ID CHSS2_HUMAN Reviewed; 775 AA. AC Q8IZ52; B4DXU0; Q6UXD6; Q7L4G1; Q9H0F8; Q9H618; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 2. DT 23-FEB-2022, entry version 164. DE RecName: Full=Chondroitin sulfate synthase 2; DE EC=2.4.1.175; DE EC=2.4.1.226; 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; Synonyms=CSS2; ORFNames=UNQ651/PRO1281; 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), INTERACTION WITH CHSY1, TISSUE RP SPECIFICITY, AND VARIANT ARG-371. RX PubMed=12716890; DOI=10.1074/jbc.m302493200; RA Kitagawa H., Izumikawa T., Uyama T., Sugahara K.; RT "Molecular cloning of a chondroitin polymerizing factor that cooperates RT with chondroitin synthase for chondroitin polymerization."; RL J. Biol. Chem. 278:23666-23671(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, TISSUE RP SPECIFICITY, AND VARIANT ARG-371. RX PubMed=12761225; DOI=10.1074/jbc.m303657200; RA Yada T., Gotoh M., Sato T., Shionyu M., Go M., Kaseyama H., Iwasaki H., RA Kikuchi N., Kwon Y.-D., Togayachi A., Kudo T., Watanabe H., Narimatsu H., RA Kimata K.; RT "Chondroitin sulfate synthase-2. Molecular cloning and characterization of RT a novel human glycosyltransferase homologous to chondroitin sulfate RT glucuronyltransferase, which has dual enzymatic activities."; RL J. Biol. Chem. 278:30235-30247(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-371. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT RP ARG-371. RC TISSUE=Small intestine; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-371. 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-371. RC TISSUE=Brain, Muscle, and Skin; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 210-775, AND VARIANT ARG-371. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [9] RP ALTERNATIVE SPLICING, FUNCTION (ISOFORM 2), INTERACTION WITH PRKN, RP SUBCELLULAR LOCATION, AND TISSUE 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 Isoform 2 may facilitate PRKN transport into the mitochondria. In CC collaboration with PRKN, isoform 2 may enhance cell viability and CC protect cells from oxidative stress. {ECO:0000269|PubMed:12761225}. 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=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:12761225}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:12761225}; CC Note=Highest activities are measured with Mn(2+). Can also utilize CC Co(2+). {ECO:0000269|PubMed:12761225}; CC -!- SUBUNIT: Binds CHSY1. Isoform 1, isoform 2 and isoform 3 interact with CC PRKN. CC -!- INTERACTION: CC Q8IZ52-2; O60260: PRKN; NbExp=5; IntAct=EBI-9029620, EBI-716346; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus, Golgi stack CC membrane {ECO:0000305}; Single-pass type II membrane protein CC {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:22082830}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol CC {ECO:0000269|PubMed:22082830}. Mitochondrion CC {ECO:0000269|PubMed:22082830}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion matrix CC {ECO:0000269|PubMed:22082830}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8IZ52-1; Sequence=Displayed; CC Name=2; Synonyms=Klokin1; CC IsoId=Q8IZ52-2; Sequence=VSP_053433; CC Name=3; Synonyms=ChPF(D996); CC IsoId=Q8IZ52-4; Sequence=VSP_053434; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in pancreas, ovary, CC brain, heart, skeletal muscle, colon, kidney, liver, stomach, spleen CC and placenta. Isoform 3 is also ubiquitous. Isoform 2 is expressed in CC brain, spleen, ovary, testis, lung and peripheral mononuclear cells. CC {ECO:0000269|PubMed:12716890, ECO:0000269|PubMed:12761225, CC ECO:0000269|PubMed:22082830}. CC -!