GenomeNet

Database: UniProt
Entry: P36412
LinkDB: P36412
Original site: P36412 
ID   RB11A_DICDI             Reviewed;         214 AA.
AC   P36412; Q55CC4;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   29-OCT-2014, entry version 101.
DE   RecName: Full=Ras-related protein Rab-11A;
GN   Name=rab11A; Synonyms=rab11; ORFNames=DDB_G0269238;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF ASN-126.
RC   STRAIN=AX3;
RX   PubMed=11686306;
RA   Harris E., Yoshida K., Cardelli J.A., Bush J.M. IV;
RT   "Rab11-like GTPase associates with and regulates the structure and
RT   function of the contractile vacuole system in dictyostelium.";
RL   J. Cell Sci. 114:3035-3045(2001).
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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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
RT   the role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
CC   -!- FUNCTION: Required for normal contractile vacuole structure and
CC       function. Cells expressing a dominant negative rab11A exhibit a
CC       more extensive contractile vacuole network and enlarged
CC       contractile vacuole bladders. These cells exhibit a functional
CC       defect in osmotic regulation where cells immersed in water become
CC       rounded and detach from the surface, and contain swollen
CC       contractile vacuoles. {ECO:0000269|PubMed:11686306}.
CC   -!- SUBCELLULAR LOCATION: Contractile vacuole membrane
CC       {ECO:0000269|PubMed:11686306}; Lipid-anchor
CC       {ECO:0000269|PubMed:11686306}; Cytoplasmic side
CC       {ECO:0000269|PubMed:11686306}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U02925; AAA80149.1; -; mRNA.
DR   EMBL; AAFI02000005; EAL71969.1; -; Genomic_DNA.
DR   RefSeq; XP_646557.1; XM_641465.1.
DR   ProteinModelPortal; P36412; -.
DR   SMR; P36412; 10-180.
DR   IntAct; P36412; 2.
DR   MINT; MINT-6947977; -.
DR   STRING; 44689.DDB_0191190; -.
DR   PRIDE; P36412; -.
DR   EnsemblProtists; DDB0191190; DDB0191190; DDB_G0269238.
DR   GeneID; 8617525; -.
DR   KEGG; ddi:DDB_G0269238; -.
DR   dictyBase; DDB_G0269238; rab11A.
DR   eggNOG; COG1100; -.
DR   InParanoid; P36412; -.
DR   OMA; AMGTRDD; -.
DR   PhylomeDB; P36412; -.
DR   GO; GO:0031164; C:contractile vacuolar membrane; IDA:UniProtKB.
DR   GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0032794; F:GTPase activating protein binding; IPI:dictyBase.
DR   GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR   GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; IDA:dictyBase.
DR   GO; GO:0071476; P:cellular hypotonic response; IMP:dictyBase.
DR   GO; GO:0007231; P:osmosensory signaling pathway; IMP:UniProtKB.
DR   GO; GO:0032851; P:positive regulation of Rab GTPase activity; IDA:GOC.
DR   GO; GO:0034394; P:protein localization to cell surface; IMP:dictyBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032482; P:Rab protein signal transduction; IMP:dictyBase.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:UniProtKB.
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   InterPro; IPR003579; Small_GTPase_Rab_type.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; GTP-binding; Lipoprotein; Membrane;
KW   Nucleotide-binding; Prenylation; Protein transport;
KW   Reference proteome; Transport; Vacuole.
FT   CHAIN         1    214       Ras-related protein Rab-11A.
FT                                /FTId=PRO_0000121274.
FT   NP_BIND      20     27       GTP. {ECO:0000250}.
FT   NP_BIND      68     72       GTP. {ECO:0000250}.
FT   NP_BIND     126    129       GTP. {ECO:0000250}.
FT   MOTIF        42     50       Effector region. {ECO:0000250}.
FT   LIPID       213    213       S-geranylgeranyl cysteine. {ECO:0000250}.
FT   LIPID       214    214       S-geranylgeranyl cysteine. {ECO:0000250}.
FT   MUTAGEN     126    126       N->I: Loss of GTP-binding activity.
FT                                {ECO:0000269|PubMed:11686306}.
SQ   SEQUENCE   214 AA;  23986 MW;  6A82CA65688B5FE0 CRC64;
     MTSKGSQEEY DYLYKIVLIG DSGVGKSNLL SRFTRNEFSL ETKSTIGVEF ATRTIQTEGK
     TIKAQVWDTA GQERYRAITS AYYRGAVGAL LVYDIAKQAT YKSVERWILE LRENADRNIE
     IMLVGNKSDL RHLREVSTDE AKEFSEKHKL TFIETSALDS SNVELAFQNI LTQIYHIMSR
     PSHSTGPQTT IDSNTETIIL PTTSEPPAAK SGCC
//
DBGET integrated database retrieval system