CGAT2_HUMAN
ID CGAT2_HUMAN Reviewed; 542 AA.
AC Q8N6G5; B3KWL7; Q6MZJ5; Q6MZP6; Q8TCH4; Q9P1I6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Chondroitin sulfate N-acetylgalactosaminyltransferase 2;
DE EC=2.4.1.174;
DE AltName: Full=Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 2;
DE Short=Beta4GalNAcT-2;
DE Short=GalNAcT-2;
GN Name=CSGALNACT2; Synonyms=CHGN2, GALNACT2; ORFNames=PRO0082;
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, 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12433924; DOI=10.1074/jbc.m209446200;
RA Uyama T., Kitagawa H., Tanaka J., Tamura J., Ogawa T., Sugahara K.;
RT "Molecular cloning and expression of a second chondroitin N-
RT acetylgalactosaminyltransferase involved in the initiation and elongation
RT of chondroitin/dermatan sulfate.";
RL J. Biol. Chem. 278:3072-3078(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-479.
RC TISSUE=Endothelial cell, and Small intestine;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 418-542 (ISOFORM 1).
RC TISSUE=Fetal liver;
RX PubMed=11483580; DOI=10.1101/gr.175501;
RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y.,
RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.;
RT "Gene expression profiling in human fetal liver and identification of
RT tissue- and developmental-stage-specific genes through compiled expression
RT profiles and efficient cloning of full-length cDNAs.";
RL Genome Res. 11:1392-1403(2001).
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. {ECO:0000269|PubMed:12433924,
CC ECO:0000269|PubMed:12446672}.
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 -!- INTERACTION:
CC Q8N6G5; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-10267100, EBI-11343438;
CC Q8N6G5; Q9UN42: ATP1B4; NbExp=3; IntAct=EBI-10267100, EBI-12894731;
CC Q8N6G5; Q8WZ55: BSND; NbExp=3; IntAct=EBI-10267100, EBI-7996695;
CC Q8N6G5; P57739: CLDN2; NbExp=3; IntAct=EBI-10267100, EBI-751440;
CC Q8N6G5; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-10267100, EBI-6942903;
CC Q8N6G5; P00387: CYB5R3; NbExp=3; IntAct=EBI-10267100, EBI-1046040;
CC Q8N6G5; P12318-2: FCGR2A; NbExp=3; IntAct=EBI-10267100, EBI-17187481;
CC Q8N6G5; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-10267100, EBI-13345167;
CC Q8N6G5; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-10267100, EBI-1052304;
CC Q8N6G5; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-10267100, EBI-373355;
CC Q8N6G5; P15941-11: MUC1; NbExp=3; IntAct=EBI-10267100, EBI-17263240;
CC Q8N6G5; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-10267100, EBI-10192441;
CC Q8N6G5; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-10267100, EBI-13389236;
CC Q8N6G5; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-10267100, EBI-17280858;
CC Q8N6G5; Q8N205: SYNE4; NbExp=3; IntAct=EBI-10267100, EBI-7131783;
CC Q8N6G5; P21579: SYT1; NbExp=3; IntAct=EBI-10267100, EBI-524909;
CC Q8N6G5; Q96AN5: TMEM143; NbExp=3; IntAct=EBI-10267100, EBI-13342951;
CC Q8N6G5; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-10267100, EBI-18178701;
CC Q8N6G5; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-10267100, EBI-10180829;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N6G5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N6G5-2; Sequence=VSP_012729, VSP_012730;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12433924,
CC ECO:0000269|PubMed:12446672}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_478";
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DR EMBL; AB079252; BAC55935.1; -; mRNA.
DR EMBL; AB090811; BAC55936.1; -; mRNA.
DR EMBL; AK074474; BAB85092.1; -; mRNA.
DR EMBL; AK125300; BAG54179.1; -; mRNA.
DR EMBL; BX640967; CAE45982.1; -; mRNA.
DR EMBL; BX641073; CAE46036.1; -; mRNA.
DR EMBL; CH471160; EAW86587.1; -; Genomic_DNA.
DR EMBL; BC030268; AAH30268.1; -; mRNA.
DR EMBL; AF116646; AAF71068.1; ALT_INIT; mRNA.
DR CCDS; CCDS7201.1; -. [Q8N6G5-1]
DR RefSeq; NP_001306583.1; NM_001319654.1.
DR RefSeq; NP_001306585.1; NM_001319656.1.
DR RefSeq; NP_061060.3; NM_018590.4. [Q8N6G5-1]
DR AlphaFoldDB; Q8N6G5; -.
DR SMR; Q8N6G5; -.
DR BioGRID; 120672; 104.
DR IntAct; Q8N6G5; 78.
DR STRING; 9606.ENSP00000363590; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q8N6G5; 2 sites.
DR iPTMnet; Q8N6G5; -.
DR PhosphoSitePlus; Q8N6G5; -.
