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3BHS7_RAT
ID   3BHS7_RAT               Reviewed;         338 AA.
AC   O35048;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=3 beta-hydroxysteroid dehydrogenase type 7 {ECO:0000305};
DE   AltName: Full=3 beta-hydroxysteroid dehydrogenase type VII;
DE            Short=3-beta-HSD VII;
DE   AltName: Full=3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase;
DE            Short=C(27) 3-beta-HSD;
DE            EC=1.1.1.-;
DE   AltName: Full=Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase;
DE            EC=1.1.1.181 {ECO:0000250|UniProtKB:Q9H2F3};
DE   AltName: Full=Confluent 3Y1 cell-associated 2;
GN   Name=Hsd3b7 {ECO:0000312|RGD:628727};
GN   Synonyms=Cca2 {ECO:0000312|EMBL:BAA22931.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAA22931.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=9199244; DOI=10.1016/s0167-4781(97)00051-1;
RA   Hayashi Y., Kiyono T., Fujita M., Ishibashi M.;
RT   "Isolation of a novel cDNA whose corresponding mRNA is accumulated in
RT   growth-arrested confluent but not in growing sub-confluent rat 3Y1 cells.";
RL   Biochim. Biophys. Acta 1352:145-150(1997).
CC   -!- FUNCTION: The 3-beta-HSD enzymatic system plays a crucial role in the
CC       biosynthesis of all classes of hormonal steroids. HSD VII is active
CC       against four 7-alpha-hydroxylated sterols. Does not metabolize several
CC       different C(19/21) steroids as substrates. Involved in bile acid
CC       synthesis. Plays a key role in cell positioning and movement in
CC       lymphoid tissues by mediating degradation of 7-alpha,25-
CC       dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand
CC       for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor
CC       for a number of lymphoid cells. {ECO:0000250|UniProtKB:Q9EQC1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7alpha-hydroxycholesterol + NAD(+) = 7alpha-hydroxycholest-4-
CC         en-3-one + H(+) + NADH; Xref=Rhea:RHEA:11896, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17500, ChEBI:CHEBI:17899, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.181;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2F3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11897;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2F3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7alpha,25-dihydroxycholesterol + NAD(+) = 7alpha,25-dihydroxy-
CC         4-cholesten-3-one + H(+) + NADH; Xref=Rhea:RHEA:47156,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:37623, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:81013;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2F3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47157;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2F3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25R)-cholest-5-en-3beta,7alpha,26-triol + NAD(+) = (25R)-
CC         7alpha,26-dihydroxycholest-4-en-3-one + H(+) + NADH;
CC         Xref=Rhea:RHEA:47180, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:76592, ChEBI:CHEBI:87476;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2F3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47181;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2F3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(24S)-7alpha-dihydroxycholesterol + NAD(+) = (24S)-7alpha,24-
CC         dihydroxycholest-4-en-3-one + H(+) + NADH; Xref=Rhea:RHEA:47200,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:37640, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:63838;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2F3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47201;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2F3};
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: High levels in liver and lung, moderate levels in
CC       spleen, brain, heart, kidney, jejunum and testis. Up-regulated in 3Y1
CC       cells upon growth arrest. {ECO:0000269|PubMed:9199244}.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR   EMBL; AB000199; BAA22931.1; -; mRNA.
DR   RefSeq; NP_647545.1; NM_139329.1.
DR   AlphaFoldDB; O35048; -.
DR   SMR; O35048; -.
DR   STRING; 10116.ENSRNOP00000025933; -.
DR   iPTMnet; O35048; -.
DR   PhosphoSitePlus; O35048; -.
DR   PaxDb; O35048; -.
DR   GeneID; 246211; -.
DR   KEGG; rno:246211; -.
DR   UCSC; RGD:628727; rat.
DR   CTD; 80270; -.
DR   RGD; 628727; Hsd3b7.
DR   eggNOG; KOG1430; Eukaryota.
DR   InParanoid; O35048; -.
DR   Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR   Reactome; R-RNO-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR   Reactome; R-RNO-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR   UniPathway; UPA00062; -.
DR   PRO; PR:O35048; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0047016; F:cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity; IDA:RGD.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0035754; P:B cell chemotaxis; ISS:UniProtKB.
DR   GO; GO:0008206; P:bile acid metabolic process; TAS:RGD.
DR   GO; GO:0006707; P:cholesterol catabolic process; IDA:RGD.
DR   GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR   GO; GO:0001558; P:regulation of cell growth; IDA:RGD.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid metabolism; Membrane; NAD; Oxidoreductase;
KW   Reference proteome; Steroidogenesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..338
FT                   /note="3 beta-hydroxysteroid dehydrogenase type 7"
FT                   /id="PRO_0000248461"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  37781 MW;  72FC828235D0BFD5 CRC64;
     MADSAQVPAL VYLVTGGCGF LGEHIVRMLL EWEPRLRELR VFDLHLSSWL EELKTGPVQV
     TAIQGDVTQA HEVAAAMAGS HVVIHTAGLV DVFGKASPET IHKVNVQGTQ NVIDACVQTG
     TRLLVYTSSM EVVGPNVKGH PFYRGNEDTP YEAIHRHPYP CSKALAEQLV LEANGRKGLR
     FGGRLFRAIP ASVEHGRVYV GNVAWMHILV ARELEQRAAL MGGQVYFCYD KSPYKSYEDF
     NMEFLSPCGL RLIGTHPLLP YWLLVLLTAL NALLQWLLRP LVLYTPLLNP YTLAVANTTF
     TVSTNKAQRH FGYKPLFSWE ESRARTIHWV QAMEGSAW
 
 
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