:0000312|HGNC:HGNC:24290}; Synonyms=CHGN, GALNACT1;
GN ORFNames=UNQ656/PRO1287;
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, GLYCOSYLATION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT ASN-193.
RC TISSUE=Melanoma;
RX PubMed=11788602; DOI=10.1074/jbc.m111434200;
RA Uyama T., Kitagawa H., Tamura J., Sugahara K.;
RT "Molecular cloning and expression of human chondroitin N-
RT acetylgalactosaminyltransferase: key enzyme for chain initiation and
RT elongation of chondroitin/dermatan sulfate on the protein linkage region
RT tetrasaccharide shared by heparin/heparan sulfate.";
RL J. Biol. Chem. 277:8841-8846(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT ASN-193.
RX PubMed=12163485; DOI=10.1074/jbc.m203619200;
RA Gotoh M., Sato T., Akashima T., Iwasaki H., Kameyama A., Mochizuki H.,
RA Yada T., Inaba N., Zhang Y., Kikuchi N., Kwon Y.-D., Togayachi A., Kudo T.,
RA Nishihara S., Watanabe H., Kimata K., Narimatsu H.;
RT "Enzymatic synthesis of chondroitin with a novel chondroitin sulfate N-
RT acetylgalactosaminyltransferase that transfers N-acetylgalactosamine to
RT glucuronic acid in initiation and elongation of chondroitin sulfate
RT synthesis.";
RL J. Biol. Chem. 277:38189-38196(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-193.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Thalamus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ASN-193.
RC TISSUE=Placenta;
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 381-532, AND VARIANT ASN-193.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12446672; DOI=10.1074/jbc.m208886200;
RA Sato T., Gotoh M., Kiyohara K., Akashima T., Iwasaki H., Kameyama A.,
RA Mochizuki H., Yada T., Inaba N., Togayachi A., Kudo T., Asada M.,
RA Watanabe H., Imamura T., Kimata K., Narimatsu H.;
RT "Differential roles of two N-acetylgalactosaminyltransferases, CSGalNAcT-1,
RT and a novel enzyme, CSGalNAcT-2. Initiation and elongation in synthesis of
RT chondroitin sulfate.";
RL J. Biol. Chem. 278:3063-3071(2003).
RN [9]
RP FUNCTION.
RX PubMed=17145758; DOI=10.1074/jbc.m606870200;
RA Sakai K., Kimata K., Sato T., Gotoh M., Narimatsu H., Shinomiya K.,
RA Watanabe H.;
RT "Chondroitin sulfate N-acetylgalactosaminyltransferase-1 plays a critical
RT role in chondroitin sulfate synthesis in cartilage.";
RL J. Biol. Chem. 282:4152-4161(2007).
RN [10]
RP VARIANTS ARG-234 AND ARG-509, CHARACTERIZATION OF VARIANTS ARG-234 AND
RP ARG-509, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21160489; DOI=10.1038/jhg.2010.148;
RA Saigoh K., Izumikawa T., Koike T., Shimizu J., Kitagawa H., Kusunoki S.;
RT "Chondroitin beta-1,4-N-acetylgalactosaminyltransferase-1 missense
RT mutations are associated with neuropathies.";
RL J. Hum. Genet. 56:143-146(2011).
RN [11]
RP INVOLVEMENT IN SDJLABA, VARIANT SDJLABA ARG-384, CHARACTERIZATION OF
RP VARIANT SDJLAB AARG-384, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27599773; DOI=10.1002/humu.23070;
RA Vodopiutz J., Mizumoto S., Lausch E., Rossi A., Unger S., Janocha N.,
RA Costantini R., Seidl R., Greber-Platzer S., Yamada S., Mueller T.,
RA Jilma B., Ganger R., Superti-Furga A., Ikegawa S., Sugahara K.,
RA Janecke A.R.;
RT "Chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1)
RT deficiency results in a mild skeletal dysplasia and joint laxity.";
RL Hum. Mutat. 38:34-38(2017).
RN [12]
RP INVOLVEMENT IN SDJLABA.
RX PubMed=31325655; DOI=10.1016/j.bone.2019.07.016;
RA Meyer R., Schacht S., Buschmann L., Begemann M., Kraft F., Haag N.,
RA Kochs A., Schulze A., Kurth I., Elbracht M.;
RT "Biallelic CSGALNACT1-mutations cause a mild skeletal dysplasia.";
RL Bone 127:446-451(2019).
RN [13]
RP INVOLVEMENT IN SDJLABA, VARIANTS SDJLABA SER-264 AND TYR-432,
RP CHARACTERIZATION OF VARIANTS SDJLABA SER-264 AND TYR-432, AND FUNCTION.
