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Protein

Ras-related protein Rab-5A

Gene

Rab5a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3 (PubMed:18425118).By similarity1 Publication

Enzyme regulationi

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 359GTPBy similarity
Nucleotide bindingi46 – 527GTPBy similarity
Nucleotide bindingi75 – 795GTPBy similarity
Nucleotide bindingi133 – 1364GTPBy similarity
Nucleotide bindingi163 – 1653GTPBy similarity

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • guanyl nucleotide binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Phagocytosis, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-5A
Gene namesi
Name:Rab5a
Synonyms:nnyRab5a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:105926. Rab5a.

Subcellular locationi

  • Cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
  • Early endosome membrane By similarity; Lipid-anchor By similarity
  • Melanosome 1 Publication
  • Cytoplasmic vesicle By similarity
  • Cell projectionruffle By similarity
  • Membrane By similarity
  • Cytoplasmcytosol By similarity
  • Cytoplasmic vesiclephagosome membrane 1 Publication

  • Note: Enriched in stage I melanosomes. Alternates between membrane-bound and cytosolic forms.By similarity

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • axon Source: ParkinsonsUK-UCL
  • axon terminus Source: ParkinsonsUK-UCL
  • cytoplasm Source: MGI
  • cytoplasmic side of early endosome membrane Source: MGI
  • cytosol Source: MGI
  • dendrite Source: ParkinsonsUK-UCL
  • early endosome Source: MGI
  • endocytic vesicle Source: MGI
  • endosome Source: MGI
  • extracellular exosome Source: MGI
  • melanosome Source: UniProtKB-SubCell
  • membrane raft Source: MGI
  • neuronal cell body Source: ParkinsonsUK-UCL
  • phagocytic vesicle Source: MGI
  • plasma membrane Source: MGI
  • ruffle Source: MGI
  • somatodendritic compartment Source: ParkinsonsUK-UCL
  • synaptic vesicle Source: ParkinsonsUK-UCL
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341S → N: Inhibits endosome localization. Disrupts interaction of RAB5A and OCRL with INPP5F. Prevents its localization to apoptotic cell corpse-containing early phagosomes. Maturation of apoptotic cell-containing phagosome into acidic phagosomes is decreased. Interacts with PIK3C3. 2 Publications
Mutagenesisi79 – 791Q → L: Induces the formation of larger endosomes. No effect on interaction with INPP5F. Prevents interaction with DYN2 without affecting the interaction with PIK3C3. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Ras-related protein Rab-5APRO_0000121106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi212 – 2121S-geranylgeranyl cysteineBy similarity
Lipidationi213 – 2131S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

EPDiQ9CQD1.
MaxQBiQ9CQD1.
PaxDbiQ9CQD1.
PRIDEiQ9CQD1.

PTM databases

iPTMnetiQ9CQD1.
PhosphoSiteiQ9CQD1.
SwissPalmiQ9CQD1.

Expressioni

Gene expression databases

BgeeiQ9CQD1.
CleanExiMM_RAB5A.
GenevisibleiQ9CQD1. MM.

Interactioni

Subunit structurei

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 RINL. Interacts with ALS2CL, SUN2, ZFYVE20 and RUFY1. Interacts with RABEP1; one RABEP1 homodimer binds two RAB5A chains, but at opposite sides of the dimer (By similarity). Interacts with SGSM1 and SGSM3 (PubMed:17509819). Interacts with PIK3CB (PubMed:21059846). Interacts with OCRL and INPP5F (PubMed:25869668). May be a component of a complex composed of RAB5A, DYN2 and PIK3C3 (PubMed:18425118).By similarity1 Publication3 Publications

Protein-protein interaction databases

BioGridi234840. 5 interactions.
IntActiQ9CQD1. 11 interactions.
STRINGi10090.ENSMUSP00000017975.

