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NACA_DROME
ID   NACA_DROME              Reviewed;         217 AA.
AC   Q94518; A4UZF1; O16813; Q0E999;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE            Short=NAC-alpha;
DE   AltName: Full=Alpha-NAC;
GN   Name=Nacalpha; Synonyms=aic; ORFNames=CG8759;
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].
RX   PubMed=10071211; DOI=10.1007/s004380050942;
RA   Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA   Barsanti P.;
RT   "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT   of a collection of D. melanogaster cDNAs homologous to sequences in the
RT   Human Gene Index database.";
RL   Mol. Gen. Genet. 261:64-70(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11102369; DOI=10.1093/genetics/156.4.1727;
RA   Frolov M.V., Benevolenskaya E.V., Birchler J.A.;
RT   "The oxen gene of Drosophila encodes a homolog of subunit 9 of yeast
RT   ubiquinol-cytochrome c oxidoreductase complex: evidence for modulation of
RT   gene expression in response to mitochondrial activity.";
RL   Genetics 156:1727-1736(2000).
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 [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH BIC.
RX   PubMed=15239960; DOI=10.1016/j.devcel.2004.06.009;
RA   Braat A.K., Yan N., Arn E., Harrison D., Macdonald P.M.;
RT   "Localization-dependent oskar protein accumulation; control after the
RT   initiation of translation.";
RL   Dev. Cell 7:125-131(2004).
CC   -!- FUNCTION: May promote appropriate targeting of ribosome-nascent
CC       polypeptide complexes (By similarity). Required for correct
CC       localization of the osk/oskar protein to the posterior pole during
CC       embryonic development. The osk protein directs the recruitment of
CC       molecules responsible for posterior body patterning and germline
CC       formation in the embryo. {ECO:0000250, ECO:0000269|PubMed:15239960}.
CC   -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC       consisting of Nac-alpha and bicaudal (bic).
CC   -!- INTERACTION:
CC       Q94518; Q7KM15: bic; NbExp=5; IntAct=EBI-127575, EBI-110745;
CC       Q94518; B3DNI1: CG13402-RA; NbExp=4; IntAct=EBI-127575, EBI-15121031;
CC   -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000305}.
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DR   EMBL; Y08969; CAA70166.1; -; mRNA.
DR   EMBL; AF017783; AAB97513.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68653.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68654.1; -; Genomic_DNA.
DR   EMBL; AY075332; AAL68199.1; -; mRNA.
DR   RefSeq; NP_001286363.1; NM_001299434.1.
DR   RefSeq; NP_477216.1; NM_057868.4.
DR   RefSeq; NP_599139.1; NM_134312.3.
DR   RefSeq; NP_725229.1; NM_165950.2.
DR   AlphaFoldDB; Q94518; -.
DR   BioGRID; 62181; 83.
DR   IntAct; Q94518; 21.
DR   STRING; 7227.FBpp0086971; -.
DR   PaxDb; Q94518; -.
DR   PRIDE; Q94518; -.
DR   DNASU; 36409; -.
DR   EnsemblMetazoa; FBtr0087858; FBpp0086971; FBgn0086904.
DR   EnsemblMetazoa; FBtr0087859; FBpp0086972; FBgn0086904.
DR   EnsemblMetazoa; FBtr0087860; FBpp0086973; FBgn0086904.
DR   EnsemblMetazoa; FBtr0345195; FBpp0311394; FBgn0086904.
DR   GeneID; 36409; -.
DR   KEGG; dme:Dmel_CG8759; -.
DR   CTD; 36409; -.
DR   FlyBase; FBgn0086904; Nacalpha.
DR   VEuPathDB; VectorBase:FBgn0086904; -.
DR   eggNOG; KOG2239; Eukaryota.
DR   GeneTree; ENSGT00940000161501; -.
DR   HOGENOM; CLU_057806_1_2_1; -.
DR   InParanoid; Q94518; -.
DR   OMA; LVMCQAN; -.
DR   OrthoDB; 1331328at2759; -.
DR   PhylomeDB; Q94518; -.
DR   SignaLink; Q94518; -.
DR   BioGRID-ORCS; 36409; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; Nacalpha; fly.
DR   GenomeRNAi; 36409; -.
DR   PRO; PR:Q94518; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0086904; Expressed in embryonic/larval hemocyte (Drosophila) and 42 other tissues.
DR   ExpressionAtlas; Q94518; baseline and differential.
DR   Genevisible; Q94518; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR   Gene3D; 2.20.70.30; -; 1.
DR   InterPro; IPR016641; EGD2/NACA.
DR   InterPro; IPR044034; NAC-like_UBA.
DR   InterPro; IPR038187; NAC_A/B_dom_sf.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR   PANTHER; PTHR21713; PTHR21713; 1.
DR   Pfam; PF19026; HYPK_UBA; 1.
DR   Pfam; PF01849; NAC; 1.
DR   PIRSF; PIRSF015901; NAC_alpha; 1.
DR   SMART; SM01407; NAC; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..217
FT                   /note="Nascent polypeptide-associated complex subunit
FT                   alpha"
FT                   /id="PRO_0000135586"
FT   DOMAIN          70..135
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   DOMAIN          177..217
FT                   /note="UBA"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        47
FT                   /note="A -> P (in Ref. 1; CAA70166)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="D -> N (in Ref. 1; CAA70166)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="N -> D (in Ref. 1; CAA70166)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   217 AA;  23021 MW;  6E1BD9C91E1D7F93 CRC64;
     MPELTEIKSE AAPSTSAEAK PEDVRVEDDG SDSDSDGGMP GLEEAVAATT QLGGGATGLP
     IDLVSKAKQS RGEKKARKIM LKLGLKQIQG VNRVTIRKSK NILFVINNPD VYKNPHSDTY
     IVFGEAKIED LSQQAQVAAA EKFKAPEAAG AADSVGATTS VAPIAEEDEE DVDDTGVDEK
     DIELVITQAN TTRAKAIKAL KNNNNDIVNA IMELTML
 
 
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