CHSS2_MOUSE
ID CHSS2_MOUSE Reviewed; 774 AA.
AC Q6IQX7; E9PUB9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Chondroitin sulfate synthase 2 {ECO:0000305};
DE EC=2.4.1.175 {ECO:0000250|UniProtKB:Q8IZ52};
DE EC=2.4.1.226 {ECO:0000250|UniProtKB:Q8IZ52};
DE AltName: Full=Chondroitin glucuronyltransferase 2;
DE AltName: Full=Chondroitin-polymerizing factor;
DE Short=ChPF;
DE AltName: Full=Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II;
DE AltName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase II;
DE AltName: Full=N-acetylgalactosaminyltransferase 2;
GN Name=Chpf {ECO:0000312|MGI:MGI:106576}; Synonyms=Css2, D1Bwg1363e;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), INTERACTION WITH PRKN, AND TISSUE
RP SPECIFICITY.
RX PubMed=22082830; DOI=10.1093/hmg/ddr530;
RA Kuroda Y., Sako W., Goto S., Sawada T., Uchida D., Izumi Y., Takahashi T.,
RA Kagawa N., Matsumoto M., Matsumoto M., Takahashi R., Kaji R., Mitsui T.;
RT "Parkin interacts with Klokin1 for mitochondrial import and maintenance of
RT membrane potential.";
RL Hum. Mol. Genet. 21:991-1003(2012).
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 Seems to act as a specific activating factor for CHSY1 in chondroitin
CC polymerization. {ECO:0000250|UniProtKB:Q8IZ52}.
CC -!- FUNCTION: [Isoform 2]: May facilitate PRKN transport into the
CC mitochondria. In collaboration with PRKN, may enhance cell viability
CC and protect cells from oxidative stress.
CC {ECO:0000250|UniProtKB:Q8IZ52}.
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 Evidence={ECO:0000250|UniProtKB:Q8IZ52};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20801;
CC Evidence={ECO:0000250|UniProtKB:Q8IZ52};
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 Evidence={ECO:0000250|UniProtKB:Q8IZ52};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55001;
CC Evidence={ECO:0000250|UniProtKB:Q8IZ52};
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; Evidence={ECO:0000250|UniProtKB:Q8IZ52};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23429;
CC Evidence={ECO:0000250|UniProtKB:Q8IZ52};
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 Evidence={ECO:0000250|UniProtKB:Q8IZ52};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54997;
CC Evidence={ECO:0000250|UniProtKB:Q8IZ52};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8IZ52};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q8IZ52};
CC Note=Highest activities are measured with Mn(2+). Can also utilize
CC Co(2+). {ECO:0000250|UniProtKB:Q8IZ52};
CC -!- SUBUNIT: [Isoform 1]: Interacts with PRKN.
CC {ECO:0000250|UniProtKB:Q8IZ52}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with PRKN.
CC {ECO:0000250|UniProtKB:Q8IZ52}.
CC -!- SUBUNIT: [Isoform 3]: Interacts with PRKN.
CC {ECO:0000250|UniProtKB:Q8IZ52}.
CC -!- INTERACTION:
CC Q6IQX7-2; Q9WVS6: Prkn; NbExp=3; IntAct=EBI-9029659, EBI-973635;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus, Golgi stack
CC membrane {ECO:0000250|UniProtKB:Q8IZ52}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:Q8IZ52}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8IZ52}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8IZ52}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q8IZ52}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q8IZ52}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6IQX7-1; Sequence=Displayed;
CC Name=2; Synonyms=Klokin1;
CC IsoId=Q6IQX7-2; Sequence=VSP_053435;
CC Name=3; Synonyms=ChPF(D996);
CC IsoId=Q6IQX7-3; Sequence=VSP_053436;
CC -!- TISSUE SPECIFICITY: Isoform 1, isoform 2 and isoform 3 are expressed in
CC brain (at protein level). {ECO:0000269|PubMed:22082830}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
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DR EMBL; AC115011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC071273; AAH71273.1; -; mRNA.
DR EMBL; BC057050; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC060598; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS15074.1; -. [Q6IQX7-1]
DR CCDS; CCDS15075.1; -. [Q6IQX7-3]
DR RefSeq; NP_001001565.1; NM_001001565.2. [Q6IQX7-3]
DR RefSeq; NP_001001566.1; NM_001001566.3. [Q6IQX7-1]
DR AlphaFoldDB; Q6IQX7; -.
DR BioGRID; 216600; 3.
DR IntAct; Q6IQX7; 1.
