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RAB14_DICDI
ID   RAB14_DICDI             Reviewed;         206 AA.
AC   P36410; Q54U25;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Ras-related protein Rab-14;
DE   AltName: Full=Rab4-like GTPase;
GN   Name=rab14; Synonyms=rab4, rabD; ORFNames=DDB_G0281337;
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;
RX   PubMed=7876348; DOI=10.1242/jcs.107.10.2801;
RA   Bush J.M. IV, Nolta K., Rodriguez-Paris J., Kaufmann N., O'Halloran T.,
RA   Ruscetti T., Temesvari L., Steck T., Cardelli J.A.;
RT   "A Rab4-like GTPase in Dictyostelium discoideum colocalizes with V-H(+)-
RT   ATPases in reticular membranes of the contractile vacuole complex and in
RT   lysosomes.";
RL   J. Cell Sci. 107:2801-2812(1994).
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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8898366; DOI=10.1091/mbc.7.10.1623;
RA   Bush J., Temesvari L., Rodriguez-Paris J., Buczynski G., Cardelli J.;
RT   "A role for a Rab4-like GTPase in endocytosis and in regulation of
RT   contractile vacuole structure and function in Dictyostelium discoideum.";
RL   Mol. Biol. Cell 7:1623-1638(1996).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLN-67 AND ASN-121.
RX   PubMed=12186956; DOI=10.1242/jcs.00050;
RA   Harris E., Cardelli J.;
RT   "RabD, a Dictyostelium Rab14-related GTPase, regulates phagocytosis and
RT   homotypic phagosome and lysosome fusion.";
RL   J. Cell Sci. 115:3703-3713(2002).
CC   -!- FUNCTION: Regulates the fusion of phagosomes and lysosomes.
CC       {ECO:0000269|PubMed:12186956, ECO:0000269|PubMed:8898366}.
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:12186956,
CC       ECO:0000269|PubMed:8898366}. Contractile vacuole
CC       {ECO:0000269|PubMed:12186956, ECO:0000269|PubMed:8898366}. Membrane
CC       {ECO:0000269|PubMed:12186956}; Lipid-anchor {ECO:0000305}.
CC       Note=Endosomal pathway and the contractile vacuole membrane system.
CC       {ECO:0000269|PubMed:12186956, ECO:0000269|PubMed:8898366}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA80151.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U02927; AAA80151.1; ALT_FRAME; mRNA.
DR   EMBL; AAFI02000040; EAL66754.1; -; Genomic_DNA.
DR   RefSeq; XP_640740.1; XM_635648.1.
DR   AlphaFoldDB; P36410; -.
DR   SMR; P36410; -.
DR   IntAct; P36410; 1.
DR   MINT; P36410; -.
DR   STRING; 44689.DDB0214821; -.
DR   PaxDb; P36410; -.
DR   EnsemblProtists; EAL66754; EAL66754; DDB_G0281337.
DR   GeneID; 8623016; -.
DR   KEGG; ddi:DDB_G0281337; -.
DR   dictyBase; DDB_G0281337; rab14.
DR   eggNOG; KOG0097; Eukaryota.
DR   HOGENOM; CLU_041217_23_1_1; -.
DR   InParanoid; P36410; -.
DR   OMA; TRRITYN; -.
DR   PhylomeDB; P36410; -.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-8873719; RAB geranylgeranylation.
DR   Reactome; R-DDI-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:P36410; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0031164; C:contractile vacuolar membrane; IDA:dictyBase.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; IBA: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:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR   GO; GO:0055037; C:recycling endosome; IEA:InterPro.
DR   GO; GO:0062160; C:spongiome; IDA:dictyBase.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0033298; P:contractile vacuole organization; IMP:dictyBase.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR   GO; GO:0032456; P:endocytic recycling; IEA:InterPro.
DR   GO; GO:0006895; P:Golgi to endosome transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0090387; P:phagolysosome assembly involved in apoptotic cell clearance; IBA:GO_Central.
DR   GO; GO:1905364; P:regulation of endosomal vesicle fusion; IMP:dictyBase.
DR   GO; GO:0048548; P:regulation of pinocytosis; IMP:dictyBase.
DR   GO; GO:0006970; P:response to osmotic stress; IMP:dictyBase.
DR   CDD; cd04122; Rab14; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR030702; Rab14.
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   Endosome; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Reference proteome; Vacuole.
FT   CHAIN           1..206
FT                   /note="Ras-related protein Rab-14"
FT                   /id="PRO_0000121272"
FT   REGION          182..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        188..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         15..22
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         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         206
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           204
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           206
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         67
FT                   /note="Q->L: Constitutively active."
FT                   /evidence="ECO:0000269|PubMed:12186956"
FT   MUTAGEN         121
FT                   /note="N->I: Constitutively inactive."
FT                   /evidence="ECO:0000269|PubMed:12186956"
SQ   SEQUENCE   206 AA;  23135 MW;  28FF9504B3A32AB6 CRC64;
     MSFPYEYIFK YIIIGDMGVG KSCLLHQFTE NKFVPDSPHT IGVEFGTRIV DVNNKKIKLQ
     IWDTAGQERF RAVTRSYYRG AAGALLVYDI TRRITYNHLT TWLTDARNLT NPNTVIMLIG
     NKKDLEGQRD VTYEEASAFA KQNGLIFVES SAKTGENVEE AFLRTAKLIF QSVQEGNVDL
     IPDGGITKNP PQTITDKPQD ASKCSC
 
 
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