UST_MOUSE
ID UST_MOUSE Reviewed; 407 AA.
AC Q8BUB6; B2RR02;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Uronyl 2-sulfotransferase;
DE EC=2.8.2.-;
GN Name=Ust;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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: Sulfotransferase that catalyzes the transfer of sulfate to
CC the position 2 of uronyl residues. Has mainly activity toward iduronyl
CC residues in dermatan sulfate, and weaker activity toward glucuronyl
CC residues of chondroitin sulfate. Has no activity toward desulfated N-
CC resulfated heparin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39625.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK086181; BAC39625.1; ALT_FRAME; mRNA.
DR EMBL; BC138155; AAI38156.1; -; mRNA.
DR CCDS; CCDS35835.1; -.
DR RefSeq; NP_796361.2; NM_177387.3.
DR AlphaFoldDB; Q8BUB6; -.
DR SMR; Q8BUB6; -.
DR STRING; 10090.ENSMUSP00000052017; -.
DR GlyGen; Q8BUB6; 5 sites.
DR PhosphoSitePlus; Q8BUB6; -.
DR PaxDb; Q8BUB6; -.
DR PRIDE; Q8BUB6; -.
DR ProteomicsDB; 297902; -.
DR Antibodypedia; 33260; 170 antibodies from 19 providers.
DR DNASU; 338362; -.
DR Ensembl; ENSMUST00000061601; ENSMUSP00000052017; ENSMUSG00000047712.
DR GeneID; 338362; -.
DR KEGG; mmu:338362; -.
DR UCSC; uc007eit.1; mouse.
DR CTD; 10090; -.
DR MGI; MGI:2442406; Ust.
DR VEuPathDB; HostDB:ENSMUSG00000047712; -.
DR eggNOG; KOG3922; Eukaryota.
DR GeneTree; ENSGT00530000063408; -.
DR HOGENOM; CLU_056190_0_0_1; -.
DR InParanoid; Q8BUB6; -.
DR OMA; YHYVREQ; -.
DR OrthoDB; 877221at2759; -.
DR PhylomeDB; Q8BUB6; -.
DR TreeFam; TF315238; -.
DR Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR BioGRID-ORCS; 338362; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Ust; mouse.
DR PRO; PR:Q8BUB6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BUB6; protein.
DR Bgee; ENSMUSG00000047712; Expressed in dentate gyrus of hippocampal formation granule cell and 166 other tissues.
DR Genevisible; Q8BUB6; 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:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:MGI.
DR GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007734; Heparan_SO4_2-O-STrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12129; PTHR12129; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..407
FT /note="Uronyl 2-sulfotransferase"
FT /id="PRO_0000207682"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..407
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 57
FT /note="L -> V (in Ref. 1; BAC39625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 47730 MW; 5DE77416709B9DC6 CRC64;
MKKKQQQHPG GGTDPWPHGA PVGGAPPCLG SCKRRIPLLP FLRFSLRDYG FCMATLLVFC
LGSLFYQLSG GPPRFLLDLR QYLGNSTYLD DHGPPPSKVL PFPSQVVYNR VGKCGSRTVV
LLLRILSEKH GFNLVTSDIH NKTRLTKNEQ MELIKNISTA EQPYLFTRHV HFLNFSRFGG
DQPVYINIIR DPVSRFLSNY FFRRFGDWRG EQNHMIRTPS MRQEERYLDI NECILENYPE
CSNPRLFYII PYFCGQHPRC REPGEWALER AKLNVNENFL LVGILEELED VLLLLERFLP
HYFKGVLSIY KDPEHRKLGN MTVTVRKTVP SPEAVQILYQ RMRYEYEFYH YVREQFHLLK
RKLGLKSRVS GPPVRPQFFI PTPLETEEPI DDEEQDDEKW LEDIYKR