RX PubMed=31705726; DOI=10.1002/humu.23952;
RA Mizumoto S., Janecke A.R., Sadeghpour A., Povysil G., McDonald M.T.,
RA Unger S., Greber-Platzer S., Deak K.L., Katsanis N., Superti-Furga A.,
RA Sugahara K., Davis E.E., Yamada S., Vodopiutz J.;
RT "CSGALNACT1-congenital disorder of glycosylation: A mild skeletal dysplasia
RT with advanced bone age.";
RL Hum. Mutat. 41:655-667(2020).
CC -!- FUNCTION: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc
CC to the non-reducing end of glucuronic acid (GlcUA). Required for
CC addition of the first GalNAc to the core tetrasaccharide linker and for
CC elongation of chondroitin chains. Important role in chondroitin chain
CC biosynthesis in cartilage formation and subsequent endochondral
CC ossification (PubMed:11788602, PubMed:12163485, PubMed:12446672,
CC PubMed:17145758, PubMed:31705726). Moreover, is involved in the
CC metabolism of aggrecan (By similarity). {ECO:0000250|UniProtKB:Q8BJQ9,
CC ECO:0000269|PubMed:11788602, ECO:0000269|PubMed:12163485,
CC ECO:0000269|PubMed:12446672, ECO:0000269|PubMed:17145758,
CC ECO:0000269|PubMed:21160489, ECO:0000269|PubMed:27599773,
CC ECO:0000269|PubMed:31705726}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine =
CC 3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-
CC D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23464, Rhea:RHEA-COMP:12573, Rhea:RHEA-COMP:12575,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:132093, ChEBI:CHEBI:132105; EC=2.4.1.174;
CC Evidence={ECO:0000269|PubMed:21160489, ECO:0000269|PubMed:27599773};
CC -!- INTERACTION:
CC Q8TDX6-3; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-12917736, EBI-10819434;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305|PubMed:11788602}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:11788602}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TDX6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDX6-2; Sequence=VSP_012726, VSP_012727;
CC Name=3;
CC IsoId=Q8TDX6-3; Sequence=VSP_012728;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the highest levels in placenta,
CC thyroid, bladder, prostate and adrenal gland. Detected at low levels in
CC the other tissues examined. {ECO:0000269|PubMed:11788602,
CC ECO:0000269|PubMed:12163485, ECO:0000269|PubMed:12446672}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11788602}.
CC -!- DISEASE: Skeletal dysplasia, mild, with joint laxity and advanced bone
CC age (SDJLABA) [MIM:618870]: An autosomal recessive disorder
CC characterized by skeletal dysplasia, short stature, short long bones,
CC advanced bone age, joint laxity, and facial dysmorphism.
CC {ECO:0000269|PubMed:27599773, ECO:0000269|PubMed:31325655,
CC ECO:0000269|PubMed:31705726}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_477";
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DR EMBL; AB071403; BAB85992.1; -; mRNA.
DR EMBL; AB081516; BAC16217.1; -; mRNA.
DR EMBL; AY358441; AAQ88806.1; -; mRNA.
DR EMBL; AK002126; BAA92093.1; -; mRNA.
DR EMBL; AK314625; BAG37191.1; -; mRNA.
DR EMBL; AC090541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060772; AAH60772.1; -; mRNA.
DR EMBL; AL157483; CAB75673.1; -; mRNA.
DR CCDS; CCDS6010.1; -. [Q8TDX6-1]
DR PIR; T46919; T46919.
DR RefSeq; NP_001123990.1; NM_001130518.1. [Q8TDX6-1]
DR RefSeq; NP_060841.5; NM_018371.4. [Q8TDX6-1]
DR RefSeq; XP_006716421.1; XM_006716358.2.
DR RefSeq; XP_006716422.1; XM_006716359.2.
DR RefSeq; XP_006716423.1; XM_006716360.2. [Q8TDX6-1]
DR RefSeq; XP_006716424.1; XM_006716361.2.
DR RefSeq; XP_006716425.1; XM_006716362.2.
DR RefSeq; XP_006716426.1; XM_006716363.1. [Q8TDX6-1]
DR RefSeq; XP_006716427.1; XM_006716364.3. [Q8TDX6-1]
DR RefSeq; XP_011542880.1; XM_011544578.1. [Q8TDX6-1]
DR RefSeq; XP_011542881.1; XM_011544579.1. [Q8TDX6-1]
DR RefSeq; XP_011542882.1; XM_011544580.1.
DR RefSeq; XP_011542884.1; XM_011544582.1.
