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EBP_DICDI
ID   EBP_DICDI               Reviewed;         219 AA.
AC   Q55E32;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase;
DE            EC=5.3.3.5;
DE   AltName: Full=Cholestenol Delta-isomerase;
DE   AltName: Full=Delta(8)-Delta(7) sterol isomerase;
DE            Short=D8-D7 sterol isomerase;
DE   AltName: Full=Emopamil-binding protein homolog;
GN   Name=ebp; ORFNames=DDB_G0269414;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their
CC       corresponding Delta(7)-isomers. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lathosterol = 5alpha-cholest-8-en-3beta-ol;
CC         Xref=Rhea:RHEA:15281, ChEBI:CHEBI:16608, ChEBI:CHEBI:17168;
CC         EC=5.3.3.5; Evidence={ECO:0000250|UniProtKB:Q15125};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15282;
CC         Evidence={ECO:0000250|UniProtKB:Q15125};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=zymosterol = 5alpha-cholesta-7,24-dien-3beta-ol;
CC         Xref=Rhea:RHEA:33999, ChEBI:CHEBI:16290, ChEBI:CHEBI:18252;
CC         Evidence={ECO:0000250|UniProtKB:Q15125};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34000;
CC         Evidence={ECO:0000250|UniProtKB:Q15125};
CC   -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EBP family. {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72057.1; -; Genomic_DNA.
DR   RefSeq; XP_645949.1; XM_640857.1.
DR   AlphaFoldDB; Q55E32; -.
DR   SMR; Q55E32; -.
DR   STRING; 44689.DDB0267002; -.
DR   PaxDb; Q55E32; -.
DR   EnsemblProtists; EAL72057; EAL72057; DDB_G0269414.
DR   GeneID; 8616893; -.
DR   KEGG; ddi:DDB_G0269414; -.
DR   dictyBase; DDB_G0269414; ebp.
DR   eggNOG; KOG4826; Eukaryota.
DR   HOGENOM; CLU_1263547_0_0_1; -.
DR   InParanoid; Q55E32; -.
DR   OMA; FEGYFAY; -.
DR   PhylomeDB; Q55E32; -.
DR   Reactome; R-DDI-6807047; Cholesterol biosynthesis via desmosterol.
DR   Reactome; R-DDI-6807062; Cholesterol biosynthesis via lathosterol.
DR   UniPathway; UPA00063; -.
DR   PRO; PR:Q55E32; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0000247; F:C-8 sterol isomerase activity; ISS:UniProtKB.
DR   GO; GO:0047750; F:cholestenol delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; IBA:GO_Central.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0016126; P:sterol biosynthetic process; ISS:dictyBase.
DR   InterPro; IPR007905; EBP.
DR   InterPro; IPR033118; EXPERA.
DR   PANTHER; PTHR14207; PTHR14207; 1.
DR   PROSITE; PS51751; EXPERA; 1.
PE   2: Evidence at transcript level;
KW   Cholesterol biosynthesis; Cholesterol metabolism; Endoplasmic reticulum;
KW   Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..219
FT                   /note="Probable 3-beta-hydroxysteroid-Delta(8),Delta(7)-
FT                   isomerase"
FT                   /id="PRO_0000331293"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..188
FT                   /note="EXPERA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01087"
SQ   SEQUENCE   219 AA;  25195 MW;  86DA1F19D2AEB6FC CRC64;
     MEIFAFVPLA VLTALCVVIS LFVKREKLVV FWLLWSGLIH IILEGSYGFF AHEVTKASTV
     SFTEKMLELV PLENAWNPHW YAQLYSQYAK YDLRYAIQDP MVVFFCFLEL VQGAACFLLV
     ICVIKQARIR HALQIFLCSI QGLGTVFYFI TPYIYGLWEQ QISSDPFELW VYVVGLNGLW
     LLVPIILTIQ SFIAINKQFS IVESTTKDAK FISRKPKTA
 
 
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