CGAT2_MOUSE
ID CGAT2_MOUSE Reviewed; 542 AA.
AC Q8C1F4; Q6PAP6; Q8R5A2; Q9D2M1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 380-542.
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
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 (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
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DR EMBL; AK019496; BAB31761.2; -; mRNA.
DR EMBL; AK028045; BAC25717.1; -; mRNA.
DR EMBL; AC135861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023112; AAH23112.2; -; mRNA.
DR CCDS; CCDS20469.1; -.
DR RefSeq; NP_084441.3; NM_030165.3.
DR RefSeq; XP_006506839.1; XM_006506776.3.
DR RefSeq; XP_006506840.1; XM_006506777.3.
DR RefSeq; XP_006506841.1; XM_006506778.3.
DR AlphaFoldDB; Q8C1F4; -.
DR SMR; Q8C1F4; -.
DR BioGRID; 219612; 2.
DR STRING; 10090.ENSMUSP00000039819; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q8C1F4; 2 sites.
DR iPTMnet; Q8C1F4; -.
DR PhosphoSitePlus; Q8C1F4; -.
DR EPD; Q8C1F4; -.
DR MaxQB; Q8C1F4; -.
DR PaxDb; Q8C1F4; -.
DR PRIDE; Q8C1F4; -.
DR ProteomicsDB; 283894; -.
DR Antibodypedia; 26871; 214 antibodies from 26 providers.
DR DNASU; 78752; -.
DR Ensembl; ENSMUST00000049344; ENSMUSP00000039819; ENSMUSG00000042042.
DR GeneID; 78752; -.
DR KEGG; mmu:78752; -.
DR UCSC; uc009dll.2; mouse.
DR CTD; 55454; -.
DR MGI; MGI:1926002; Csgalnact2.
DR VEuPathDB; HostDB:ENSMUSG00000042042; -.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244968; -.
DR HOGENOM; CLU_025958_0_1_1; -.
DR InParanoid; Q8C1F4; -.
DR OMA; GMMVFRE; -.
DR OrthoDB; 389974at2759; -.
DR PhylomeDB; Q8C1F4; -.
DR TreeFam; TF318303; -.
DR BRENDA; 2.4.1.174; 3474.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR BioGRID-ORCS; 78752; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Csgalnact2; mouse.
DR PRO; PR:Q8C1F4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8C1F4; protein.
DR Bgee; ENSMUSG00000042042; Expressed in left lung lobe and 245 other tissues.
DR ExpressionAtlas; Q8C1F4; baseline and differential.
DR Genevisible; Q8C1F4; MM.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IDA:MGI.
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; IGI:MGI.
DR GO; GO:0050651; P:dermatan sulfate proteoglycan biosynthetic process; ISO:MGI.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS: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 2: Evidence at transcript level;
KW Coiled coil; Glycoprotein; Golgi apparatus; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..542
FT /note="Chondroitin sulfate N-
FT acetylgalactosaminyltransferase 2"
FT /id="PRO_0000189567"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..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 CONFLICT 397
FT /note="S -> N (in Ref. 1; BAB31761)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="T -> A (in Ref. 3; AAH23112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 62530 MW; 974D37EB441419C7 CRC64;
MSRRGSILHS RTQWLLLGLA LLFSLVLFMY LLECAPQTDG NASLPGVVRE NYGKEYYQAL
LQEQEEHYQT RATSLKRQIA QLKQELQDMS EKMRALQERK KLGANGVGYP GNREQAPSDL
LEFLHSQIDR AEVSVGAKLP SEYGVVPFES FTLMKVFQLE MGLTRHPEEK PVRKDKRDEL
VEVIEAGVEV INNPDEDDAQ EDEEGPLGEK LIFNENDFIE GYYRTERDKG TQYELFFKKA
DLMEYRHVTL FRPFGPLMKV KNELIDITRS VINIIVPLAE RTEAFSQFMQ NFRDVCIHQD
KRIHLTVVYF GKEGLSKVKS ILESVSSESD FHNYTLVSLD EEFNRGRGLN VGARAWDKGE
VLMFFCDVDI YFSAEFLNSC RLNAEPGKKV FYPVVFSLYN PAIVYANQDV PPPVEQQLVH
KKDSGFWRDF GFGMTCQYQS DFLSVGGFDM EVKGWGGEDV HLYRKYLHGD LIVIRTPVPG
LFHLWHEKHC ADELTPEQYR MCIQSKAMNE ASHSHLGMMV FREEIEMHLR KQAYRTNSET
AG
