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Ras-related protein Rab-5A (Small GTP-binding protein rab5)

 RAB5A_RAT               Reviewed;         215 AA.
M0RC99; O88565;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
03-APR-2013, sequence version 1.
12-SEP-2018, entry version 47.
RecName: Full=Ras-related protein Rab-5A;
AltName: Full=Small GTP-binding protein rab5 {ECO:0000303|Ref.1};
Name=Rab5a {ECO:0000312|RGD:620936};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
Looman A.C., Hofsommer S., Stevens P.A.;
"Small GTP-binding protein rab5 from rat type II pneumocytes.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: The small GTPases Rab are key regulators of
intracellular membrane trafficking, from the formation of
transport vesicles to their fusion with membranes. Rabs cycle
between an inactive GDP-bound form and an active GTP-bound form
that is able to recruit to membranes different sets of downstream
effectors directly responsible for vesicle formation, movement,
tethering and fusion. RAB5A is required for the fusion of plasma
membranes and early endosomes. Contributes to the regulation of
filopodia extension. Required for the exosomal release of SDCBP,
CD63, PDCD6IP and syndecan. Regulates maturation of apoptotic
cell-containing phagosomes, probably downstream of DYN2 and
PIK3C3. {ECO:0000250|UniProtKB:P18066,
ECO:0000250|UniProtKB:P20339, ECO:0000250|UniProtKB:Q9CQD1}.
-!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange
factors (GEFs) which promote the exchange of bound GDP for free
GTP. {ECO:0000250|UniProtKB:P18066}.
-!- SUBUNIT: Interacts with GDI1; this promotes dissociation from
membranes. Interacts with EEA1. Interacts with RIN1 and GAPVD1,
which regulate its pathway, probably by acting as a GEF. Interacts
with ALS2CL, SUN2, ZFYVE20 and RUFY1. Interacts with RABEP1; one
RABEP1 homodimer binds two RAB5A chains, but at opposite sides of
the dimer. Interacts with SGSM1, SGSM3 and PIK3CB. Interacts with
RINL. May be a component of a complex composed of RAB5A, DYN2 and
PIK3C3. Does not interact with the BLOC-3 complex (heterodimer of
HPS1 and HPS4). Interacts with CLN5.
{ECO:0000250|UniProtKB:P18066, ECO:0000250|UniProtKB:P20339,
ECO:0000250|UniProtKB:Q9CQD1}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P20339}; Lipid-anchor
{ECO:0000250|UniProtKB:P20339}; Cytoplasmic side
{ECO:0000250|UniProtKB:P18066}. Early endosome membrane
{ECO:0000250|UniProtKB:P20339}; Lipid-anchor
{ECO:0000250|UniProtKB:P20339}. Melanosome
{ECO:0000250|UniProtKB:P20339}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:P20339}. Cell projection, ruffle
{ECO:0000250|UniProtKB:P18066}. Membrane
{ECO:0000250|UniProtKB:P20339}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P20339}. Cytoplasmic vesicle, phagosome
membrane {ECO:0000250|UniProtKB:Q9CQD1}. Endosome membrane
{ECO:0000250|UniProtKB:P20339}. Note=Enriched in stage I
melanosomes. Alternates between membrane-bound and cytosolic
forms. {ECO:0000250|UniProtKB:P20339}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF072935; AAC26004.1; -; mRNA.
EMBL; AABR06079878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474184; EDL82849.1; -; Genomic_DNA.
EMBL; BC161848; AAI61848.1; -; mRNA.
RefSeq; NP_073183.1; NM_022692.1.
RefSeq; XP_003751425.1; XM_003751377.4.
RefSeq; XP_003752788.1; XM_003752740.4.
UniGene; Rn.44477; -.
SMR; M0RC99; -.
BioGrid; 249171; 1.
IntAct; M0RC99; 3.
MINT; M0RC99; -.
STRING; 10116.ENSRNOP00000067210; -.
PaxDb; M0RC99; -.
PRIDE; M0RC99; -.
GeneID; 100361891; -.
GeneID; 64633; -.
KEGG; rno:100361891; -.
KEGG; rno:64633; -.
CTD; 100361891; -.
CTD; 5868; -.
RGD; 620936; Rab5a.
eggNOG; KOG0092; Eukaryota.
eggNOG; ENOG410YCCP; LUCA.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; M0RC99; -.
KO; K07887; -.
TreeFam; TF300199; -.
PRO; PR:M0RC99; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
GO; GO:0030424; C:axon; IDA:ParkinsonsUK-UCL.
GO; GO:0043679; C:axon terminus; IDA:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
GO; GO:0005769; C:early endosome; IDA:RGD.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
GO; GO:0005768; C:endosome; IDA:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0098842; C:postsynaptic early endosome; IDA:SynGO.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0055037; C:recycling endosome; IDA:RGD.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0036477; C:somatodendritic compartment; IDA:ParkinsonsUK-UCL.
GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
GO; GO:0042589; C:zymogen granule membrane; IDA:RGD.
GO; GO:0051021; F:GDP-dissociation inhibitor binding; IDA:RGD.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IMP:RGD.
GO; GO:0007032; P:endosome organization; IMP:ParkinsonsUK-UCL.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
GO; GO:0051489; P:regulation of filopodium assembly; IBA:GO_Central.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:RGD.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISS:ParkinsonsUK-UCL.
GO; GO:0016192; P:vesicle-mediated transport; NAS:RGD.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
2: Evidence at transcript level;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Endocytosis; Endosome; GTP-binding; Lipoprotein;
Membrane; Nucleotide-binding; Phagocytosis; Prenylation;
Protein transport; Reference proteome; Transport.
CHAIN 1 215 Ras-related protein Rab-5A.
/FTId=PRO_0000430501.
NP_BIND 27 35 GTP. {ECO:0000250|UniProtKB:P20339}.
NP_BIND 46 52 GTP. {ECO:0000250|UniProtKB:P20339}.
NP_BIND 75 79 GTP. {ECO:0000250|UniProtKB:P20339}.
NP_BIND 133 136 GTP. {ECO:0000250|UniProtKB:P20339}.
NP_BIND 163 165 GTP. {ECO:0000250|UniProtKB:P20339}.
MOTIF 49 57 Effector region. {ECO:0000250}.
LIPID 212 212 S-geranylgeranyl cysteine.
{ECO:0000250|UniProtKB:P20339}.
LIPID 213 213 S-geranylgeranyl cysteine.
{ECO:0000250|UniProtKB:P20339}.
CONFLICT 167 167 P -> S (in Ref. 1; AAC26004, 3; EDL82849
and 4; AAI61848). {ECO:0000305}.
SEQUENCE 215 AA; 23625 MW; 716AB5CC4ECAFD77 CRC64;
MANRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLTQ
TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNEESFSR AKNWVKELQR
QASPNIVIAL SGNKADLANK RAVDFQEAQS YADDNSLLFM ETSAKTPMNV NEIFMAIAKK
LPKNEPQNPG ANSARGRGVD LTEPAQPARS QCCSN


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