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DIP2_DROME
ID   DIP2_DROME              Reviewed;        1773 AA.
AC   Q9W0S9; Q9NGP2;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Disco-interacting protein 2;
GN   Name=DIP2; ORFNames=CG7020;
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].
RA   Decroos F.C., Voas M.G., Rebay I.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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   TISSUE SPECIFICITY, AND INTERACTION WITH DISCO.
RX   PubMed=12137943; DOI=10.1016/s0378-1119(02)00694-7;
RA   Mukhopadhyay M., Pelka P., DeSousa D., Kablar B., Schindler A.,
RA   Rudnicki M.A., Campos A.R.;
RT   "Cloning, genomic organization and expression pattern of a novel Drosophila
RT   gene, the disco-interacting protein 2 (dip2), and its murine homolog.";
RL   Gene 293:59-65(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-60 AND TYR-61, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28396149; DOI=10.1016/j.bbrc.2017.04.028;
RA   Nitta Y., Sugie A.;
RT   "DISCO interacting protein 2 determines direction of axon projection under
RT   the regulation of c-Jun N-terminal kinase in the Drosophila mushroom
RT   body.";
RL   Biochem. Biophys. Res. Commun. 487:116-121(2017).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=27908785; DOI=10.1016/j.ydbio.2016.11.015;
RA   Nitta Y., Yamazaki D., Sugie A., Hiroi M., Tabata T.;
RT   "DISCO Interacting Protein 2 regulates axonal bifurcation and guidance of
RT   Drosophila mushroom body neurons.";
RL   Dev. Biol. 421:233-244(2017).
CC   -!- FUNCTION: Required for precise axonal bifurcation in mushroom body
CC       neurons by suppressing ectopic bifurcation and regulating the guidance
CC       of sister axons (PubMed:28396149, PubMed:27908785). Acts downstream of
CC       the serine/threonine-protein kinase Bsk to modulate the direction of
CC       axon projection (PubMed:28396149). May play a role in fatty acid
CC       metabolism (PubMed:27908785). {ECO:0000269|PubMed:27908785,
CC       ECO:0000269|PubMed:28396149}.
CC   -!- SUBUNIT: Interacts with Disco. {ECO:0000269|PubMed:12137943}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27908785,
CC       ECO:0000269|PubMed:28396149}; Peripheral membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the developing nervous system
CC       (PubMed:12137943). Ubiquitously expressed in the developing brain
CC       (PubMed:27908785). Within the mushroom body, a higher level is detected
CC       in the core of lobes and peduncle in the late third instar larva
CC       (PubMed:12137943). Detected in whole mushroom body neuron structures at
CC       48 hours after puparium formation and during later stages
CC       (PubMed:27908785). {ECO:0000269|PubMed:12137943,
CC       ECO:0000269|PubMed:27908785}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the central nervous system
CC       (CNS) in both the brain lobes and the ventral cord throughout
CC       embryogenesis, from early stages of neurogenesis. Expressed in both
CC       neuroblasts and neurons. Expressed at lower level in the visceral
CC       mesoderm during stage 12. Expression of DIP2 overlaps with that of
CC       Disco in the visceral mesoderm and CNS.
CC   -!- DISRUPTION PHENOTYPE: Mushroom body lobe defects including ectopic axon
CC       bifurcations and/or axon guidance defects (PubMed:27908785). RNAi-
CC       mediated knockdown results in an increase in the number of mushroom
CC       body lobes as well as ectopic lobes and guidance defects
CC       (PubMed:28396149, PubMed:27908785). {ECO:0000269|PubMed:27908785,
CC       ECO:0000269|PubMed:28396149}.
CC   -!- SIMILARITY: Belongs to the DIP2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF64300.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF246991; AAF64300.1; ALT_FRAME; mRNA.
DR   EMBL; AE014296; AAF47364.2; -; Genomic_DNA.
DR   RefSeq; NP_612019.2; NM_138175.4.
DR   AlphaFoldDB; Q9W0S9; -.
DR   SMR; Q9W0S9; -.
DR   BioGRID; 76010; 1.
DR   IntAct; Q9W0S9; 3.
DR   STRING; 7227.FBpp0072420; -.
DR   iPTMnet; Q9W0S9; -.
DR   PaxDb; Q9W0S9; -.
DR   PRIDE; Q9W0S9; -.
DR   EnsemblMetazoa; FBtr0072520; FBpp0072420; FBgn0024806.
DR   GeneID; 252479; -.
DR   KEGG; dme:Dmel_CG7020; -.
DR   CTD; 252479; -.
DR   FlyBase; FBgn0024806; DIP2.
DR   VEuPathDB; VectorBase:FBgn0024806; -.
DR   eggNOG; KOG3628; Eukaryota.
DR   GeneTree; ENSGT00950000182997; -.
DR   InParanoid; Q9W0S9; -.
DR   OrthoDB; 539697at2759; -.
DR   PhylomeDB; Q9W0S9; -.
DR   SignaLink; Q9W0S9; -.
DR   BioGRID-ORCS; 252479; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; norpA; fly.
DR   GenomeRNAi; 252479; -.
DR   PRO; PR:Q9W0S9; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0024806; Expressed in eye disc (Drosophila) and 28 other tissues.
DR   ExpressionAtlas; Q9W0S9; baseline and differential.
