CHSS3_MOUSE
ID CHSS3_MOUSE Reviewed; 884 AA.
AC Q5DTK1; B2RXU7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Chondroitin sulfate synthase 3;
DE EC=2.4.1.175;
DE EC=2.4.1.226;
DE AltName: Full=Carbohydrate synthase 2;
DE AltName: Full=Chondroitin glucuronyltransferase 3;
DE AltName: Full=Chondroitin synthase 2;
DE Short=ChSy-2;
DE AltName: Full=Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II;
DE AltName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 3;
DE AltName: Full=N-acetylgalactosaminyltransferase 3;
GN Name=Chsy3; Synonyms=Chsy2, Css3, Kiaa4168;
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 TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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: Has both beta-1,3-glucuronic acid and beta-1,4-N-
CC acetylgalactosamine transferase activity. Transfers glucuronic acid
CC (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-
CC GalNAc to the non-reducing end of the elongating chondroitin polymer.
CC Specific activity is much reduced compared to CHSY1.
CC {ECO:0000250|UniProtKB:Q70JA7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-(beta-D-GalNAc-
CC (1->4)-beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-
CC beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:20800, Rhea:RHEA-COMP:14058, Rhea:RHEA-
CC COMP:14059, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138442, ChEBI:CHEBI:138443; EC=2.4.1.175;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-
CC D-galactosamine = 3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n+1)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:55000, Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138444, ChEBI:CHEBI:138445; EC=2.4.1.175;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-
CC glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:23428, Rhea:RHEA-COMP:12575,
CC Rhea:RHEA-COMP:14058, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132105, ChEBI:CHEBI:138442;
CC EC=2.4.1.226;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-
CC D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54996,
CC Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14061, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:138444,
CC ChEBI:CHEBI:138445; EC=2.4.1.226;
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Highest activities are measured with
CC Co(2+), Mn(2+) and Cd(2+). {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90307.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220519; BAD90307.1; ALT_INIT; mRNA.
DR EMBL; CH466528; EDL09842.1; -; Genomic_DNA.
DR EMBL; BC151164; AAI51165.1; -; mRNA.
DR EMBL; BC151165; AAI51166.1; -; mRNA.
DR EMBL; BC157985; AAI57986.1; -; mRNA.
DR CCDS; CCDS37829.1; -.
DR RefSeq; NP_001074797.1; NM_001081328.1.
DR AlphaFoldDB; Q5DTK1; -.
DR SMR; Q5DTK1; -.
DR STRING; 10090.ENSMUSP00000079546; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q5DTK1; 4 sites.
DR iPTMnet; Q5DTK1; -.
DR PhosphoSitePlus; Q5DTK1; -.
DR SwissPalm; Q5DTK1; -.
DR MaxQB; Q5DTK1; -.
DR PaxDb; Q5DTK1; -.
DR PeptideAtlas; Q5DTK1; -.
DR PRIDE; Q5DTK1; -.
DR ProteomicsDB; 279075; -.
DR Antibodypedia; 25854; 107 antibodies from 25 providers.
DR DNASU; 78923; -.
DR Ensembl; ENSMUST00000080721; ENSMUSP00000079546; ENSMUSG00000058152.
DR Ensembl; ENSMUST00000238155; ENSMUSP00000158180; ENSMUSG00000058152.
DR GeneID; 78923; -.
DR KEGG; mmu:78923; -.
DR UCSC; uc008ezw.1; mouse.
DR CTD; 337876; -.
DR MGI; MGI:1926173; Chsy3.
DR VEuPathDB; HostDB:ENSMUSG00000058152; -.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_016244_2_0_1; -.
DR InParanoid; Q5DTK1; -.
DR OMA; QGPQLPE; -.
DR OrthoDB; 442283at2759; -.
DR PhylomeDB; Q5DTK1; -.
DR TreeFam; TF318303; -.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR BioGRID-ORCS; 78923; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Chsy3; mouse.
DR PRO; PR:Q5DTK1; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q5DTK1; protein.
DR Bgee; ENSMUSG00000058152; Expressed in humerus cartilage element and 114 other tissues.
DR Genevisible; Q5DTK1; 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; IBA:GO_Central.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IBA:GO_Central.
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; 2.
PE 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..884
FT /note="Chondroitin sulfate synthase 3"
FT /id="PRO_0000320145"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..884
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 47..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 722
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 836
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 108
FT /note="L -> P (in Ref. 1; BAD90307)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="V -> A (in Ref. 1; BAD90307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 884 AA; 100099 MW; D1D9E9EAA6D2FB3E CRC64;
MAVRSRRPWV SVALGLVLGF TAASWLIAPR VAELSEKRRR GSSLCSYYGR SATGPRADAQ
QLLPQPQSRP RLEQSPPPAS HELPGPQQPE AAPGGPSFRS SPWQQPALLP QRRRGHTPEG
ATALPGAPAA KGEPEEEDGG AADPRKGGRP GSSHNGSGDG GAAVPTSGPG DFLYVGVMTA
QKYLGSRALA AQRTWARFIP GRVEFFSSQQ SPSAALGQPP PPLPVIALPG VDDSYPPQKK
SFMMIKYMHD HYLDKYEWFM RADDDVYIKG DKLEEFLRSL NSSKPLYLGQ TGLGNTEELG
KLGLEPGENF CMGGPGMIFS REVLRRMVPH IGECLREMYT THEDVEVGRC VRRFGGTQCV
WSYEMQQLFH ENYEHNRKGY IQDLHNSKIH AAITLHPNKR PAYQYRLHNY MLSRKISELR
YRTIQLHRES ALMSKLSNSE VSKEDQQLGR TPSFNHFQPR ERNEVMEWEF LTGKLLYSAA
ENQPPRQSIN SILRSALDDT VLQVMEMINE NAKSRGRLID FKEIQYGYRR VDPMHGVEYI
LDLLLLYKRH KGRKLTVPVR RHAYLQQPFS KPFFREVEEL DVNRLVESIN SGTQSFSVIS
NSLKILSSLQ EAKDIGGHNE KKVHILVPLV GRYDIFLRFM ENFESTCLIP KQNVKLVIIL
FSRDAGQESI KHIELIQEYQ SRYPSAEMML IPMKGEFSRG LGLEMASSQF DNDTLLLFCD
VDLIFRGDFL QRCRDNTVQG QQVYYPIIFS QYDPKVTHMR NPPTEGDFVF SKETGFWRDY
GYGITCIYKS DLLGAGGFDT SIQGWGLEDV DLYNKVILSG LRPFRSQEVG VVHIFHPVHC
DPNLDPKQYK MCLGSKASTF ASTMQLAELW LEKHLGVRDN RTLS
