Reviewed, UniProtKB/Swiss-Prot Q8TDX6 (CGAT1_HUMAN)

Names and origin

Protein names

Recommended name:
    Chondroitin sulfate N-acetylgalactosaminyltransferase 1
      Short name=CsGalNAcT-1
    EC=2.4.1.174
Alternative name(s):
    Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1
      Short name=Beta4GalNAcT-1

Gene names

Name:	CSGALNACT1
Synonyms:	CHGN, GALNACT1
ORF Names:	UNQ656/PRO1287

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	532 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Ref.1 Ref.2 Ref.7 Ref.8
Catalytic activity	UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan = UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein Probable.
Tissue specificity	Ubiquitous, with the highest levels in placenta, thyroid, bladder, prostate and adrenal gland. Detected at low levels in the other tissues examined. Ref.1 Ref.2 Ref.7
Post-translational modification	N-glycosylated. Ref.1
Sequence similarities	Belongs to the chondroitin N-acetylgalactosaminyltransferase family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Signal-anchor Transmembrane
Ligand	Metal-binding
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	UDP-N-acetylgalactosamine metabolic process Inferred from direct assay. Source: UniProtKB UDP-glucuronate metabolic process Inferred from direct assay. Source: UniProtKB anatomical structure morphogenesis Non-traceable author statement. Source: UniProtKB cell proliferation Non-traceable author statement. Source: UniProtKB cell recognition Non-traceable author statement. Source: UniProtKB chondroitin sulfate biosynthetic process Ref.2 Inferred from direct assay. Source: UniProtKB chondroitin sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Ref.2 Inferred from direct assay. Source: UniProtKB dermatan sulfate proteoglycan biosynthetic process Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB extracellular matrix organization Non-traceable author statement. Source: UniProtKB heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Non-traceable author statement. Source: UniProtKB heparin biosynthetic process Non-traceable author statement. Source: UniProtKB nervous system development Non-traceable author statement. Source: UniProtKB
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: InterPro integral to Golgi membrane Non-traceable author statement. Source: UniProtKB soluble fraction Inferred from direct assay. Source: UniProtKB
Molecular function	glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity Ref.2 Inferred from direct assay. Source: UniProtKB glucuronosyltransferase activity Inferred from direct assay. Source: UniProtKB glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity Ref.2 Inferred from direct assay. Source: UniProtKB metal ion binding Ref.2 Non-traceable author statement. Source: UniProtKB peptidoglycan glycosyltransferase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8TDX6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8TDX6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-257: Missing.
     258-282: MANTLINVIVPLAKRVDKFRQFMQN → MESYSVTQAGVQWHELCSLQPSPPR

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8TDX6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     285-532: EMCIEQDGRV...QKQKTSSKKT → PADEVFRCVPLSP