DR   Genevisible; Q9W0S9; DM.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; ISS:FlyBase.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; ISS:FlyBase.
DR   GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR   CDD; cd05905; Dip2; 2.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.12780; -; 2.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR037337; Dip2-like_dom.
DR   InterPro; IPR010506; DMAP1-bd.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF06464; DMAP_binding; 1.
DR   SMART; SM01137; DMAP_binding; 1.
DR   PROSITE; PS51912; DMAP1_BIND; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Developmental protein; Membrane; Neurogenesis;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..1773
FT                   /note="Disco-interacting protein 2"
FT                   /id="PRO_0000079905"
FT   DOMAIN          3..110
FT                   /note="DMAP1-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT   REGION          112..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..317
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         60
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         61
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CONFLICT        1038..1048
FT                   /note="PLGGIHLCEAR -> LLGAYIYAKHG (in Ref. 1; AAF64300)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1773 AA;  194154 MW;  2A05C475B47DCF9A CRC64;
     MEHTASLPGY VREKLAELDL ELSEGDITQK GYEKKRAKLL QPFLKKPEGD KVKSTPPPPY
     YNVKNANNST NHGNINNDGV IVSSEGYSYV TEVPSLSSSQ QRHSKKIDFH QQAAMSLSSA
     PQSGNAGAPG YENMRPQGGA VGDPGYQNTR EPSAFQNQQS TNNSQHRQRR TQRKVTHNEK
     RYHSEVRQEA VQQALAALKG RPKPSLPMPS KRTSVLNRSP GCNDELDSST DDESIPEETI
     SPDKEYNYPR DHISNSILPP EPIIKPPIRE SSMGSQQHAR TDVKQNQITN QKYTAPNSAP
     ERRPPQNLPP LPTSEPLSSD YPPIAYKREN DFSDKAFKQK QYNAPDITQF NNAHRAADRV
     TRYVNVSQNE LNETDANGKW KVSAKIQQLL NTLKRPKRRP LPEFYEDNDI ELEIAANTKD
     PNAPKPEGST MTPVQGEQLS IPAGLPRTLE CALQRYGTNS FKSPMATVLD PNGKVTTTLT
     YGKLLSRAQK IAHALSTKIF SKGPEQVTLK PGDRVALVYP NNDPLSFITA WYGCMFRGLV
     PLPIELPLSS SDTPPQQVGF LLSSCGITVA LTSEACLKGL PKSTTTGEIA KLKGWPRLQW
     FVTEHLPKPP KEFNVGNLRA DDSAAAYIEY TTDKEGSVMG VTVTRAAMIN HCRALTMACH
     YTEGETIVCV LDFKREVGLW HSVLTSVLNG MHVIFIPYAL MKLRPSSWMQ LITKHRASCC
     LVKSRDLHWG LLATKDHKDI SLSSLRMLLV ADGANPWSLS SCDQFLSVFQ AKGLRSDAIC
     PCASSSEVFT VSLRRPGRGS CGFSPSATGR GVLSMAALSH GVVRVDSEDS LTSLTLQDCG
     QVMPAAQMVV VRSEGPPVLC KTDQVGEICV TSGSTSASYF GLDGMTNSTF KVQPLLEELE
     QPKDGNGTVN IISKPIGEDF YVRSGLLGFL GPGGLVFVCG SRDGLMTVTG RKHNADDIIA
     TVLAVEPMRF IYRGRIAVFS IKVLRDERVC VIAEQRPDCS EEESFQWMSR VLQAVDSIHQ
     VGIYCLALVP PNHLPKTPLG GIHLCEARRR FLEGSLHPAN VLMCPHTCVT NLPKPRELHQ
     GVQTAAKLSS SSGCGITDTG VGPASVMVGN LVQGNRLAEA HGRDVGLAED CERKPQLITG
     VLRWRANTSP DHIIFTLLNS KGAIAKTLTC SELHKRAEKI AALLQERGRI EPGDHVALIF
     PPGLDLLCAF YGCLYLGAIP ITIRPPHPQN LNTTLPTVRM IVDVSKSGIV LSIQPIIKLL
     KSREAATSID PKTWPPILDI DDNPKRKYAG IATVSFDSSA YLDFSVSTCG RLSGVNITHR
     SLSSLCASLK LACELYPSRH VALCLDPYCG LGFVMWTLIG VYSGHHSILI APYEVEANPS
     LWLSTLSQHR VRDTFCSYGV IELCTKALSN SIPSLKQRNI DLRCVRTCVV VAEERPRVQL
     TQQFCKLFQA LGLNTRCVST SFGCRVNPAI CVQGASSAES AQVYVDMRAL RNNRVALVER
     GAPNSLCVIE SGKLLPGVKV IIANPETKGH CGDSHLGEIW VQAPHNANGY FTIYGDETDY
     NDHFNAKLVT GATSELYART GYLGFLRRTE CSQSASLLDE TTPSVASRDS DTESLNSISQ
     LQLNFSNVSL GGNSEHSLVG GASNANDQEL HDAVYVVGAV DEVISLRGMN YHPIDIENSV
     MRCHKKIAEC AVFTWTNLLV VVVELDGNES EALDLVPLVT NTVLEDHQLI VGVVVVVDPG
     VVPINSRGEK QRMHLRDGFL ADQLDPIYVA YNM
 
 
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