DR STRING; 10090.ENSMUSP00000078199; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q6IQX7; 2 sites.
DR iPTMnet; Q6IQX7; -.
DR PhosphoSitePlus; Q6IQX7; -.
DR EPD; Q6IQX7; -.
DR MaxQB; Q6IQX7; -.
DR PaxDb; Q6IQX7; -.
DR PeptideAtlas; Q6IQX7; -.
DR PRIDE; Q6IQX7; -.
DR ProteomicsDB; 283834; -. [Q6IQX7-1]
DR ProteomicsDB; 283835; -. [Q6IQX7-2]
DR ProteomicsDB; 283836; -. [Q6IQX7-3]
DR Antibodypedia; 34339; 206 antibodies from 28 providers.
DR DNASU; 74241; -.
DR Ensembl; ENSMUST00000079205; ENSMUSP00000078199; ENSMUSG00000032997. [Q6IQX7-1]
DR Ensembl; ENSMUST00000094818; ENSMUSP00000092412; ENSMUSG00000032997. [Q6IQX7-3]
DR GeneID; 74241; -.
DR KEGG; mmu:74241; -.
DR UCSC; uc007bph.1; mouse. [Q6IQX7-1]
DR CTD; 79586; -.
DR MGI; MGI:106576; Chpf.
DR VEuPathDB; HostDB:ENSMUSG00000032997; -.
DR eggNOG; KOG3708; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_016244_1_0_1; -.
DR InParanoid; Q6IQX7; -.
DR OMA; MEGKYCY; -.
DR OrthoDB; 758579at2759; -.
DR PhylomeDB; Q6IQX7; -.
DR TreeFam; TF318303; -.
DR BRENDA; 2.4.1.175; 3474.
DR BRENDA; 2.4.1.226; 3474.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR BioGRID-ORCS; 74241; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q6IQX7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6IQX7; protein.
DR Bgee; ENSMUSG00000032997; Expressed in CA3 field of hippocampus and 135 other tissues.
DR ExpressionAtlas; Q6IQX7; baseline and differential.
DR Genevisible; Q6IQX7; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; ISO:MGI.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; ISO:MGI.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IMP:MGI.
DR InterPro; IPR008428; Chond_GalNAc.
DR Pfam; PF05679; CHGN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Glycoprotein; Golgi apparatus; Membrane;
KW Metal-binding; Mitochondrion; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..774
FT /note="Chondroitin sulfate synthase 2"
FT /id="PRO_0000189561"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..774
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 37..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 616
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..460
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053435"
FT VAR_SEQ 1..162
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053436"
SQ SEQUENCE 774 AA; 85534 MW; A3D3BA5E3142026B CRC64;
MRASLLLSVL RPAGPVAVGI SLGFTLSLLS VTWVEEPCGP GPPQPGDSEL PPRGNTNAAR
RPNSVQPGSE RERPGAGAGT GESWEPRVLP YHPAQPGQAT KKAVRTRYIS TELGIRQKLL
VAVLTSQATL PTLGVAVNRT LGHRLEHVVF LTGARGRRTP SGMAVVALGE ERPIGHLHLA
LRHLLEQHGD DFDWFFLVPD ATYTEAHGLD RLAGHLSLAS ATHLYLGRPQ DFIGGDTTPG
RYCHGGFGVL LSRTLLQQLR PHLESCRNDI VSARPDEWLG RCILDATGVG CTGDHEGMHY
NYLELSPGEP VQEGDPRFRS ALTAHPVRDP VHMYQLHKAF ARAELDRTYQ EIQELQWEIQ
NTSRLAADGE RASAWPVGIP APSRPASRFE VLRWDYFTEQ YAFSCADGSP RCPLRGADQA
DVADVLGTAL EELNRRYQPA LQLQKQQLVN GYRRFDPARG MEYTLDLQLE ALTPQGGRWP
LTRRVQLLRP LSRVEILPVP YVTEASRLTV LLPLAAAERD LASGFLEAFA TAALEPGDAA
ALTLLLLYEP RQAQRAAHSD VFAPVKAHVA ELERRFPGAR VPWLSVQTAA PSPLRLMDLL
SKKHPLDTLF LLAGPDTVLT PDFLNRCRMH AISGWQAFFP MHFQAFHPAV APPQGPGPPE
LGRDTGHFDR QAASEACFYN SDYVAARGRL VAASEQEEEL LESLDVYELF LRFSNLHVLR
AVEPALLQRY RAQPCSARLS EDLYHRCRQS VLEGLGSRTQ LAMLLFEQEQ GNST
