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HS3S2_RAT
ID   HS3S2_RAT               Reviewed;         367 AA.
AC   Q80W66; A1A5M1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 2;
DE            EC=2.8.2.29 {ECO:0000250|UniProtKB:Q9Y278};
DE   AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2;
DE            Short=Heparan sulfate 3-O-sulfotransferase 2;
GN   Name=Hs3st2; Synonyms=3ost2;
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 [MRNA], FUNCTION IN CIRCADIAN PHYSIOLOGY, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=12601002; DOI=10.1074/jbc.m300828200;
RA   Borjigin J., Deng J., Sun X., De Jesus M., Liu T., Wang M.M.;
RT   "Diurnal pineal 3-O-sulphotransferase 2 expression controlled by beta-
RT   adrenergic repression.";
RL   J. Biol. Chem. 278:16315-16319(2003).
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 utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted
CC       glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan
CC       sulfate. Catalyzes the O-sulfation of glucosamine in GlcA2S-GlcNS.
CC       Unlike HS3ST1/3-OST-1, does not convert non-anticoagulant heparan
CC       sulfate to anticoagulant heparan sulfate (By similarity). May
CC       contribute to the pineal circadian physiology (PubMed:12601002).
CC       {ECO:0000250|UniProtKB:Q9Y278, ECO:0000269|PubMed:12601002}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC         sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC         adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:15461, Rhea:RHEA-
CC         COMP:9830, Rhea:RHEA-COMP:9831, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:70975; EC=2.8.2.29;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y278};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain, in the pineal gland
CC       specifically during the daylight hours, and weakly in the olfactory
CC       bulb and pineal gland during the night. First detected between
CC       postnatal days 5 and 10. {ECO:0000269|PubMed:12601002}.
CC   -!- INDUCTION: Activated by light stimulation at night through the
CC       suppression of beta-adrenergic signaling.
CC       {ECO:0000269|PubMed:12601002}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; AY240873; AAP30887.1; -; mRNA.
DR   EMBL; BC128721; AAI28722.1; -; mRNA.
DR   RefSeq; NP_852035.1; NM_181370.2.
DR   AlphaFoldDB; Q80W66; -.
DR   SMR; Q80W66; -.
DR   STRING; 10116.ENSRNOP00000023773; -.
DR   GlyGen; Q80W66; 4 sites.
DR   iPTMnet; Q80W66; -.
DR   PhosphoSitePlus; Q80W66; -.
DR   PaxDb; Q80W66; -.
DR   Ensembl; ENSRNOT00000023773; ENSRNOP00000023773; ENSRNOG00000017659.
DR   GeneID; 293451; -.
DR   KEGG; rno:293451; -.
DR   UCSC; RGD:727787; rat.
DR   CTD; 9956; -.
DR   RGD; 727787; Hs3st2.
DR   eggNOG; KOG3704; Eukaryota.
DR   GeneTree; ENSGT00940000160498; -.
DR   HOGENOM; CLU_017703_0_1_1; -.
DR   InParanoid; Q80W66; -.
DR   OMA; NIIFYRG; -.
DR   OrthoDB; 712400at2759; -.
DR   PhylomeDB; Q80W66; -.
DR   TreeFam; TF350755; -.
DR   Reactome; R-RNO-2022928; HS-GAG biosynthesis.
DR   PRO; PR:Q80W66; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000017659; Expressed in frontal cortex and 4 other tissues.
DR   Genevisible; Q80W66; RN.
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:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; ISS:UniProtKB.
DR   GO; GO:0033871; F:[heparan sulfate]-glucosamine 3-sulfotransferase 2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0007623; P:circadian rhythm; IDA:RGD.
DR   GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR037359; NST/OST.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR10605; PTHR10605; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="Heparan sulfate glucosamine 3-O-sulfotransferase 2"
FT                   /id="PRO_0000085216"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..39
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..367
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          66..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..90
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         124..128
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT   BINDING         146..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT   BINDING         177..180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT   BINDING         205
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT   BINDING         213
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT   BINDING         245..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT   BINDING         330..334
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        313..325
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y663"
SQ   SEQUENCE   367 AA;  41378 MW;  774E8E32C1C4588D CRC64;
     MAYRVLGRAG PPQPRRARRL LFAFTLSLSC TYLCYSFLCC CDGLGQSRLL GAPRCLRGPS
     ASGQKLLAKS RPCDPPGPTP SEPSAPSAPA AAAPAPRLSG SNHSGSPKPG TKRLPQALIV
     GVKKGGTRAV LEFIRVHPDV RALGTEPHFF DRNYGRGLDW YRSLMPRTLE TQITLEKTPS
     YFVTQEAPRR IFNMSRDTKL IVVVRNPVTR AISDYTQTLS KKPDIPTFEG LSFRNRSLGL
     VDVSWNAIRI GMYALHLESW LRYFPLAQIH FVSGERLITD PAGEMGRIQD FLGIKRFITD
     KHFYFNKTKG FPCLKKPEST LLPRCLGKSK GRTHVQIDPE VIDQLREFYR PYNIKFYETV
     GQDFRWE
 
 
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