CHSTB_RAT
ID CHSTB_RAT Reviewed; 352 AA.
AC P69478;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Carbohydrate sulfotransferase 11;
DE EC=2.8.2.5;
DE AltName: Full=Chondroitin 4-O-sulfotransferase 1;
DE AltName: Full=Chondroitin 4-sulfotransferase 1;
DE Short=C4S-1;
DE Short=C4ST-1;
DE Short=C4ST1;
GN Name=Chst11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PROTEIN SEQUENCE OF 59-66; 163-171; 187-197; 274-278 AND 285-300.
RX PubMed=10722746; DOI=10.1074/jbc.275.12.8975;
RA Yamauchi S., Mita S., Matsubara T., Fukuta M., Habuchi H., Kimata K.,
RA Habuchi O.;
RT "Molecular cloning and expression of chondroitin 4-sulfotransferase.";
RL J. Biol. Chem. 275:8975-8981(2000).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-
CC acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin
CC sulfate constitutes the predominant proteoglycan present in cartilage
CC and is distributed on the surfaces of many cells and extracellular
CC matrices. Can also sulfate Gal residues in desulfated dermatan sulfate.
CC Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit.
CC Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is
CC used as an acceptor (By 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 -!- PTM: N-glycosylated; required for activity and stability.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; AABR03057909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03059893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03062052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03060128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03059314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03056595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03057359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03059499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03056571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03061700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03056958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001101549.1; NM_001108079.1.
DR RefSeq; XP_017450314.1; XM_017594825.1.
DR AlphaFoldDB; P69478; -.
DR STRING; 10116.ENSRNOP00000012017; -.
DR GlyGen; P69478; 4 sites.
DR PaxDb; P69478; -.
DR PRIDE; P69478; -.
DR GeneID; 314694; -.
DR KEGG; rno:314694; -.
DR UCSC; RGD:1308400; rat.
DR CTD; 50515; -.
DR RGD; 1308400; Chst11.
DR VEuPathDB; HostDB:ENSRNOG00000008885; -.
DR eggNOG; KOG4651; Eukaryota.
DR HOGENOM; CLU_043398_1_1_1; -.
DR InParanoid; P69478; -.
DR OMA; KMDFLMF; -.
DR OrthoDB; 1330889at2759; -.
DR PhylomeDB; P69478; -.
DR TreeFam; TF325581; -.
DR BRENDA; 2.8.2.5; 5301.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR SABIO-RK; P69478; -.
DR PRO; PR:P69478; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000008885; Expressed in ovary and 18 other tissues.
DR ExpressionAtlas; P69478; baseline and differential.
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; ISO:RGD.
DR GO; GO:0001537; F:N-acetylgalactosamine 4-O-sulfotransferase activity; ISO:RGD.
DR GO; GO:0050659; F:N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity; ISO:RGD.
DR GO; GO:0008146; F:sulfotransferase activity; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0002063; P:chondrocyte development; ISO:RGD.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; ISO:RGD.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0033037; P:polysaccharide localization; ISO:RGD.
DR GO; GO:0036342; P:post-anal tail morphogenesis; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR InterPro; IPR018011; Carb_sulfotrans_8-10.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12137; PTHR12137; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..352
FT /note="Carbohydrate sulfotransferase 11"
FT /id="PRO_0000189666"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..352
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 124..130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 186..194
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CONFLICT 277
FT /note="G -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 41626 MW; 3A693D10430A2EA4 CRC64;
MKPALLEVMR MNRICRMVLA TCLGSFILVI FYFQSMLHPV MRRNPFGVDI CCRKGSRSPL
QELYNPIQLE LSNTAILHQM RRDQVTDTCR ANSAMSRKRR VLTPNDLKHL VVDEDHELIY
CYVPKVACTN WKRLMMVLSG RGKYSDPMEI PANEAHVSAN LKTLNQYSIP EINHRLKSYM
KFLFVREPFE RLVSAYRNKF TQKYNTSFHK RYGTKIIRRQ RKNATQEALR KGDDVKFEEF
VAYLIDPHTQ REEPFNEHWQ TVYSLCHPCH IHYDLVGKYE TLEEDSNYVL RLAGVSGYLK
FPTYAKSTRT TDEMTTEFFQ NISAEHQTQL YEVYKLDFLM FNYSVPNYLK LD
