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Chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CsGalNAcT-1) (EC 2.4.1.174) (Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1) (Beta4GalNAcT-1)

 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.
12-SEP-2018, entry version 140.
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: UDP-N-acetyl-D-galactosamine + [protein]-3-O-
(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-
Xyl)-L-serine = UDP + [protein]-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-
serine. {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; -.
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; ENSGT00760000119143; -.
HOGENOM; HOG000230628; -.
HOVERGEN; HBG050930; -.
InParanoid; Q8TDX6; -.
KO; K00746; -.
OMA; GKEEMNE; -.
OrthoDB; EOG091G070I; -.
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.
CleanEx; HS_CSGALNACT1; -.
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 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; 2.
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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