Structurei

3D structure databases

ProteinModelPortaliQ9CQD1.
SMRiQ9CQD1. Positions 15-184.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi49 – 579Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG0092. Eukaryota.
ENOG410YCCP. LUCA.
GeneTreeiENSGT00760000119101.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9CQD1.
KOiK07887.
OMAiPKSQCCS.
OrthoDBiEOG77DJ7M.
PhylomeDBiQ9CQD1.
TreeFamiTF300199.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CQD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE
60 70 80 90 100
STIGAAFLTQ TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY
110 120 130 140 150
DITNEESFAR AKNWVKELQR QASPNIVIAL SGNKADLANK RAVDFQEAQS
160 170 180 190 200
YADDNSLLFM ETSAKTSMNV NEIFMAIAKK LPKNEPQNPG ANSARGRGVD
210
LTEPAQPARS QCCSN
Length:215
Mass (Da):23,599
Last modified:June 1, 2001 - v1
Checksum:i9CDE2FD9B37C261A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131N → D in BAE29485 (PubMed:16141072).Curated
Sequence conflicti119 – 1191Q → R in BAB22245 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB232593 mRNA. Translation: BAF02855.1.
AK002631 mRNA. Translation: BAB22245.1.
AK008198 mRNA. Translation: BAB25527.1.
AK010495 mRNA. Translation: BAB26985.1.
AK081999 mRNA. Translation: BAC38391.1.
AK150296 mRNA. Translation: BAE29448.1.
AK150346 mRNA. Translation: BAE29485.1.
AK150405 mRNA. Translation: BAE29531.1.
AK151066 mRNA. Translation: BAE30082.1.
AK153131 mRNA. Translation: BAE31744.1.
AK159706 mRNA. Translation: BAE35305.1.
CH466559 Genomic DNA. Translation: EDL23663.1.
BC004842 mRNA. Translation: AAH04842.1.
BC034370 mRNA. Translation: AAH34370.1.
BC096481 mRNA. Translation: AAH96481.1.
CCDSiCCDS28879.1.
RefSeqiNP_080163.1. NM_025887.4.
UniGeneiMm.329123.

Genome annotation databases

EnsembliENSMUST00000017975; ENSMUSP00000017975; ENSMUSG00000017831.
GeneIDi271457.
KEGGimmu:271457.
UCSCiuc008czn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB232593 mRNA. Translation: BAF02855.1.
AK002631 mRNA. Translation: BAB22245.1.
AK008198 mRNA. Translation: BAB25527.1.
AK010495 mRNA. Translation: BAB26985.1.
AK081999 mRNA. Translation: BAC38391.1.
AK150296 mRNA. Translation: BAE29448.1.
AK150346 mRNA. Translation: BAE29485.1.
AK150405 mRNA. Translation: BAE29531.1.
AK151066 mRNA. Translation: BAE30082.1.
AK153131 mRNA. Translation: BAE31744.1.
AK159706 mRNA. Translation: BAE35305.1.
CH466559 Genomic DNA. Translation: EDL23663.1.
BC004842 mRNA. Translation: AAH04842.1.
BC034370 mRNA. Translation: AAH34370.1.
BC096481 mRNA. Translation: AAH96481.1.
CCDSiCCDS28879.1.
RefSeqiNP_080163.1. NM_025887.4.
UniGeneiMm.329123.

3D structure databases

ProteinModelPortaliQ9CQD1.
SMRiQ9CQD1. Positions 15-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234840. 5 interactions.
IntActiQ9CQD1. 11 interactions.
STRINGi10090.ENSMUSP00000017975.

PTM databases

iPTMnetiQ9CQD1.
PhosphoSiteiQ9CQD1.
SwissPalmiQ9CQD1.

Proteomic databases

EPDiQ9CQD1.
MaxQBiQ9CQD1.
PaxDbiQ9CQD1.
PRIDEiQ9CQD1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017975; ENSMUSP00000017975; ENSMUSG00000017831.
GeneIDi271457.
KEGGimmu:271457.
UCSCiuc008czn.1. mouse.

Organism-specific databases

CTDi5868.
MGIiMGI:105926. Rab5a.

Phylogenomic databases

eggNOGiKOG0092. Eukaryota.
ENOG410YCCP. LUCA.
GeneTreeiENSGT00760000119101.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9CQD1.
KOiK07887.
OMAiPKSQCCS.
OrthoDBiEOG77DJ7M.
PhylomeDBiQ9CQD1.
TreeFamiTF300199.

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiRab5a. mouse.
PROiQ9CQD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQD1.
CleanExiMM_RAB5A.
GenevisibleiQ9CQD1. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain."
    Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.
    J. Biol. Chem. 277:9212-9218(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing proteins based on their Rab-binding activity."
    Itoh T., Satoh M., Kanno E., Fukuda M.
    Genes Cells 11:1023-1037(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Embryonic stem cell, Head and Small intestine.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  6. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-33; 82-110 AND 184-195, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  7. "Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway."
    Yang H., Sasaki T., Minoshima S., Shimizu N.
    Genomics 90:249-260(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGSM1 AND SGSM3.
  8. Cited for: FUNCTION, INTERACTION WITH PIK3C3 AND DYN2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-34 AND GLN-79.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive regulator of autophagy."
    Dou Z., Chattopadhyay M., Pan J.-A., Guerriero J.L., Jiang Y.-P., Ballou L.M., Yue Z., Lin R.Z., Zong W.-X.
    J. Cell Biol. 191:827-843(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIK3CB.
  11. "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic pathway."
    Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M., De Camilli P.
    J. Cell Biol. 209:85-95(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OCRL AND INPP5F, MUTAGENESIS OF SER-34 AND GLN-79.

Entry informationi

Entry nameiRAB5A_MOUSE
AccessioniPrimary (citable) accession number: Q9CQD1
Secondary accession number(s): Q3UCX7, Q4VAA1, Q9DCN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.