CHSTC_HUMAN
ID CHSTC_HUMAN Reviewed; 414 AA.
AC Q9NRB3; A4D1Z9; Q502W3; Q9NXY7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Carbohydrate sulfotransferase 12;
DE EC=2.8.2.5;
DE AltName: Full=Chondroitin 4-O-sulfotransferase 2;
DE AltName: Full=Chondroitin 4-sulfotransferase 2;
DE Short=C4ST-2;
DE Short=C4ST2;
DE AltName: Full=Sulfotransferase Hlo;
GN Name=CHST12; ORFNames=UNQ500/PRO1017;
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], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=10781601; DOI=10.1074/jbc.m002443200;
RA Hiraoka N., Nakagawa H., Ong E., Akama O.T., Fukuda N.M., Fukuda M.;
RT "Molecular cloning and expression of two distinct human chondroitin 4-O-
RT sulfotransferases that belong to the HNK-1 sulfotransferase gene family.";
RL J. Biol. Chem. 275:20188-20196(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xia G., Evers M.R., Schachner M.;
RT "Cloning and expression of molecules homologous to HNK-1
RT sulfotransferase.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RC TISSUE=Colon;
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=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, 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 [7]
RP SUBSTRATE SPECIFICITY.
RX PubMed=12847091; DOI=10.1074/jbc.m306044200;
RA Mikami T., Mizumoto S., Kago N., Kitagawa H., Sugahara K.;
RT "Specificities of three distinct human chondroitin/dermatan N-
RT acetylgalactosamine 4-O-sulfotransferases demonstrated using partially
RT desulfated dermatan sulfate as an acceptor. Implication of differential
RT roles in dermatan sulfate biosynthesis.";
RL J. Biol. Chem. 278:36115-36127(2003).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-
CC acetylgalactosamine (GalNAc) residue of chondroitin and desulfated
CC dermatan sulfate. Chondroitin sulfate constitutes the predominant
CC proteoglycan present in cartilage and is distributed on the surfaces of
CC many cells and extracellular matrices. Activity toward partially
CC desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-
CC sulfated GalNAc when chondroitin sulfate C is used as an acceptor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate
CC = n adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate + n H(+);
CC Xref=Rhea:RHEA:16101, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9829,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:58422; EC=2.8.2.5;
CC Evidence={ECO:0000269|PubMed:10781601};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed a high level in spinal
CC chord, heart, spleen, thyroid, pituitary gland, adrenal gland,
CC peripheral blood leukocytes, thymus, lung, small intestine, fetal
CC kidney, fetal spleen and fetal lung. {ECO:0000269|PubMed:10781601}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; AF239822; AAF81692.1; -; mRNA.
DR EMBL; AJ289131; CAB92133.1; -; mRNA.
DR EMBL; AY358574; AAQ88937.1; -; mRNA.
DR EMBL; AK313484; BAG36268.1; -; mRNA.
DR EMBL; CH236953; EAL23955.1; -; Genomic_DNA.
DR EMBL; BC002918; AAH02918.1; -; mRNA.
DR EMBL; BC095492; AAH95492.1; -; mRNA.
DR CCDS; CCDS5333.1; -.
DR RefSeq; NP_001230723.1; NM_001243794.1.
DR RefSeq; NP_001230724.1; NM_001243795.1.
DR RefSeq; NP_061111.1; NM_018641.4.
DR RefSeq; XP_011513745.1; XM_011515443.2.
DR RefSeq; XP_011513746.1; XM_011515444.2.
DR AlphaFoldDB; Q9NRB3; -.
DR BioGRID; 120681; 312.
DR IntAct; Q9NRB3; 19.
DR STRING; 9606.ENSP00000481912; -.
DR GlyGen; Q9NRB3; 4 sites.
DR iPTMnet; Q9NRB3; -.
DR MetOSite; Q9NRB3; -.
DR PhosphoSitePlus; Q9NRB3; -.
DR BioMuta; CHST12; -.
DR EPD; Q9NRB3; -.
DR jPOST; Q9NRB3; -.
DR MassIVE; Q9NRB3; -.
DR MaxQB; Q9NRB3; -.
DR PaxDb; Q9NRB3; -.
DR PeptideAtlas; Q9NRB3; -.
DR PRIDE; Q9NRB3; -.
DR ProteomicsDB; 82325; -.
