CGAT1_MOUSE
ID CGAT1_MOUSE Reviewed; 530 AA.
AC Q8BJQ9; Q3UNQ5; Q3UZX6; Q5FWX8; Q8BWV9; Q8BZU7; Q8C195; Q8R0M6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Chondroitin sulfate N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE Short=CsGalNAcT-1 {ECO:0000305};
DE EC=2.4.1.174 {ECO:0000250|UniProtKB:Q8TDX6};
DE AltName: Full=Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1;
DE Short=Beta4GalNAcT-1;
GN Name=Csgalnact1 {ECO:0000312|MGI:MGI:2442354}; Synonyms=Chgn, Galnact1;
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;
RC TISSUE=Brain cortex, Colon, Pituitary, Skin, and Spinal cord;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
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 [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21148564; DOI=10.1074/jbc.m110.159244;
RA Sato T., Kudo T., Ikehara Y., Ogawa H., Hirano T., Kiyohara K.,
RA Hagiwara K., Togayachi A., Ema M., Takahashi S., Kimata K., Watanabe H.,
RA Narimatsu H.;
RT "Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is necessary for
RT normal endochondral ossification and aggrecan metabolism.";
RL J. Biol. Chem. 286:5803-5812(2011).
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:17145758, PubMed:21148564). Moreover, is involved
CC in the metabolism of aggrecan (PubMed:21148564).
CC {ECO:0000269|PubMed:17145758, ECO:0000269|PubMed:21148564}.
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:0000250|UniProtKB:Q8TDX6};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: High expression in developing cartilage and during
CC chondrocyte differentiation. {ECO:0000269|PubMed:17145758}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are viable and fertile, but
CC decreased body weight and length and abnormal cartilage
CC (PubMed:21148564). {ECO:0000269|PubMed:21148564}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE25692.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK028688; BAC26066.1; -; mRNA.
DR EMBL; AK033522; BAC28340.1; -; mRNA.
DR EMBL; AK049770; BAC33912.1; -; mRNA.
DR EMBL; AK080687; BAC37982.1; -; mRNA.
DR EMBL; AK133567; BAE21729.1; -; mRNA.
DR EMBL; AK144089; BAE25692.1; ALT_SEQ; mRNA.
DR EMBL; BC026599; AAH26599.1; -; mRNA.
DR EMBL; BC089162; AAH89162.1; -; mRNA.
DR CCDS; CCDS22341.1; -.
DR RefSeq; NP_001239552.1; NM_001252623.1.
DR RefSeq; NP_766341.4; NM_172753.5.
DR RefSeq; XP_006509687.1; XM_006509624.3.
DR RefSeq; XP_006509688.1; XM_006509625.3.
DR RefSeq; XP_006509689.1; XM_006509626.1.
DR RefSeq; XP_006509690.1; XM_006509627.3.
DR RefSeq; XP_006509691.1; XM_006509628.3.
DR RefSeq; XP_006509692.1; XM_006509629.1.
DR RefSeq; XP_006509693.1; XM_006509630.3.
DR RefSeq; XP_011240592.1; XM_011242290.2.
DR AlphaFoldDB; Q8BJQ9; -.
DR SMR; Q8BJQ9; -.
DR BioGRID; 231514; 2.
DR STRING; 10090.ENSMUSP00000077459; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q8BJQ9; 2 sites.
DR iPTMnet; Q8BJQ9; -.
DR PhosphoSitePlus; Q8BJQ9; -.
DR MaxQB; Q8BJQ9; -.
DR PaxDb; Q8BJQ9; -.
DR PRIDE; Q8BJQ9; -.
DR ProteomicsDB; 281401; -.
DR Antibodypedia; 22388; 214 antibodies from 26 providers.
DR DNASU; 234356; -.
DR Ensembl; ENSMUST00000078350; ENSMUSP00000077459; ENSMUSG00000036356.
DR Ensembl; ENSMUST00000130214; ENSMUSP00000119817; ENSMUSG00000036356.
DR GeneID; 234356; -.
DR KEGG; mmu:234356; -.
DR UCSC; uc009lwf.3; mouse.
DR CTD; 55790; -.
DR MGI; MGI:2442354; Csgalnact1.
DR VEuPathDB; HostDB:ENSMUSG00000036356; -.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244968; -.
DR HOGENOM; CLU_025958_0_1_1; -.
DR InParanoid; Q8BJQ9; -.
DR OMA; MCDVDIM; -.
DR OrthoDB; 389974at2759; -.
DR PhylomeDB; Q8BJQ9; -.
DR TreeFam; TF318303; -.
DR BRENDA; 2.4.1.174; 3474.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR BioGRID-ORCS; 234356; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Csgalnact1; mouse.
DR PRO; PR:Q8BJQ9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BJQ9; protein.
DR Bgee; ENSMUSG00000036356; Expressed in stroma of bone marrow and 220 other tissues.
DR ExpressionAtlas; Q8BJQ9; baseline and differential.
DR Genevisible; Q8BJQ9; 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; ISS:UniProtKB.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047237; F:glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; IMP:MGI.
DR GO; GO:0050653; P:chondroitin sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0046398; P:UDP-glucuronate metabolic process; ISS:UniProtKB.
DR GO; GO:0019276; P:UDP-N-acetylgalactosamine metabolic 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..530
FT /note="Chondroitin sulfate N-
FT acetylgalactosaminyltransferase 1"
FT /id="PRO_0000189565"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..530
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 88..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 57..93
FT /evidence="ECO:0000255"
FT COMPBIAS 90..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 358
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 475
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 163
FT /note="R -> P (in Ref. 1; BAE25692)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="L -> M (in Ref. 1; BAC26066)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="L -> V (in Ref. 1; BAC28340)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="I -> V (in Ref. 2; AAH89162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 60917 MW; 0DE695EDEB7F7765 CRC64;
MVRRGLLGWI SRVVILLVLL CCAISVLYML ACTPKGDQEQ LGLPRANGPT GKDGYQAVLQ
EREEQHRNYV NSLKRQIAQL KDELQARSEQ FRSGQDQASD ATSLRSGWDR EPKAQADLLA
FLRGQVDKAE VHAGVKLATE YAAVPFDSFT LQKVYQLETG LTRHPEEKPV RKDKRDELVE
AIESALESLN SPVESSPHQR PYTAADFIEG IYRTERDKGT LYELTFKGDH KHEFQRLVLF
RPFGPIMKVK KEKLNLANTL INVIVPLARR VDKFRHFMQN FREMCIQQDG RVHLTVVYFG
KEEMNEVKGI LENTSKAANF RNFTFIQLNG EFSRGKGLDV GARFWKGSNV LLFFCDVDIY
FTSEFLNTCR LNTQPGKKVF YPVLFSQYNP GVIYGHHDAV PPLGQQLVIK KETGFWRDFG
FGMTCQYRSD FINIGGFDLD IKGWGGEDVH LYRKYLHSNL IVVRTPVRGL FHLWHEKHCM
DELTPEQYKM CMQSKAMNEA SHGQLGMLVF RHEIEAHLRK QKQKASSKKT
