Q9CQD1 (RAB5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-5A

Gene names

Name:	Rab5a
Synonyms:	nnyRab5a

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension By similarity.
Enzyme regulation	Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP.
Subunit structure	Binds EEA1. Interacts with ALS2CL, SUN2, ZFYVE20 and RUFY1. Interacts with RIN1 and GAPVD1, which regulate its pathway, probably by acting as a GEF. Interacts with RINL By similarity. Interacts with SGSM1 and SGSM3. Interacts with PIK3CB. Ref.7 Ref.8
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Early endosome membrane; Lipid-anchor By similarity. Melanosome By similarity. Cytoplasmic vesicle By similarity. Cell projection › ruffle By similarity.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis Protein transport Transport
Cellular component	Cell membrane Cell projection Cytoplasmic vesicle Endosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW endocytosis Inferred from sequence or structural similarity. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of exocytosis Inferred from electronic annotation. Source: Compara protein transport Inferred from electronic annotation. Source: UniProtKB-KW receptor internalization involved in canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara regulation of filopodium assembly Inferred from electronic annotation. Source: Compara small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	actin cytoskeleton Inferred from direct assay PubMed 21419809. Source: MGI early endosome Inferred from direct assay PubMed 12446704PubMed 14668490PubMed 19509052PubMed 8197185PubMed 9034150. Source: MGI early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endocytic vesicle Inferred from direct assay PubMed 8197185. Source: MGI melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane raft Inferred from direct assay PubMed 12388596. Source: MGI plasma membrane Inferred from direct assay PubMed 8197185. Source: MGI ruffle Inferred from direct assay PubMed 12446704PubMed 21419809. Source: MGI
Molecular_function	GDP binding Inferred from sequence or structural similarity. Source: UniProtKB GTP binding Inferred from sequence or structural similarity. Source: UniProtKB GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 215	215	Ras-related protein Rab-5A		PRO_0000121106
Regions
	Nucleotide binding	27 – 35	9	GTP By similarity
	Nucleotide binding	75 – 79	5	GTP By similarity
	Nucleotide binding	133 – 136	4	GTP By similarity
	Nucleotide binding	163 – 165	3	GTP By similarity
	Motif	49 – 57	9	Effector region By similarity
Amino acid modifications
	Lipidation	212	1	S-geranylgeranyl cysteine By similarity
	Lipidation	213	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Sequence conflict	13	1	N → D in BAE29485. Ref.3
	Sequence conflict	119	1	Q → R in BAB22245. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9CQD1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 9CDE2FD9B37C261A	FASTA	215	23,599
	10 20 30 40 50 60 MANRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLTQ 70 80 90 100 110 120 TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNEESFAR AKNWVKELQR 130 140 150 160 170 180 QASPNIVIAL SGNKADLANK RAVDFQEAQS YADDNSLLFM ETSAKTSMNV NEIFMAIAKK 190 200 210 LPKNEPQNPG ANSARGRGVD LTEPAQPARS QCCSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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/c. 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/c. 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, MASS SPECTROMETRY. Strain: C57BL/6. 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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00132410.
RefSeq	NP_080163.1. NM_025887.4.
UniGene	Mm.329123.
3D structure databases
ProteinModelPortal	Q9CQD1.
SMR	Q9CQD1. Positions 15-184.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9CQD1. 1 interaction.
STRING	10090.ENSMUSP00000017975.
PTM databases
PhosphoSite	Q9CQD1.
Proteomic databases
PaxDb	Q9CQD1.
PRIDE	Q9CQD1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000017975; ENSMUSP00000017975; ENSMUSG00000017831.
GeneID	271457.
KEGG	mmu:271457.
Organism-specific databases
CTD	5868.
MGI	MGI:105926. Rab5a.
Phylogenomic databases
eggNOG	COG1100.
GeneTree	ENSGT00640000091139.
HOGENOM	HOG000233968.
HOVERGEN	HBG009351.
InParanoid	Q9CQD1.
KO	K07887.
OMA	EPQNTGA.
OrthoDB	EOG4Z0B6M.
Gene expression databases
ArrayExpress	Q9CQD1.
Bgee	Q9CQD1.
CleanEx	MM_RAB5A.
Genevestigator	Q9CQD1.
GermOnline	ENSMUSG00000017831. Mus musculus.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view]
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00175. RAB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51419. RAB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RAB5A. mouse.
NextBio	393462.
SOURCE	Search...

Entry information

Entry name

RAB5A_MOUSE

Accession

Primary (citable) accession number: Q9CQD1
Secondary accession number(s): Q3UCX7, Q4VAA1, Q9DCN5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program