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CHSTF_MOUSE
ID   CHSTF_MOUSE             Reviewed;         561 AA.
AC   Q91XQ5; Q80TW4; Q8BLQ5; Q9D2N6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Carbohydrate sulfotransferase 15;
DE            EC=2.8.2.33;
DE   AltName: Full=B-cell RAG-associated gene protein;
DE   AltName: Full=N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase;
DE            Short=GalNAc4S-6ST;
GN   Name=Chst15; Synonyms=Brag, Galnac4s6st, Kiaa0598;
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].
RX   PubMed=9754571;
RX   DOI=10.1002/(sici)1521-4141(199809)28:09<2839::aid-immu2839>3.0.co;2-6;
RA   Verkoczy L.K., Marsden P.A., Berinstein N.L.;
RT   "hBRAG, a novel B cell lineage cDNA encoding a type II transmembrane
RT   glycoprotein potentially involved in the regulation of recombination
RT   activating gene 1 (RAG1).";
RL   Eur. J. Immunol. 28:2839-2853(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ohtake S., Morisaki T., Kondo S., Matsumura K., Kimata K., Habuchi O.;
RT   "Characterization of GalNAc 4-sulfate 6-O-sulfotransferase expressed in
RT   bone marrow derived mast cells synthesizing chondroitin sulfate E.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Cerebellum, Skin, and Urinary bladder;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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 transfers sulfate from 3'-
CC       phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of
CC       the GalNAc 4-sulfate residue of chondroitin sulfate A and forms
CC       chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating
CC       units. It also transfers sulfate to a unique non-reducing terminal
CC       sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly
CC       sulfated structure similar to the structure found in thrombomodulin
CC       chondroitin sulfate. May also act as a B-cell receptor involved in BCR
CC       ligation-mediated early activation that mediate regulatory signals key
CC       to B-cell development and/or regulation of B-cell-specific RAG
CC       expression; however such results are unclear in vivo (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=n 3'-phosphoadenylyl sulfate + dermatan 4'-sulfate = n
CC         adenosine 3',5'-bisphosphate + dermatan 4',6'-bissulfate + n H(+);
CC         Xref=Rhea:RHEA:54304, Rhea:RHEA-COMP:9965, Rhea:RHEA-COMP:13850,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC         ChEBI:CHEBI:58465, ChEBI:CHEBI:138121; EC=2.8.2.33;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=n 3'-phosphoadenylyl sulfate + chondroitin 4'-sulfate = n
CC         adenosine 3',5'-bisphosphate + chondroitin 4',6'-bissulfate + n H(+);
CC         Xref=Rhea:RHEA:54300, Rhea:RHEA-COMP:9829, Rhea:RHEA-COMP:13849,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC         ChEBI:CHEBI:58422, ChEBI:CHEBI:138112; EC=2.8.2.33;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by phenyl beta-GalNAc(4,6-SO(4)).
CC   -!- SUBUNIT: Homodimer; disulfide-linked (Potential). The relevance of
CC       homodimerization is however unsure. May interact with phosphorylated
CC       proteins in resting B-cells, including HCK (By similarity).
CC       {ECO:0000250, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}. Note=A small fraction may
CC       also be present at the cell surface, where it acts as a B-cell
CC       receptor.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65606.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF320786; AAK69604.1; -; mRNA.
DR   EMBL; AB187269; BAD89559.1; -; mRNA.
DR   EMBL; AK122324; BAC65606.1; ALT_INIT; mRNA.
DR   EMBL; AK019474; BAB31743.1; -; mRNA.
DR   EMBL; AK035637; BAC29133.1; -; mRNA.
DR   EMBL; AK043803; BAC31658.1; -; mRNA.
DR   EMBL; AK082318; BAC38463.1; -; mRNA.
DR   EMBL; AK083614; BAC38968.1; -; mRNA.
DR   EMBL; BC031443; AAH31443.1; -; mRNA.
DR   CCDS; CCDS21922.1; -.
DR   RefSeq; NP_084211.2; NM_029935.5.