DR BioMuta; CSGALNACT2; -.
DR DMDM; 60391915; -.
DR EPD; Q8N6G5; -.
DR jPOST; Q8N6G5; -.
DR MassIVE; Q8N6G5; -.
DR MaxQB; Q8N6G5; -.
DR PaxDb; Q8N6G5; -.
DR PeptideAtlas; Q8N6G5; -.
DR PRIDE; Q8N6G5; -.
DR ProteomicsDB; 72168; -. [Q8N6G5-1]
DR ProteomicsDB; 72169; -. [Q8N6G5-2]
DR Antibodypedia; 26871; 214 antibodies from 26 providers.
DR DNASU; 55454; -.
DR Ensembl; ENST00000374466.4; ENSP00000363590.3; ENSG00000169826.8. [Q8N6G5-1]
DR GeneID; 55454; -.
DR KEGG; hsa:55454; -.
DR MANE-Select; ENST00000374466.4; ENSP00000363590.3; NM_018590.5; NP_061060.3.
DR UCSC; uc001jan.5; human. [Q8N6G5-1]
DR CTD; 55454; -.
DR DisGeNET; 55454; -.
DR GeneCards; CSGALNACT2; -.
DR HGNC; HGNC:24292; CSGALNACT2.
DR HPA; ENSG00000169826; Tissue enriched (bone).
DR MIM; 616616; gene.
DR neXtProt; NX_Q8N6G5; -.
DR OpenTargets; ENSG00000169826; -.
DR PharmGKB; PA162382854; -.
DR VEuPathDB; HostDB:ENSG00000169826; -.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244968; -.
DR HOGENOM; CLU_025958_0_1_1; -.
DR InParanoid; Q8N6G5; -.
DR OMA; GMMVFRE; -.
DR PhylomeDB; Q8N6G5; -.
DR TreeFam; TF318303; -.
DR BioCyc; MetaCyc:HS10013-MON; -.
DR BRENDA; 2.4.1.174; 2681.
DR BRENDA; 2.4.1.175; 2681.
DR PathwayCommons; Q8N6G5; -.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR SignaLink; Q8N6G5; -.
DR BioGRID-ORCS; 55454; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; CSGALNACT2; human.
DR GenomeRNAi; 55454; -.
DR Pharos; Q8N6G5; Tbio.
DR PRO; PR:Q8N6G5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8N6G5; protein.
DR Bgee; ENSG00000169826; Expressed in secondary oocyte and 193 other tissues.
DR ExpressionAtlas; Q8N6G5; baseline and differential.
DR Genevisible; Q8N6G5; 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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0047237; F:glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IBA:GO_Central.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0050653; P:chondroitin sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; TAS:UniProtKB.
DR GO; GO:0050651; P:dermatan sulfate proteoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0050652; P:dermatan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; TAS:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic 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; Glycoprotein; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..542
FT /note="Chondroitin sulfate N-
FT acetylgalactosaminyltransferase 2"
FT /id="PRO_0000189566"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..542
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 59..105
FT /evidence="ECO:0000255"
FT BINDING 369
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 486
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 327..333
FT /note="SESNFHN -> RLASSTW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012729"
FT VAR_SEQ 334..542
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012730"
FT VARIANT 215
FT /note="E -> K (in dbSNP:rs11238456)"
FT /id="VAR_048715"
FT VARIANT 479
FT /note="P -> S (in dbSNP:rs2435381)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_048716"
FT CONFLICT 438
FT /note="Y -> H (in Ref. 3; BAB85092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 62572 MW; E19103EE6F903AB6 CRC64;
MPRRGLILHT RTHWLLLGLA LLCSLVLFMY LLECAPQTDG NASLPGVVGE NYGKEYYQAL
LQEQEEHYQT RATSLKRQIA QLKQELQEMS EKMRSLQERR NVGANGIGYQ SNKEQAPSDL
LEFLHSQIDK AEVSIGAKLP SEYGVIPFES FTLMKVFQLE MGLTRHPEEK PVRKDKRDEL
VEVIEAGLEV INNPDEDDEQ EDEEGPLGEK LIFNENDFVE GYYRTERDKG TQYELFFKKA
DLTEYRHVTL FRPFGPLMKV KSEMIDITRS IINIIVPLAE RTEAFVQFMQ NFRDVCIHQD
KKIHLTVVYF GKEGLSKVKS ILESVTSESN FHNYTLVSLN EEFNRGRGLN VGARAWDKGE
VLMFFCDVDI YFSAEFLNSC RLNAEPGKKV FYPVVFSLYN PAIVYANQEV PPPVEQQLVH
KKDSGFWRDF GFGMTCQYRS DFLTIGGFDM EVKGWGGEDV HLYRKYLHGD LIVIRTPVPG
LFHLWHEKRC ADELTPEQYR MCIQSKAMNE ASHSHLGMLV FREEIETHLH KQAYRTNSEA
VG