DR Antibodypedia; 24375; 76 antibodies from 23 providers.
DR DNASU; 55501; -.
DR Ensembl; ENST00000258711.7; ENSP00000258711.6; ENSG00000136213.10.
DR Ensembl; ENST00000618655.2; ENSP00000481912.1; ENSG00000136213.10.
DR GeneID; 55501; -.
DR KEGG; hsa:55501; -.
DR MANE-Select; ENST00000618655.2; ENSP00000481912.1; NM_018641.5; NP_061111.1.
DR UCSC; uc003smc.4; human.
DR CTD; 55501; -.
DR DisGeNET; 55501; -.
DR GeneCards; CHST12; -.
DR HGNC; HGNC:17423; CHST12.
DR HPA; ENSG00000136213; Low tissue specificity.
DR MIM; 610129; gene.
DR neXtProt; NX_Q9NRB3; -.
DR OpenTargets; ENSG00000136213; -.
DR PharmGKB; PA134969008; -.
DR VEuPathDB; HostDB:ENSG00000136213; -.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000156614; -.
DR HOGENOM; CLU_043398_1_0_1; -.
DR InParanoid; Q9NRB3; -.
DR OMA; HNTSTHL; -.
DR OrthoDB; 1330889at2759; -.
DR PhylomeDB; Q9NRB3; -.
DR TreeFam; TF325581; -.
DR BioCyc; MetaCyc:HS06130-MON; -.
DR BRENDA; 2.8.2.5; 2681.
DR PathwayCommons; Q9NRB3; -.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR SignaLink; Q9NRB3; -.
DR BioGRID-ORCS; 55501; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; CHST12; human.
DR GeneWiki; CHST12; -.
DR GenomeRNAi; 55501; -.
DR Pharos; Q9NRB3; Tbio.
DR PRO; PR:Q9NRB3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NRB3; protein.
DR Bgee; ENSG00000136213; Expressed in buccal mucosa cell and 185 other tissues.
DR ExpressionAtlas; Q9NRB3; baseline and differential.
DR Genevisible; Q9NRB3; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030173; C:integral component of Golgi membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; NAS:UniProtKB.
DR GO; GO:0047756; F:chondroitin 4-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030208; P:dermatan sulfate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR InterPro; IPR018011; Carb_sulfotrans_8-10.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12137; PTHR12137; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..414
FT /note="Carbohydrate sulfotransferase 12"
FT /id="PRO_0000189668"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..414
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 80..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171..177
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 245..253
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 52
FT /note="P -> H (in dbSNP:rs3735099)"
FT /id="VAR_021471"
FT VARIANT 61
FT /note="T -> S (in dbSNP:rs3735100)"
FT /id="VAR_021472"
FT VARIANT 94
FT /note="P -> L (in dbSNP:rs12536223)"
FT /id="VAR_033738"
FT VARIANT 109
FT /note="R -> S (in dbSNP:rs17132395)"
FT /id="VAR_021473"
FT VARIANT 145
FT /note="A -> P (in dbSNP:rs17132399)"
FT /id="VAR_021474"
FT CONFLICT 30
FT /note="G -> S (in Ref. 1; AAF81692)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="R -> K (in Ref. 1; AAF81692)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="P -> L (in Ref. 1; AAF81692)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="W -> C (in Ref. 1; AAF81692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 48414 MW; 8730D8731F623078 CRC64;
MTKARLFRLW LVLGSVFMIL LIIVYWDSAG AAHFYLHTSF SRPHTGPPLP TPGPDRDREL
TADSDVDEFL DKFLSAGVKQ SDLPRKETEQ PPAPGSMEES VRGYDWSPRD ARRSPDQGRQ
QAERRSVLRG FCANSSLAFP TKERAFDDIP NSELSHLIVD DRHGAIYCYV PKVACTNWKR
VMIVLSGSLL HRGAPYRDPL RIPREHVHNA SAHLTFNKFW RRYGKLSRHL MKVKLKKYTK
FLFVRDPFVR LISAFRSKFE LENEEFYRKF AVPMLRLYAN HTSLPASARE AFRAGLKVSF
ANFIQYLLDP HTEKLAPFNE HWRQVYRLCH PCQIDYDFVG KLETLDEDAA QLLQLLQVDR
QLRFPPSYRN RTASSWEEDW FAKIPLAWRQ QLYKLYEADF VLFGYPKPEN LLRD