DR RefSeq; XP_011542885.1; XM_011544583.1. [Q8TDX6-1]
DR RefSeq; XP_011542886.1; XM_011544584.1. [Q8TDX6-1]
DR RefSeq; XP_016869112.1; XM_017013623.1. [Q8TDX6-1]
DR RefSeq; XP_016869113.1; XM_017013624.1. [Q8TDX6-1]
DR RefSeq; XP_016869114.1; XM_017013625.1. [Q8TDX6-1]
DR RefSeq; XP_016869115.1; XM_017013626.1.
DR RefSeq; XP_016869116.1; XM_017013627.1. [Q8TDX6-1]
DR RefSeq; XP_016869117.1; XM_017013628.1. [Q8TDX6-1]
DR RefSeq; XP_016869118.1; XM_017013629.1. [Q8TDX6-1]
DR RefSeq; XP_016869119.1; XM_017013630.1.
DR RefSeq; XP_016869120.1; XM_017013631.1.
DR RefSeq; XP_016869121.1; XM_017013632.1.
DR RefSeq; XP_016869122.1; XM_017013633.1.
DR RefSeq; XP_016869123.1; XM_017013634.1.
DR RefSeq; XP_016869124.1; XM_017013635.1.
DR RefSeq; XP_016869125.1; XM_017013636.1.
DR RefSeq; XP_016869126.1; XM_017013637.1.
DR RefSeq; XP_016869127.1; XM_017013638.1. [Q8TDX6-1]
DR AlphaFoldDB; Q8TDX6; -.
DR SMR; Q8TDX6; -.
DR BioGRID; 120904; 65.
DR IntAct; Q8TDX6; 12.
DR STRING; 9606.ENSP00000411816; -.
DR BindingDB; Q8TDX6; -.
DR ChEMBL; CHEMBL2040705; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q8TDX6; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TDX6; -.
DR PhosphoSitePlus; Q8TDX6; -.
DR BioMuta; CSGALNACT1; -.
DR DMDM; 308153425; -.
DR EPD; Q8TDX6; -.
DR jPOST; Q8TDX6; -.
DR MassIVE; Q8TDX6; -.
DR MaxQB; Q8TDX6; -.
DR PaxDb; Q8TDX6; -.
DR PeptideAtlas; Q8TDX6; -.
DR PRIDE; Q8TDX6; -.
DR ProteomicsDB; 74361; -. [Q8TDX6-1]
DR ProteomicsDB; 74362; -. [Q8TDX6-2]
DR ProteomicsDB; 74363; -. [Q8TDX6-3]
DR Antibodypedia; 22388; 214 antibodies from 26 providers.
DR DNASU; 55790; -.
DR Ensembl; ENST00000332246.10; ENSP00000330805.6; ENSG00000147408.15. [Q8TDX6-1]
DR Ensembl; ENST00000397998.7; ENSP00000381084.3; ENSG00000147408.15. [Q8TDX6-3]
DR Ensembl; ENST00000454498.6; ENSP00000411816.2; ENSG00000147408.15. [Q8TDX6-1]
DR Ensembl; ENST00000519222.5; ENSP00000428216.1; ENSG00000147408.15. [Q8TDX6-3]
DR Ensembl; ENST00000522854.5; ENSP00000429809.1; ENSG00000147408.15. [Q8TDX6-1]
DR Ensembl; ENST00000692225.1; ENSP00000509853.1; ENSG00000147408.15. [Q8TDX6-1]
DR GeneID; 55790; -.
DR KEGG; hsa:55790; -.
DR MANE-Select; ENST00000692225.2; ENSP00000509853.1; NM_001354483.2; NP_001341412.1.
DR UCSC; uc003wzg.4; human. [Q8TDX6-1]
DR CTD; 55790; -.
DR DisGeNET; 55790; -.
DR GeneCards; CSGALNACT1; -.
DR HGNC; HGNC:24290; CSGALNACT1.
DR HPA; ENSG00000147408; Tissue enhanced (thyroid).
DR MalaCards; CSGALNACT1; -.
DR MIM; 616615; gene.
DR MIM; 618870; phenotype.
DR neXtProt; NX_Q8TDX6; -.
DR OpenTargets; ENSG00000147408; -.
DR PharmGKB; PA162382829; -.
DR VEuPathDB; HostDB:ENSG00000147408; -.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244968; -.
DR HOGENOM; CLU_025958_0_1_1; -.
DR InParanoid; Q8TDX6; -.
DR OMA; MCDVDIM; -.
DR OrthoDB; 389974at2759; -.
DR PhylomeDB; Q8TDX6; -.
DR TreeFam; TF318303; -.