DR   RefSeq; XP_006508395.1; XM_006508332.1.
DR   RefSeq; XP_006508396.1; XM_006508333.3.
DR   RefSeq; XP_017167875.1; XM_017312386.1.
DR   AlphaFoldDB; Q91XQ5; -.
DR   STRING; 10090.ENSMUSP00000079105; -.
DR   GlyGen; Q91XQ5; 1 site.
DR   iPTMnet; Q91XQ5; -.
DR   PhosphoSitePlus; Q91XQ5; -.
DR   MaxQB; Q91XQ5; -.
DR   PaxDb; Q91XQ5; -.
DR   PRIDE; Q91XQ5; -.
DR   ProteomicsDB; 281681; -.
DR   Antibodypedia; 2663; 72 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000077472; ENSMUSP00000076682; ENSMUSG00000030930.
DR   Ensembl; ENSMUST00000080215; ENSMUSP00000079105; ENSMUSG00000030930.
DR   GeneID; 77590; -.
DR   KEGG; mmu:77590; -.
DR   UCSC; uc009kbx.1; mouse.
DR   CTD; 51363; -.
DR   MGI; MGI:1924840; Chst15.
DR   VEuPathDB; HostDB:ENSMUSG00000030930; -.
DR   eggNOG; ENOG502QU6N; Eukaryota.
DR   GeneTree; ENSGT00390000004719; -.
DR   HOGENOM; CLU_017703_2_1_1; -.
DR   InParanoid; Q91XQ5; -.
DR   OMA; KYTMHMV; -.
DR   OrthoDB; 356648at2759; -.
DR   PhylomeDB; Q91XQ5; -.
DR   TreeFam; TF333516; -.
DR   BRENDA; 2.8.2.33; 3474.
DR   Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR   BioGRID-ORCS; 77590; 2 hits in 72 CRISPR screens.
DR   PRO; PR:Q91XQ5; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q91XQ5; protein.
DR   Bgee; ENSMUSG00000030930; Expressed in epithelium of cochlear duct and 281 other tissues.
DR   Genevisible; Q91XQ5; 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:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; ISS:UniProtKB.
DR   GO; GO:0050659; F:N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity; ISS:UniProtKB.
DR   GO; GO:0019319; P:hexose biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..561
FT                   /note="Carbohydrate sulfotransferase 15"
FT                   /id="PRO_0000225624"
FT   TOPO_DOM        1..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..561
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   BINDING         263..267
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         400
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        115
FT                   /note="G -> S (in Ref. 4; BAB31743)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535
FT                   /note="I -> V (in Ref. 4; BAC31658)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   561 AA;  64986 MW;  E00ADD0584559278 CRC64;
     MRHCINCCVQ LFPEDTHKQQ VACQGGPHHS HQACPTCKGE NKILFRVDSK QMNLLAVLEV
     RTEGNENWGG FLRFRKGKRC SLVFGLIIMT LVMASYILSG AHQELLISSP FHYGGFPSNP
     SVMDGENPSD VKEHHYQPSV NNISYVKDYP SIKLIIDSIA ARIEFTTRQL PDLQDLKRQE
     LHMFSVIPSK FLPTSKSPCW YEEFSGRNTT DPYLTNSYVL YSKRFRSTFD ALRKVFWGHL
     SHVQGKHFRL RCLPHFYIIG QPKCGTTDLY DRLRLHPEVK FSAIKEPHWW TRKRFGIVRL
     RDGLRDRYPV EDYLDLFDLA AHQIHQGLQA ASAEQPSKMN KIIIGEASAS TMWDNNAWTF
     FYDNSTDGEP PFLTQDFIHA FQPEAKLIVM LRDPVERLYS DYLYFASSNK SADDFHEKVT
     EALQLFENCM LDYSLRACVY NNTLNNAMPV RLQVGLYAVY LLDWLTVFSK EQFLILRLED
     HASNVKYTMH KVFQFLNLGP LSEKQEALMT KSPASNTRRP EDRSLGPMWP ITQKILREFY
     GPFNTRLAQV LDDEAFAWKT T
 
 
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