- SIMILARITY: Belongs to the chondroitin N- CC acetylgalactosaminyltransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB095813; BAC78393.1; -; mRNA. DR EMBL; AB086063; BAC81536.1; -; mRNA. DR EMBL; AY358403; AAQ88769.1; -; mRNA. DR EMBL; AK026331; BAB15449.1; -; mRNA. DR EMBL; AK302124; BAG63502.1; -; mRNA. DR EMBL; AC009955; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471063; EAW70768.1; -; Genomic_DNA. DR EMBL; BC008878; AAH08878.2; -; mRNA. DR EMBL; BC021223; AAH21223.2; -; mRNA. DR EMBL; BC023531; AAH23531.1; -; mRNA. DR EMBL; AL136814; CAB66748.2; -; mRNA. DR CCDS; CCDS2443.1; -. [Q8IZ52-1] DR CCDS; CCDS56169.1; -. [Q8IZ52-4] DR RefSeq; NP_001182660.1; NM_001195731.1. [Q8IZ52-4] DR RefSeq; NP_078812.2; NM_024536.5. [Q8IZ52-1] DR BioGRID; 122729; 30. DR IntAct; Q8IZ52; 17. DR MINT; Q8IZ52; -. DR STRING; 9606.ENSP00000243776; -. DR CAZy; GT31; Glycosyltransferase Family 31. DR CAZy; GT7; Glycosyltransferase Family 7. DR GlyGen; Q8IZ52; 2 sites. DR iPTMnet; Q8IZ52; -. DR PhosphoSitePlus; Q8IZ52; -. DR BioMuta; CHPF; -. DR DMDM; 311033361; -. DR EPD; Q8IZ52; -. DR jPOST; Q8IZ52; -. DR MassIVE; Q8IZ52; -. DR MaxQB; Q8IZ52; -. DR PaxDb; Q8IZ52; -. DR PeptideAtlas; Q8IZ52; -. DR PRIDE; Q8IZ52; -. DR ProteomicsDB; 71279; -. [Q8IZ52-1] DR Antibodypedia; 34339; 203 antibodies from 28 providers. DR DNASU; 79586; -. DR Ensembl; ENST00000243776; ENSP00000243776; ENSG00000123989. DR Ensembl; ENST00000535926; ENSP00000445571; ENSG00000123989. [Q8IZ52-4] DR GeneID; 79586; -. DR KEGG; hsa:79586; -. DR MANE-Select; ENST00000243776.11; ENSP00000243776.6; NM_024536.6; NP_078812.3. DR UCSC; uc002vmc.5; human. [Q8IZ52-1] DR CTD; 79586; -. DR DisGeNET; 79586; -. DR GeneCards; CHPF; -. DR HGNC; HGNC:24291; CHPF. DR HPA; ENSG00000123989; Low tissue specificity. DR MIM; 610405; gene. DR neXtProt; NX_Q8IZ52; -. DR OpenTargets; ENSG00000123989; -. DR PharmGKB; PA162382245; -. DR VEuPathDB; HostDB:ENSG00000123989; -. DR eggNOG; KOG3708; Eukaryota. DR GeneTree; ENSGT01030000234702; -. DR HOGENOM; CLU_016244_1_0_1; -. DR InParanoid; Q8IZ52; -. DR OMA; VHIIIPL; -. DR OrthoDB; 758579at2759; -. DR PhylomeDB; Q8IZ52; -. DR TreeFam; TF318303; -. DR BRENDA; 2.4.1.175; 2681. DR BRENDA; 2.4.1.226; 2681. DR PathwayCommons; Q8IZ52; -. DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis. DR SignaLink; Q8IZ52; -. DR BioGRID-ORCS; 79586; 9 hits in 1053 CRISPR screens. DR ChiTaRS; CHPF; human. DR GeneWiki; CHPF; -. DR GenomeRNAi; 79586; -. DR Pharos; Q8IZ52; Tbio. DR PRO; PR:Q8IZ52; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8IZ52; protein. DR Bgee; ENSG00000123989; Expressed in right testis and 208 other tissues. DR ExpressionAtlas; Q8IZ52; baseline and differential. DR Genevisible; Q8IZ52; HS. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. 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; IDA:FlyBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; IDA:FlyBase. DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:FlyBase. 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..775 FT /note="Chondroitin sulfate synthase 2" FT /id="PRO_0000189560" 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..775 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 37..100 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 617 FT /note="Divalent metal cation" 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:0000303|PubMed:14702039" FT /id="VSP_053433" FT VAR_SEQ 1..162 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053434" FT VARIANT 371 FT /note="Q -> R (in dbSNP:rs6436155)" FT /evidence="ECO:0000269|PubMed:11230166, FT ECO:0000269|PubMed:12716890, ECO:0000269|PubMed:12761225, FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6" FT /id="VAR_047394" FT CONFLICT 650 FT /note="A -> G (in Ref. 3; AAQ88769)" FT /evidence="ECO:0000305" SQ SEQUENCE 775 AA; 85467 MW; 94EDDB2481C97B70 CRC64; MRASLLLSVL RPAGPVAVGI SLGFTLSLLS VTWVEEPCGP GPPQPGDSEL PPRGNTNAAR RPNSVQPGAE REKPGAGEGA GENWEPRVLP YHPAQPGQAA KKAVRTRYIS TELGIRQRLL VAVLTSQTTL PTLGVAVNRT LGHRLERVVF LTGARGRRAP PGMAVVTLGE ERPIGHLHLA LRHLLEQHGD DFDWFFLVPD TTYTEAHGLA RLTGHLSLAS AAHLYLGRPQ DFIGGEPTPG RYCHGGFGVL LSRMLLQQLR PHLEGCRNDI VSARPDEWLG RCILDATGVG CTGDHEGVHY SHLELSPGEP VQEGDPHFRS ALTAHPVRDP VHMYQLHKAF ARAELERTYQ EIQELQWEIQ NTSHLAVDGD QAAAWPVGIP APSRPASRFE VLRWDYFTEQ HAFSCADGSP RCPLRGADRA DVADVLGTAL EELNRRYHPA LRLQKQQLVN GYRRFDPARG MEYTLDLQLE ALTPQGGRRP LTRRVQLLRP LSRVEILPVP YVTEASRLTV LLPLAAAERD LAPGFLEAFA TAALEPGDAA AALTLLLLYE PRQAQRVAHA DVFAPVKAHV AELERRFPGA RVPWLSVQTA APSPLRLMDL LSKKHPLDTL FLLAGPDTVL TPDFLNRCRM HAISGWQAFF PMHFQAFHPA VAPPQGPGPP ELGRDTGRFD RQAASEACFY NSDYVAARGR LAAASEQEEE LLESLDVYEL FLHFSSLHVL RAVEPALLQR YRAQTCSARL SEDLYHRCLQ SVLEGLGSRT QLAMLLFEQE QGNST //