DR BioCyc; MetaCyc:HS07428-MON; -.
DR BRENDA; 2.4.1.174; 2681.
DR BRENDA; 2.4.1.175; 2681.
DR PathwayCommons; Q8TDX6; -.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR SignaLink; Q8TDX6; -.
DR BioGRID-ORCS; 55790; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; CSGALNACT1; human.
DR GeneWiki; ChGn; -.
DR GenomeRNAi; 55790; -.
DR Pharos; Q8TDX6; Tbio.
DR PRO; PR:Q8TDX6; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8TDX6; protein.
DR Bgee; ENSG00000147408; Expressed in cartilage tissue and 197 other tissues.
DR ExpressionAtlas; Q8TDX6; baseline and differential.
DR Genevisible; Q8TDX6; HS.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030173; C:integral component of Golgi membrane; NAS:UniProtKB.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047237; F:glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; NAS:UniProtKB.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0050653; P:chondroitin sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IDA:UniProtKB.
DR GO; GO:0050651; P:dermatan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; NAS:UniProtKB.
DR GO; GO:0030210; P:heparin biosynthetic process; NAS:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046398; P:UDP-glucuronate metabolic process; IDA:UniProtKB.
DR GO; GO:0019276; P:UDP-N-acetylgalactosamine metabolic process; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008428; Chond_GalNAc.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF05679; CHGN; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disease variant; Dwarfism; Glycoprotein;
KW Golgi apparatus; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..532
FT /note="Chondroitin sulfate N-
FT acetylgalactosaminyltransferase 1"
FT /id="PRO_0000189564"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..532
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 57..100
FT /evidence="ECO:0000255"
FT BINDING 360
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 477
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..257
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012726"
FT VAR_SEQ 258..282
FT /note="MANTLINVIVPLAKRVDKFRQFMQN -> MESYSVTQAGVQWHELCSLQPSP
FT PR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012727"
FT VAR_SEQ 285..532
FT /note="EMCIEQDGRVHLTVVYFGKEEINEVKGILENTSKAANFRNFTFIQLNGEFSR
FT GKGLDVGARFWKGSNVLLFFCDVDIYFTSEFLNTCRLNTQPGKKVFYPVLFSQYNPGII
FT YGHHDAVPPLEQQLVIKKETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWGGEDVHLY
FT RKYLHSNLIVVRTPVRGLFHLWHEKRCMDELTPEQYKMCMQSKAMNEASHGQLGMLVFR
FT HEIEAHLRKQKQKTSSKKT -> PADEVFRCVPLSP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012728"
FT VARIANT 137
FT /note="V -> I (in dbSNP:rs17128518)"
FT /id="VAR_055647"
FT VARIANT 193
FT /note="S -> N (in dbSNP:rs7017776)"
FT /evidence="ECO:0000269|PubMed:11788602,
FT ECO:0000269|PubMed:12163485, ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_060391"
FT VARIANT 234
FT /note="H -> R (found in a patient with neuropathy; unknown
FT pathological significance; loss of GalNAc-transferase
FT activity; no effect on protein expression;
FT dbSNP:rs200092345)"
FT /evidence="ECO:0000269|PubMed:21160489"
FT /id="VAR_078123"
FT VARIANT 264
FT /note="N -> S (in SDJLABA; reduced GalNAc-transferase
FT activity)"
FT /evidence="ECO:0000269|PubMed:31705726"
FT /id="VAR_084187"
FT VARIANT 384
FT /note="P -> R (in SDJLABA; loss of GalNAc-transferase
FT activity; dbSNP:rs746391651)"
FT /evidence="ECO:0000269|PubMed:27599773"
FT /id="VAR_078124"
FT VARIANT 432
FT /note="D -> Y (in SDJLABA; severely reduced GalNAc
FT transferase activity)"
FT /evidence="ECO:0000269|PubMed:31705726"
FT /id="VAR_084188"
FT VARIANT 473
FT /note="F -> Y (in dbSNP:rs17128366)"
FT /id="VAR_055648"
FT VARIANT 509
FT /note="M -> R (found in a patient with neuropathy; unknown
FT pathological significance; loss of GalNAc-transferase
FT activity; no effect on protein expression;
FT dbSNP:rs533235539)"
FT /evidence="ECO:0000269|PubMed:21160489"
FT /id="VAR_078125"
FT CONFLICT 246
FT /note="G -> S (in Ref. 1; BAB85992 and 3; AAQ88806)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="K -> E (in Ref. 6; AAH60772)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="I -> V (in Ref. 4; BAA92093)"
FT /evidence="ECO:0000305"
SQ 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
