P51150 (RAB7A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-7a

Gene names

Name:	Rab7a
Synonyms:	Rab7

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in late endocytic transport. Contributes to the maturation of phagosomes (acidification) By similarity.
Subunit structure	Interacts with RILP By similarity. Interacts with PSMA7 By similarity. Interacts with RNF115. Interacts with FYCO1 By similarity. Ref.6
Subcellular location	Late endosome By similarity. Lysosome By similarity. Cytoplasmic vesicle › phagosome By similarity. Melanosome By similarity. Note: Found on late endosomes, lysosomes and phagosomes By similarity.
Tissue specificity	Widely expressed. High expression in liver, heart and kidney. Found in sensory and motor neurons. Ref.5
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasmic vesicle Endosome Lysosome
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	intracellular protein transport Traceable author statement. Source: MGI small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from direct assay. Source: MGI late endosome Inferred from direct assay. Source: MGI lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 207	207	Ras-related protein Rab-7a		PRO_0000121122
Regions
	Nucleotide binding	15 – 22	8	GTP By similarity
	Nucleotide binding	63 – 67	5	GTP By similarity
	Nucleotide binding	125 – 128	4	GTP By similarity
	Motif	37 – 45	9	Effector region By similarity
Amino acid modifications
	Modified residue	72	1	Phosphoserine Ref.7
	Modified residue	183	1	Phosphotyrosine By similarity
	Modified residue	207	1	Cysteine methyl ester By similarity
	Lipidation	205	1	S-geranylgeranyl cysteine By similarity
	Lipidation	207	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Sequence conflict	145	1	S → R in CAA61797. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P51150 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: A2AF33B16A672971	FASTA	207	23,490
	10 20 30 40 50 60 MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ 70 80 90 100 110 120 IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF 130 140 150 160 170 180 VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP YFETSAKEAI NVEQAFQTIA RNALKQETEV 190 200 ELYNEFPEPI KLDKNDRAKA SAESCSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression analysis of the murine Rab7 cDNA." Vitelli R., Chiariello M., Bruni C.B., Bucci C. Biochim. Biophys. Acta 1264:268-270(1995) [PubMed: 8547311] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Liver.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and FVB/N. Tissue: Brain and Mammary tumor.
[4]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 11-31; 70-79; 114-126 AND 147-157, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[5]	"Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot-Marie-Tooth type 2B neuropathy." Verhoeven K., De Jonghe P., Coen K., Verpoorten N., Auer-Grumbach M., Kwon J.M., FitzPatrick D., Schmedding E., De Vriendt E., Jacobs A., Van Gerwen V., Wagner K., Hartung H.-P., Timmerman V. Am. J. Hum. Genet. 72:722-727(2003) [PubMed: 12545426] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Rabring7, a novel Rab7 target protein with a RING finger motif." Mizuno K., Kitamura A., Sasaki T. Mol. Biol. Cell 14:3741-3752(2003) [PubMed: 12972561] [Abstract] Cited for: INTERACTION WITH RNF115.
[7]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X89650 mRNA. Translation: CAA61797.1. AK005004 mRNA. Translation: BAB23738.1. BC004597 mRNA. Translation: AAH04597.1. BC086793 mRNA. Translation: AAH86793.1.
IPI	IPI00408892.
PIR	S62733.
RefSeq	NP_033031.2. NM_009005.2.
UniGene	Mm.333233. Mm.471618.
3D structure databases
ProteinModelPortal	P51150.
SMR	P51150. Positions 7-190.
ModBase	Search...
Protein-protein interaction databases
STRING	P51150.
PTM databases
PhosphoSite	P51150.
Proteomic databases
PRIDE	P51150.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000095048; ENSMUSP00000092658; ENSMUSG00000079477. ENSMUST00000113596; ENSMUSP00000109226; ENSMUSG00000079477. ENSMUST00000113597; ENSMUSP00000109227; ENSMUSG00000079477. ENSMUST00000113598; ENSMUSP00000109228; ENSMUSG00000079477. ENSMUST00000113600; ENSMUSP00000109230; ENSMUSG00000079477.
GeneID	19349.
KEGG	mmu:19349.
Organism-specific databases
CTD	19349.
MGI	MGI:105068. Rab7.
Phylogenomic databases
HOGENOM	HBG745225.
HOVERGEN	HBG009351.
InParanoid	P51150.
OMA	SPRDPEH.
OrthoDB	EOG4QFWF4.
PhylomeDB	P51150.
Gene expression databases
ArrayExpress	P51150.
Bgee	P51150.
CleanEx	MM_RAB7.
Genevestigator	P51150.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view]
KO	K07897.
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
NextBio	296377.
SOURCE	Search...

Entry information

Entry name

RAB7A_MOUSE

Accession

Primary (citable) accession number: P51150

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	April 13, 2004
Last modified:	November 16, 2011
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program