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SIMA_DROME
ID   SIMA_DROME              Reviewed;        1507 AA.
AC   Q24167; Q9VAA5;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=Protein similar;
GN   Name=sima; ORFNames=CG45051;
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], AND TISSUE SPECIFICITY.
RX   PubMed=8682312; DOI=10.1016/0378-1119(96)00060-1;
RA   Nambu J.R., Chen W., Hu S., Crews S.T.;
RT   "The Drosophila melanogaster similar bHLH-PAS gene encodes a protein
RT   related to human hypoxia-inducible factor 1 alpha and Drosophila single-
RT   minded.";
RL   Gene 172:249-254(1996).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=9731218; DOI=10.1006/bbrc.1998.9234;
RA   Bacon N.C., Wappner P., O'Rourke J.F., Bartlett S.M., Shilo B., Pugh C.W.,
RA   Ratcliffe P.J.;
RT   "Regulation of the Drosophila bHLH-PAS protein Sima by hypoxia: functional
RT   evidence for homology with mammalian HIF-1 alpha.";
RL   Biochem. Biophys. Res. Commun. 249:811-816(1998).
RN   [5]
RP   INTERACTION WITH VHL.
RX   PubMed=11006129; DOI=10.1006/bbrc.2000.3451;
RA   Aso T., Yamazaki K., Aigaki T., Kitajima S.;
RT   "Drosophila von Hippel-Lindau tumor suppressor complex possesses E3
RT   ubiquitin ligase activity.";
RL   Biochem. Biophys. Res. Commun. 276:355-361(2000).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND ODD DOMAIN.
RX   PubMed=12215541; DOI=10.1128/mcb.22.19.6842-6853.2002;
RA   Lavista-Llanos S., Centanin L., Irisarri M., Russo D.M., Gleadle J.M.,
RA   Bocca S.N., Muzzopappa M., Ratcliffe P.J., Wappner P.;
RT   "Control of the hypoxic response in Drosophila melanogaster by the basic
RT   helix-loop-helix PAS protein similar.";
RL   Mol. Cell. Biol. 22:6842-6853(2002).
CC   -!- FUNCTION: Functions as a transcriptional regulator of the adaptive
CC       response to hypoxia. Binds to core DNA sequence 5'-[AG]CGTG-3' within
CC       the hypoxia response element (HRE) of target gene promoters.
CC       {ECO:0000269|PubMed:12215541, ECO:0000269|PubMed:9731218}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Interacts with Vhl. {ECO:0000269|PubMed:11006129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12215541}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:12215541}.
CC       Note=Cytoplasmic in normoxia, nuclear translocation in response to
CC       hypoxia.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in the embryo.
CC       {ECO:0000269|PubMed:8682312}.
CC   -!- INDUCTION: By hypoxia. {ECO:0000269|PubMed:12215541,
CC       ECO:0000269|PubMed:9731218}.
CC   -!- DOMAIN: The oxygen-dependent degradation (ODD) domain is required for
CC       cytoplasmic localization in normoxia.
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DR   EMBL; U43090; AAC47303.1; -; mRNA.
DR   EMBL; AE014297; AAF57008.2; -; Genomic_DNA.
DR   PIR; JC4851; JC4851.
DR   RefSeq; NP_524584.2; NM_079845.4.
DR   AlphaFoldDB; Q24167; -.
DR   SMR; Q24167; -.
DR   BioGRID; 68436; 207.
DR   DIP; DIP-21002N; -.
DR   ELM; Q24167; -.
DR   IntAct; Q24167; 5.
DR   STRING; 7227.FBpp0084931; -.
DR   PaxDb; Q24167; -.
DR   EnsemblMetazoa; FBtr0344374; FBpp0310747; FBgn0266411.
DR   GeneID; 43580; -.
DR   KEGG; dme:Dmel_CG45051; -.
DR   CTD; 43580; -.
DR   FlyBase; FBgn0266411; sima.
DR   VEuPathDB; VectorBase:FBgn0266411; -.
DR   eggNOG; KOG3558; Eukaryota.
DR   HOGENOM; CLU_004124_0_0_1; -.
DR   InParanoid; Q24167; -.
DR   OrthoDB; 922461at2759; -.
DR   PhylomeDB; Q24167; -.
DR   Reactome; R-DME-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR   Reactome; R-DME-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-DME-8951664; Neddylation.
DR   SignaLink; Q24167; -.
DR   BioGRID-ORCS; 43580; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; sima; fly.
DR   GenomeRNAi; 43580; -.
DR   PRO; PR:Q24167; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0266411; Expressed in brain and 29 other tissues.
DR   ExpressionAtlas; Q24167; baseline and differential.
DR   Genevisible; Q24167; DM.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IMP:FlyBase.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0071456; P:cellular response to hypoxia; IDA:FlyBase.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IDA:FlyBase.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:FlyBase.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:FlyBase.
DR   GO; GO:0045088; P:regulation of innate immune response; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:FlyBase.
DR   GO; GO:0060438; P:trachea development; IMP:FlyBase.
