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RAB7A_DICDI
ID   RAB7A_DICDI             Reviewed;         203 AA.
AC   P36411; Q55E70;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Ras-related protein Rab-7a;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P51149};
GN   Name=rab7A; Synonyms=rab7; ORFNames=DDB_G0269236;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX3;
RA   Bush J.M. IV, Nolta K., Rodriguez-Paris J., Temesvari L., Ruscetti T.,
RA   Steck T., Cardelli J.A.;
RT   "Cloning and characterization of a Rab 7-like GTPase in Dictyostelium
RT   discoideum.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
CC   -!- FUNCTION: Small GTPase which cycles between active GTP-bound and
CC       inactive GDP-bound states. In its active state, binds to a variety of
CC       effector proteins playing a key role in the regulation of endo-
CC       lysosomal trafficking. Governs early-to-late endosomal maturation,
CC       microtubule minus-end as well as plus-end directed endosomal migration
CC       and positioning, and endosome-lysosome transport through different
CC       protein-protein interaction cascades (By similarity). Involved in
CC       lipophagy, a cytosolic lipase-independent autophagic pathway (By
CC       similarity). {ECO:0000250|UniProtKB:P51149,
CC       ECO:0000250|UniProtKB:P51150}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P51149};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P51149};
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC       autophagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral
CC       membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid
CC       droplet {ECO:0000250|UniProtKB:P51150}. Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:P51150}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; U02928; AAA80152.1; -; mRNA.
DR   EMBL; AAFI02000005; EAL71968.1; -; Genomic_DNA.
DR   RefSeq; XP_645911.1; XM_640819.2.
DR   AlphaFoldDB; P36411; -.
DR   SMR; P36411; -.
DR   STRING; 44689.DDB0191507; -.
DR   PaxDb; P36411; -.
DR   PRIDE; P36411; -.
DR   EnsemblProtists; EAL71968; EAL71968; DDB_G0269236.
DR   GeneID; 8616852; -.
DR   KEGG; ddi:DDB_G0269236; -.
DR   dictyBase; DDB_G0269236; rab7A.
DR   eggNOG; KOG0394; Eukaryota.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; P36411; -.
DR   OMA; IQACPRD; -.
DR   PhylomeDB; P36411; -.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-8854214; TBC/RABGAPs.
DR   Reactome; R-DDI-8873719; RAB geranylgeranylation.
DR   Reactome; R-DDI-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR   Reactome; R-DDI-9013406; RHOQ GTPase cycle.
DR   Reactome; R-DDI-9013407; RHOH GTPase cycle.
DR   Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR   Reactome; R-DDI-9706019; RHOBTB3 ATPase cycle.
DR   PRO; PR:P36411; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR   GO; GO:0036186; C:early phagosome membrane; IDA:dictyBase.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
DR   GO; GO:0032419; C:extrinsic component of lysosome membrane; ISS:GO_Central.
DR   GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR   GO; GO:0031902; C:late endosome membrane; ISS:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:dictyBase.
DR   GO; GO:0005764; C:lysosome; IDA:dictyBase.
DR   GO; GO:0044354; C:macropinosome; IDA:dictyBase.
DR   GO; GO:0140220; C:pathogen-containing vacuole; IDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR   GO; GO:0032195; C:post-lysosomal vacuole; IDA:dictyBase.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0099638; P:endosome to plasma membrane protein transport; ISS:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0061724; P:lipophagy; ISS:GO_Central.
DR   GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR   GO; GO:0090385; P:phagosome-lysosome fusion; IBA:GO_Central.
DR   GO; GO:1905303; P:positive regulation of macropinocytosis; IMP:dictyBase.
DR   GO; GO:1905162; P:regulation of phagosome maturation; IMP:dictyBase.
DR   GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:dictyBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cytoplasmic vesicle; Endosome; GTP-binding; Hydrolase;
KW   Lipid degradation; Lipid droplet; Lipid metabolism; Lipoprotein; Lysosome;
KW   Membrane; Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..203
FT                   /note="Ras-related protein Rab-7a"
FT                   /id="PRO_0000121273"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..158
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           202
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           203
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   203 AA;  22695 MW;  8984547A7725B521 CRC64;
     MATKKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEL MVDDRVVTMQ
     IWDTAGQERF QSLGVAFYRG ADCCVLCYDV NVAKTFENLD SWRDEFLIQA GPRDPDNFPF
     VVLGNKIDLE NQRVVSQKRA ASWCQSKGNI PYFETSAKEA INVEQAFQTI ARNAIKLEDG
     LVFPIPTNIQ VIPEPQPAKS GCC
 
 
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