CHSTC_MOUSE
ID CHSTC_MOUSE Reviewed; 419 AA.
AC Q99LL3; Q3TCX9; Q9JJS3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 132.
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;
GN Name=Chst12;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart;
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 [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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: 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 (By
CC similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; AJ289132; CAB92140.1; -; mRNA.
DR EMBL; AK142155; BAE24951.1; -; mRNA.
DR EMBL; AK170484; BAE41826.1; -; mRNA.
DR EMBL; AK171208; BAE42314.1; -; mRNA.
DR EMBL; CH466529; EDL19118.1; -; Genomic_DNA.
DR EMBL; BC003201; AAH03201.1; -; mRNA.
DR CCDS; CCDS19820.1; -.
DR RefSeq; NP_067503.3; NM_021528.3.
DR RefSeq; XP_006504788.1; XM_006504725.2.
DR AlphaFoldDB; Q99LL3; -.
DR BioGRID; 208498; 1.
DR STRING; 10090.ENSMUSP00000041663; -.
DR GlyGen; Q99LL3; 4 sites.
DR iPTMnet; Q99LL3; -.
DR PhosphoSitePlus; Q99LL3; -.
DR EPD; Q99LL3; -.
DR MaxQB; Q99LL3; -.
DR PaxDb; Q99LL3; -.
DR PRIDE; Q99LL3; -.
DR ProteomicsDB; 281680; -.
DR Antibodypedia; 24375; 76 antibodies from 23 providers.
DR DNASU; 59031; -.
DR Ensembl; ENSMUST00000043050; ENSMUSP00000041663; ENSMUSG00000036599.
DR GeneID; 59031; -.
DR KEGG; mmu:59031; -.
DR UCSC; uc009ahs.2; mouse.
DR CTD; 55501; -.
DR MGI; MGI:1929064; Chst12.
DR VEuPathDB; HostDB:ENSMUSG00000036599; -.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000156614; -.
DR HOGENOM; CLU_043398_1_0_1; -.
DR InParanoid; Q99LL3; -.
DR OMA; HNTSTHL; -.
DR OrthoDB; 1330889at2759; -.
DR PhylomeDB; Q99LL3; -.
DR TreeFam; TF325581; -.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR BioGRID-ORCS; 59031; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Chst12; mouse.
DR PRO; PR:Q99LL3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99LL3; protein.
DR Bgee; ENSMUSG00000036599; Expressed in granulocyte and 212 other tissues.
DR ExpressionAtlas; Q99LL3; baseline and differential.
DR Genevisible; Q99LL3; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047756; F:chondroitin 4-sulfotransferase activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0030208; P:dermatan sulfate biosynthetic process; ISS: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..419
FT /note="Carbohydrate sulfotransferase 12"
FT /id="PRO_0000189669"
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..419
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 78..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..182
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 250..258
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 91
FT /note="V -> A (in Ref. 1; CAB92140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 49398 MW; 3F5339D4EE1DE7BF CRC64;
MTKPRLFRLW LVLGSALMIL LIIVYWDNVG TAHFYLHTSL SRPHILEPLP TQGLVEENVF
TSDVDEFLDT LLSSDAKHND LSRRKTEQPP VPAPSKPVLS HMEENVRGYD WSTHDAHQNP
DRDRQQAERR SLLRDFCANA SLAFPTKDRS FDDIPNYELN HLIVDDRHGV IYCYVPKVAC
TNWKRVMIVL SESLLDRGSP YRDPLDIPRE HVHNTSTHLT FNKFWRRYGK FSRHLMKVKL
KKYTKFLFVR DPFVRLISAF RSKFELENEE FYRKFAVPML RLYANHTSLP ASVSEAFSAG
LKVSFANFIQ YLLDPHTEKL APFNEHWRQV YRLCHPCQID YDFVGKLETL DEDAAQLLRF
LKVDSQLHFP PSYRNRTASS WEEDWFANIP LAWRQQLYKL YEADFVLFGY PKPENLLRD