DR   CDD; cd00130; PAS; 2.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   1: Evidence at protein level;
KW   Activator; Coiled coil; Cytoplasm; DNA-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..1507
FT                   /note="Protein similar"
FT                   /id="PRO_0000127444"
FT   DOMAIN          72..125
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          167..240
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          307..377
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          381..422
FT                   /note="PAC"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..863
FT                   /note="ODD"
FT   REGION          706..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1204..1228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1251..1287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1356..1460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          880..908
FT                   /evidence="ECO:0000255"
FT   COILED          982..1054
FT                   /evidence="ECO:0000255"
FT   COILED          1110..1162
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        12..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1204..1223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1384..1400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1408..1426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        38
FT                   /note="S -> A (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="S -> L (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        492
FT                   /note="A -> V (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        588
FT                   /note="T -> I (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        709
FT                   /note="T -> K (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        776
FT                   /note="Q -> QQQQ (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        895
FT                   /note="Q -> QQ (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        902
FT                   /note="G -> S (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        982
FT                   /note="A -> T (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1125..1126
FT                   /note="Missing (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1154..1157
FT                   /note="Missing (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1444
FT                   /note="F -> L (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1447
FT                   /note="G -> C (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1451
FT                   /note="S -> N (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1494
FT                   /note="D -> G (in Ref. 1; AAC47303)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1507 AA;  165824 MW;  4102939C8FBFB0C6 CRC64;
     MVSLIDTIEA AAEKQKQSQA VVTNTSASSS SCSSSFSSSP PSSSVGSPSP GAPKTNLTAS
     GKPKEKRRNN EKRKEKSRDA ARCRRSKETE IFMELSAALP LKTDDVNQLD KASVMRITIA
     FLKIREMLQF VPSLRDCNDD IKQDIETAED QQEVKPKLEV GTEDWLNGAE ARELLKQTMD
     GFLLVLSHEG DITYVSENVV EYLGITKIDT LGQQIWEYSH QCDHAEIKEA LSLKRELAQK
     VKDEPQQNSG VSTHHRDLFV RLKCTLTSRG RSINIKSASY KVIHITGHLV VNAKGERLLM
     AIGRPIPHPS NIEIPLGTST FLTKHSLDMR FTYVDDKMHD LLGYSPKDLL DTSLFSCQHG
     ADSERLMATF KSVLSKGQGE TSRYRFLGKY GGYCWILSQA TIVYDKLKPQ SVVCVNYVIS
     NLENKHEIYS LAQQTAASEQ KEQHHQAAET EKEPEKAADP EIIAQETKET VNTPIHTSEL
     QAKPLQLESE KAEKTIEETK TIATIPPVTA TSTADQIKQL PESNPYKQIL QAELLIKREN
     HSPGPRTITA QLLSGSSSGL RPEEKRPKSV TASVLRPSPA PPLTPPPTAV LCKKTPLGVE
     PNLPPTTTAT AAIISSSNQQ LQIAQQTQLQ NPQQPAQDMS KGFCSLFADD GRGLTMLKEE
     PDDLSHHLAS TNCIQLDEMT PFSDMLVGLM GTCLLPEDIN SLDSTTCSTT ASGQHYQSPS
     SSSTSAPSNT SSSNNSYANS PLSPLTPNST ATASNPSHQQ QQQHHNQQQQ QQQQQQHHPQ
     HHDNSNSSSN IDPLFNYREE SNDTSCSQHL HSPSITSKSP EDSSLPSLCS PNSLTQEDDF
     SFEAFAMRAP YIPIDDDMPL LTETDLMWCP PEDLQTMVPK EIDAIQQQLQ QLQQQHHQQY
     AGNTGYQQQQ QQPQLQQQHF SNSLCSSPAS TVSSLSPSPV QQHHQQQQAA VFTSDSSELA
     ALLCGSGNGT LSILAGSGVT VAEECNERLQ QHQQQQQQTS GNEFRTFQQL QQELQLQEEQ
     QQRQQQQQQQ QQQQQQQQLL SLNIECKKEK YDVQMGGSLC HPMEDAFEND YSKDSANLDC
     WDLIQMQVVD TEPVSPNAAS PTPCKVSAIQ LLQQQQQLQQ QQQQQQNIIL NAVPLITIQN
     NKELMQQQQQ QQQQQQQEQL QQPAIKLLNG ASIAPVNTKA TIRLVESKPP TTTQSRMAKV
     NLVPQQQQHG NKRHLNSATG AGNPVESKRL KSGTLCLDVQ SPQLLQQLIG KDPAQQQTQA
     AKRAGSERWQ LSAESKQQKQ QQQQSNSVLK NLLVSGRDDD DSEAMIIDED NSLVQPIPLG
     KYGLPLHCHT STSSVLRDYH NNPLISGTNF QLSPVFGGSD SSGGDGETGS VVSLDDSVPP
     GLTACDTDAS SDSGIDENSL MDGASGSPRK RLSSTSNSTN QAESAPPALD VETPVTQKSV
     EEEFEGGGSG SNAPSRKTSI SFLDSSNPLL HTPAMMDLVN DDYIMGEGGF EFSDNQLEQV
     LGWPEIA
 
 
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