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 532	532	Chondroitin sulfate N-acetylgalactosaminyltransferase 1		PRO_0000189564
Regions
	Topological domain	1 – 14	14	Cytoplasmic Potential
	Transmembrane	15 – 35	21	Signal-anchor for type II membrane protein Potential
	Topological domain	36 – 532	497	Lumenal Potential
	Coiled coil	57 – 100	44	Potential
Sites
	Metal binding	360	1	Divalent metal cation Potential
	Metal binding	477	1	Divalent metal cation Potential
Amino acid modifications
	Glycosylation	315	1	N-linked (GlcNAc...) Potential
	Glycosylation	324	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 257	257	Missing in isoform 2.		VSP_012726
	Alternative sequence	258 – 282	25	MANTL…QFMQN → MESYSVTQAGVQWHELCSLQ PSPPR in isoform 2.		VSP_012727
	Alternative sequence	285 – 532	248	EMCIE…SSKKT → PADEVFRCVPLSP in isoform 3.		VSP_012728
	Natural variant	137	1	V → I: dbSNP rs17128518.		VAR_055647
	Natural variant	193	1	N → S: dbSNP rs7017776.		VAR_060391
	Natural variant	473	1	F → Y: dbSNP rs17128366.		VAR_055648
Experimental info
	Sequence conflict	246	1	S → G in BAC16217. Ref.2
	Sequence conflict	246	1	S → G in AAH60772. Ref.5
	Sequence conflict	252	1	K → E in AAH60772. Ref.5
	Sequence conflict	312	1	I → V in BAA92093. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: CC60FA772489C35A	FASTA	532	61,351
	10 20 30 40 50 60 MMMVRRGLLA WISRVVVLLV LLCCAISVLY MLACTPKGDE EQLALPRANS PTGKEGYQAV 70 80 90 100 110 120 LQEWEEQHRN YVSSLKRQIA QLKEELQERS EQLRNGQYQA SDAAGLGLDR SPPEKTQADL 130 140 150 160 170 180 LAFLHSQVDK AEVNAGVKLA TEYAAVPFDS FTLQKVYQLE TGLTRHPEEK PVRKDKRDEL 190 200 210 220 230 240 VEAIESALET LNNPAENSPN HRPYTASDFI EGIYRTERDK GTLYELTFKG DHKHEFKRLI 250 260 270 280 290 300 LFRPFSPIMK VKNEKLNMAN TLINVIVPLA KRVDKFRQFM QNFREMCIEQ DGRVHLTVVY 310 320 330 340 350 360 FGKEEINEVK GILENTSKAA NFRNFTFIQL NGEFSRGKGL DVGARFWKGS NVLLFFCDVD 370 380 390 400 410 420 IYFTSEFLNT CRLNTQPGKK VFYPVLFSQY NPGIIYGHHD AVPPLEQQLV IKKETGFWRD 430 440 450 460 470 480 FGFGMTCQYR SDFINIGGFD LDIKGWGGED VHLYRKYLHS NLIVVRTPVR GLFHLWHEKR 490 500 510 520 530 CMDELTPEQY KMCMQSKAMN EASHGQLGML VFRHEIEAHL RKQKQKTSSK KT
	Isoform 2. Checksum: B9353B075BE8C7DB	FASTA	275	31,924
	10 20 30 40 50 60 MESYSVTQAG VQWHELCSLQ PSPPRFREMC IEQDGRVHLT VVYFGKEEIN EVKGILENTS 70 80 90 100 110 120 KAANFRNFTF IQLNGEFSRG KGLDVGARFW KGSNVLLFFC DVDIYFTSEF LNTCRLNTQP 130 140 150 160 170 180 GKKVFYPVLF SQYNPGIIYG HHDAVPPLEQ QLVIKKETGF WRDFGFGMTC QYRSDFINIG 190 200 210 220 230 240 GFDLDIKGWG GEDVHLYRKY LHSNLIVVRT PVRGLFHLWH EKRCMDELTP EQYKMCMQSK 250 260 270 AMNEASHGQL GMLVFRHEIE AHLRKQKQKT SSKKT
	Isoform 3. Checksum: 6A93FDBEEC3BDE36	FASTA	297	33,974
	10 20 30 40 50 60 MMMVRRGLLA WISRVVVLLV LLCCAISVLY MLACTPKGDE EQLALPRANS PTGKEGYQAV 70 80 90 100 110 120 LQEWEEQHRN YVSSLKRQIA QLKEELQERS EQLRNGQYQA SDAAGLGLDR SPPEKTQADL 130 140 150 160 170 180 LAFLHSQVDK AEVNAGVKLA TEYAAVPFDS FTLQKVYQLE TGLTRHPEEK PVRKDKRDEL 190 200 210 220 230 240 VEAIESALET LNNPAENSPN HRPYTASDFI EGIYRTERDK GTLYELTFKG DHKHEFKRLI 250 260 270 280 290 LFRPFSPIMK VKNEKLNMAN TLINVIVPLA KRVDKFRQFM QNFRPADEVF RCVPLSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Uyama T., Kitagawa H., Tamura J., Sugahara K. J. Biol. Chem. 277:8841-8846(2002) [PubMed: 11788602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Melanoma.
[2]	"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." 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. J. Biol. Chem. 277:38189-38196(2002) [PubMed: 12163485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." 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. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Placenta.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Placenta.
[6]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-532. Tissue: Melanoma.
[7]	"Differential roles of two N-acetylgalactosaminyltransferases, CSGalNAcT-1, and a novel enzyme, CSGalNAcT-2. Initiation and elongation in synthesis of chondroitin sulfate." 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. J. Biol. Chem. 278:3063-3071(2003) [PubMed: 12446672] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[8]	"Chondroitin sulfate N-acetylgalactosaminyltransferase-1 plays a critical role in chondroitin sulfate synthesis in cartilage." Sakai K., Kimata K., Sato T., Gotoh M., Narimatsu H., Shinomiya K., Watanabe H. J. Biol. Chem. 282:4152-4161(2007) [PubMed: 17145758] [Abstract] Cited for: FUNCTION.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB071403 mRNA. Translation: BAB85992.1. AB081516 mRNA. Translation: BAC16217.1. AY358441 mRNA. Translation: AAQ88806.1. AK002126 mRNA. Translation: BAA92093.1. BC060772 mRNA. Translation: AAH60772.1. AL157483 mRNA. Translation: CAB75673.1.
IPI	IPI00171386. IPI00216738. IPI00550004.
PIR	T46919.
RefSeq	NP_060841.5.
UniGene	Hs.613729 Hs.655166
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8TDX6.
Protein family/group databases
CAZy	GT7. Glycosyltransferase Family 7.
Proteomic databases
PRIDE	Q8TDX6.
Genome annotation databases
Ensembl	ENST00000311540; ENSP00000310891; ENSG00000147408; Homo sapiens. [Genome view] ENST00000332246; ENSP00000330805; ENSG00000147408; Homo sapiens. [Genome view] ENST00000397998; ENSP00000381084; ENSG00000147408; Homo sapiens. [Genome view] ENST00000454498; ENSP00000411816; ENSG00000147408; Homo sapiens. [Genome view]
GeneID	55790.
Organism-specific databases
CTD	55790.
GeneCards	GC08M019306.
H-InvDB	HIX0007349.
HGNC	HGNC:24290. CSGALNACT1.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8TDX6.
HOVERGEN	Q8TDX6.
Enzyme and pathway databases
BRENDA	2.4.1.174. 247. 2.4.1.175. 247.
Gene expression databases
ArrayExpress	Q8TDX6.
Bgee	Q8TDX6.
CleanEx	HS_CSGALNACT1.
Genevestigator	Q8TDX6.
GermOnline	ENSG00000147408. Homo sapiens.
Family and domain databases
InterPro	IPR008428. Chond_GalNAc. [Graphical view]
PANTHER	PTHR12369. CHGN. 1 hit.
Pfam	PF05679. CHGN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CGAT1_HUMAN

Accession

Primary (citable) accession number: Q8TDX6
Secondary accession number(s): Q6P9G6 , Q8IUF9, Q9NSQ7, Q9NUM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	June 1, 2002
Last modified:	November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.