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CP18A_DROME
ID   CP18A_DROME             Reviewed;         538 AA.
AC   Q95078; A5AC86; A5AC96; Q0KHQ8; Q27767; Q9VWR4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Cytochrome P450 18a1;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPXVIIIA1;
GN   Name=Cyp18a1; Synonyms=CYP18, Eig17-1; ORFNames=CG6816;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Larva;
RX   PubMed=9256362; DOI=10.1016/s0303-7207(97)00093-2;
RA   Bassett M.H., McCarthy J.L., Waterman M.R., Sliter T.J.;
RT   "Sequence and developmental expression of Cyp18, a member of a new
RT   cytochrome P450 family from Drosophila.";
RL   Mol. Cell. Endocrinol. 131:39-49(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-530.
RC   STRAIN=CN10X, CN11X, CN13X, CN15X, CN16X, CN17X, CN19X, CN21X, CN22BX,
RC   CN3X, and CN7X;
RX   PubMed=17322555; DOI=10.1093/molbev/msm032;
RA   Orengo D.J., Aguade M.;
RT   "Genome scans of variation and adaptive change: extended analysis of a
RT   candidate locus close to the phantom gene region in Drosophila
RT   melanogaster.";
RL   Mol. Biol. Evol. 24:1122-1129(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 459-479.
RC   STRAIN=Canton-S;
RX   PubMed=8413299; DOI=10.1128/mcb.13.11.7101-7111.1993;
RA   Hurban P., Thummel C.S.;
RT   "Isolation and characterization of fifteen ecdysone-inducible Drosophila
RT   genes reveal unexpected complexities in ecdysone regulation.";
RL   Mol. Cell. Biol. 13:7101-7111(1993).
CC   -!- FUNCTION: Probably involved in steroid hormones biosynthesis.
CC       {ECO:0000269|PubMed:9256362}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in body wall (epidermal and muscle cells)
CC       and mid- and hind-gut. {ECO:0000269|PubMed:9256362}.
CC   -!- DEVELOPMENTAL STAGE: Low levels throughout postembryonic development.
CC   -!- INDUCTION: By 20-hydroxyecdysone during the three larval stages, at
CC       pupariation and in pupae. {ECO:0000269|PubMed:9256362}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U44753; AAB69750.1; -; mRNA.
DR   EMBL; AM411848; CAL69930.1; -; Genomic_DNA.
DR   EMBL; AM411849; CAL69932.1; -; Genomic_DNA.
DR   EMBL; AM411850; CAL69934.1; -; Genomic_DNA.
DR   EMBL; AM411851; CAL69936.1; -; Genomic_DNA.
DR   EMBL; AM411852; CAL69938.1; -; Genomic_DNA.
DR   EMBL; AM411853; CAL69940.1; -; Genomic_DNA.
DR   EMBL; AM411854; CAL69942.1; -; Genomic_DNA.
DR   EMBL; AM411855; CAL69944.1; -; Genomic_DNA.
DR   EMBL; AM411856; CAL69946.1; -; Genomic_DNA.
DR   EMBL; AM411857; CAL69948.1; -; Genomic_DNA.
DR   EMBL; AM411858; CAL69950.1; -; Genomic_DNA.
DR   EMBL; AM411859; CAL69952.1; -; Genomic_DNA.
DR   EMBL; AM411860; CAL69954.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAN09473.1; -; Genomic_DNA.
DR   EMBL; S66112; AAB28524.1; -; mRNA.
DR   RefSeq; NP_523403.2; NM_078679.3.
DR   RefSeq; NP_728191.1; NM_167628.2.
DR   AlphaFoldDB; Q95078; -.
DR   SMR; Q95078; -.
DR   BioGRID; 59170; 2.
DR   STRING; 7227.FBpp0074381; -.
DR   PaxDb; Q95078; -.
DR   EnsemblMetazoa; FBtr0074609; FBpp0074380; FBgn0010383.
DR   EnsemblMetazoa; FBtr0074610; FBpp0074381; FBgn0010383.
DR   GeneID; 32858; -.
DR   KEGG; dme:Dmel_CG6816; -.
DR   CTD; 32858; -.
DR   FlyBase; FBgn0010383; Cyp18a1.
DR   VEuPathDB; VectorBase:FBgn0010383; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000167749; -.
DR   HOGENOM; CLU_001570_22_0_1; -.
DR   InParanoid; Q95078; -.
DR   OMA; FDGKNHE; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; Q95078; -.
DR   BioCyc; MetaCyc:MON-18164; -.
DR   Reactome; R-DME-196791; Vitamin D (calciferol) metabolism.
DR   Reactome; R-DME-211916; Vitamins.
DR   Reactome; R-DME-211958; Miscellaneous substrates.
DR   Reactome; R-DME-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR   BioGRID-ORCS; 32858; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32858; -.
DR   PRO; PR:Q95078; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0010383; Expressed in capitellum (Drosophila) and 45 other tissues.
DR   Genevisible; Q95078; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IDA:FlyBase.
DR   GO; GO:0007304; P:chorion-containing eggshell formation; IMP:FlyBase.
DR   GO; GO:0046344; P:ecdysteroid catabolic process; IMP:FlyBase.
DR   GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR   GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
DR   GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0035210; P:prepupal development; IMP:FlyBase.
DR   GO; GO:0035074; P:pupation; IMP:FlyBase.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..538
FT                   /note="Cytochrome P450 18a1"
FT                   /id="PRO_0000051949"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         466
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   VARIANT         530
FT                   /note="H -> Y (in strain: CN15X)"
FT                   /evidence="ECO:0000269|PubMed:17322555"
FT   CONFLICT        19
FT                   /note="Q -> E (in Ref. 1; AAB69750)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        478..479
FT                   /note="LF -> PV (in Ref. 5; AAB28524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520
FT                   /note="R -> S (in Ref. 1; AAB69750)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   538 AA;  61949 MW;  A1C95E74505C28CE CRC64;
     MLADSYLIKF VLRQLQVQQD GDAQHLLMVF LGLLALVTLL QWLVRNYREL RKLPPGPWGL
     PVIGYLLFMG SEKHTRFMEL AKQYGSLFST RLGSQLTVVM SDYKMIRECF RREEFTGRPD
     TPFMQTLNGY GIINSTGKLW KDQRRFLHDK LRQFGMTYMG NGKQQMQKRI MTEVHEFIGH
     LHASDGQPVD MSPVISVAVS NVICSLMMST RFSIDDPKFR RFNFLIEEGM RLFGEIHTVD
     YIPTMQCFPS ISTAKNKIAQ NRAEMQRFYQ DVIDDHKRSF DPNNIRDLVD FYLCEIEKAK
     AEGTDAELFD GKNHEEQLVQ VIIDLFSAGM ETIKTTLLWI NVFMLRNPKE MRRVQDELDQ
     VVGRHRLPTI EDLQYLPITE STILESMRRS SIVPLATTHS PTRDVELNGY TIPAGSHVIP
     LINSVHMDPN LWEKPEEFRP SRFIDTEGKV RKPEYFIPFG VGRRMCLGDV LARMELFLFF
     ASFMHCFDIA LPEGQPLPSL KGNVGATITP ESFKVCLKRR PLGPTAADPH HMRNVGAN
 
 
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