RB11A_DICDI
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 03-AUG-2022, entry version 142.
DE RecName: Full=Ras-related protein Rab-11A;
GN Name=rab11A; Synonyms=rab11; ORFNames=DDB_G0269238;
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], FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF ASN-126.
RC STRAIN=AX3;
RX PubMed=11686306; DOI=10.1242/jcs.114.16.3035;
RA Harris E., Yoshida K., Cardelli J.A., Bush J.M. IV;
RT "Rab11-like GTPase associates with and regulates the structure and function
RT 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., 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: Required for normal contractile vacuole structure and
CC function. Cells expressing a dominant negative rab11A exhibit a more
CC extensive contractile vacuole network and enlarged contractile vacuole
CC bladders. These cells exhibit a functional defect in osmotic regulation
CC where cells immersed in water become rounded and detach from the
CC surface, and contain swollen contractile vacuoles.
CC {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 https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U02925; AAA80149.1; -; mRNA.
DR EMBL; AAFI02000005; EAL71969.1; -; Genomic_DNA.
DR RefSeq; XP_646557.1; XM_641465.1.
DR AlphaFoldDB; P36412; -.
DR SMR; P36412; -.
DR IntAct; P36412; 2.
DR MINT; P36412; -.
DR STRING; 44689.DDB0191190; -.
DR PaxDb; P36412; -.
DR PRIDE; P36412; -.
DR EnsemblProtists; EAL71969; EAL71969; DDB_G0269238.
DR GeneID; 8617525; -.
DR KEGG; ddi:DDB_G0269238; -.
DR dictyBase; DDB_G0269238; rab11A.
DR eggNOG; KOG0087; Eukaryota.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; P36412; -.
DR OMA; SMKEDYY; -.
DR PhylomeDB; P36412; -.
DR Reactome; R-DDI-8854214; TBC/RABGAPs.
DR Reactome; R-DDI-8873719; RAB geranylgeranylation.
DR PRO; PR:P36412; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0031164; C:contractile vacuolar membrane; IDA:UniProtKB.
DR GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR GO; GO:0140220; C:pathogen-containing vacuole; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:dictyBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR GO; GO:0071476; P:cellular hypotonic response; IMP:dictyBase.
DR GO; GO:0033298; P:contractile vacuole organization; IMP:dictyBase.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0007231; P:osmosensory signaling pathway; IMP:UniProtKB.
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 GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport; Vacuole.
FT CHAIN 1..214
FT /note="Ras-related protein Rab-11A"
FT /id="PRO_0000121274"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 39..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 156..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 126
FT /note="N->I: Loss of GTP-binding activity."
FT /evidence="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
