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RIPL_DROME
ID   RIPL_DROME              Reviewed;         443 AA.
AC   O76878;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=RILP-like protein homolog {ECO:0000305};
DE   AltName: Full=Rab-interacting lysosomal protein-like {ECO:0000303|PubMed:30115618, ECO:0000312|FlyBase:FBgn0024985};
GN   Name=Rilpl {ECO:0000303|PubMed:30115618, ECO:0000312|FlyBase:FBgn0024985};
GN   ORFNames=CG11448 {ECO:0000312|FlyBase:FBgn0024985};
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA   Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA   Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA   Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA   Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA   Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [4]
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   [5]
RP   FUNCTION, INTERACTION WITH ARL8, AND SUBCELLULAR LOCATION.
RX   PubMed=30115618; DOI=10.1242/bio.035964;
RA   Rosa-Ferreira C., Sweeney S.T., Munro S.;
RT   "The small G protein Arl8 contributes to lysosomal function and long-range
RT   axonal transport in Drosophila.";
RL   Biol. Open 7:0-0(2018).
CC   -!- FUNCTION: May have a role in lysosome distribution by interacting with
CC       Arl8. {ECO:0000269|PubMed:30115618}.
CC   -!- SUBUNIT: Interacts with Arl8 (in GTP-bound form).
CC       {ECO:0000269|PubMed:30115618}.
CC   -!- INTERACTION:
CC       O76878; Q9VHM7: nom; NbExp=4; IntAct=EBI-163187, EBI-180584;
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:30115618}.
CC       Note=Localizes to the perinuclear region when associated with Arl8.
CC       {ECO:0000269|PubMed:30115618}.
CC   -!- SIMILARITY: Belongs to the RILPL family. {ECO:0000305}.
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DR   EMBL; AE014298; AAF45619.1; -; Genomic_DNA.
DR   EMBL; AL023893; CAA19654.1; -; Genomic_DNA.
DR   EMBL; AY060341; AAL25380.1; -; mRNA.
DR   RefSeq; NP_569910.1; NM_130554.3.
DR   AlphaFoldDB; O76878; -.
DR   SMR; O76878; -.
DR   BioGRID; 57648; 14.
DR   IntAct; O76878; 10.
DR   STRING; 7227.FBpp0304571; -.
DR   PaxDb; O76878; -.
DR   PRIDE; O76878; -.
DR   DNASU; 31090; -.
DR   EnsemblMetazoa; FBtr0070225; FBpp0070216; FBgn0024985.
DR   GeneID; 31090; -.
DR   KEGG; dme:Dmel_CG11448; -.
DR   UCSC; CG11448-RA; d. melanogaster.
DR   CTD; 31090; -.
DR   FlyBase; FBgn0024985; Rilpl.
DR   VEuPathDB; VectorBase:FBgn0024985; -.
DR   eggNOG; ENOG502QR9G; Eukaryota.
DR   GeneTree; ENSGT00940000169426; -.
DR   InParanoid; O76878; -.
DR   OMA; NHELHGA; -.
DR   PhylomeDB; O76878; -.
DR   SignaLink; O76878; -.
DR   BioGRID-ORCS; 31090; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; CG11448; fly.
DR   GenomeRNAi; 31090; -.
DR   PRO; PR:O76878; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0024985; Expressed in seminal fluid secreting gland and 21 other tissues.
DR   ExpressionAtlas; O76878; baseline and differential.
DR   Genevisible; O76878; DM.
DR   GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030742; F:GTP-dependent protein binding; IPI:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR   GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR   InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR   InterPro; IPR034743; RH1.
DR   InterPro; IPR034744; RH2.
DR   Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR   PROSITE; PS51776; RH1; 1.
DR   PROSITE; PS51777; RH2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Lysosome; Membrane; Reference proteome.
FT   CHAIN           1..443
FT                   /note="RILP-like protein homolog"
FT                   /id="PRO_0000299315"
FT   DOMAIN          8..96
FT                   /note="RH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT   DOMAIN          282..401
FT                   /note="RH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT   REGION          311..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          59..315
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        335..358
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   443 AA;  50147 MW;  E5F1242F3DDBD15B CRC64;
     MPGFHLNEMG EMVLDAIDDI GVVDVYDLAS DIGKEYERIM DRFGTDAVSG LMPKIINTLE
     LLEALATKNE RENATIQELR DKVAQLESEK LEKAEFRRRF DKELELIEEQ WRSETNELVD
     LVSSLQDENK RLVKQTQDLQ SSSAQSSGLG ASLTESIISM TNHELHSALS DTQVLQRLKE
     QIYKQRDELK HRERELQDKY SELEHLNIQA ERLKASERDT RRRHKLMQAQ VKTLCEERAD
     FLAQLQDQSR EINQLRKRLG LAEKENEDLV ASYDDGQNDP NRPRYTTREL KELISERDEL
     LTTIDTLNEQ LAELKPPSQA KGKRQRHFSS SDDSDEDDDG HVADNDDDDD EEEAAAEANE
     LEPPAAGETP PGHDAPVQGP LPYEPDDAPW KKSSESGIRK FFRKLFSDPS DGSNTFPKRS
     LATLSKMALS ATPGSVSASA AAK
 
 
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