P35284 (RAB12_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-12

Gene names

Name:

Rab12

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

Protein attributes

Sequence length	243 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor By similarity.
Enzyme regulation	Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP). That Rab is activated by DENND3, a guanine exchange factor By similarity.
Subcellular location	Recycling endosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Lysosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Golgi apparatus membrane By similarity.
Tissue specificity	Highest levels in skeletal and cardiac muscle. Also found in comparable amounts in brain, spinal cord and lung. Also detected in testis where it is expressed by Sertoli cells of the seminiferous tubules (at protein level). Ref.3
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endosome Golgi apparatus Lysosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Phosphoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB endosome to lysosome transport Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from sequence or structural similarity. Source: UniProtKB recycling endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB secretory granule Inferred from direct assay PubMed 8575079. Source: RGD
Molecular_function	GDP binding Inferred from sequence or structural similarity. Source: UniProtKB GTP binding Traceable author statement PubMed 8575079. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 243	243	Ras-related protein Rab-12		PRO_0000121181
Regions
	Nucleotide binding	48 – 56	9	GTP By similarity
	Nucleotide binding	96 – 100	5	GTP By similarity
	Nucleotide binding	154 – 158	5	GTP By similarity
	Nucleotide binding	186 – 187	2	GTP By similarity
	Motif	70 – 78	9	Effector region By similarity
Amino acid modifications
	Modified residue	20	1	Phosphoserine By similarity
	Modified residue	105	1	Phosphoserine By similarity
	Lipidation	242	1	S-geranylgeranyl cysteine By similarity
	Lipidation	243	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Sequence conflict	152	1	V → A in AAA41992. Ref.2
	Sequence conflict	181	1	F → L in AAA41992. Ref.2
	Sequence conflict	182	1	C → S in AAA41992. Ref.2
	Sequence conflict	184	1	A → P in AAA41992. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P35284 [UniParc]. Last modified February 6, 2013. Version 2. Checksum: 237A9421E6784584	FASTA	243	27,271
	10 20 30 40 50 60 MDPSAALHRR PAGGGLGAVS PALSGGQARR RKQPPRPADF KLQVIIIGSR GVGKTSLMER 70 80 90 100 110 120 FTDDTFCEAC KSTVGVDFKI KTVELRGKKI RLQIWDTAGQ ERFNSITSAY YRSAKGIILV 130 140 150 160 170 180 YDITKKETFD DLPKWMKMID KYASEDAELL LVGNKLDCET DREISRQQGE KFAQQITGMR 190 200 210 220 230 240 FCEASAKDNF NVDEIFLKLV DDILKKMPLD VLRSELSNSI LSLQPEPEIP PELPPPRPHV RCC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." 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. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"Rab15, a novel low molecular weight GTP-binding protein specifically expressed in rat brain." Elferink L.A., Anzai K., Scheller R.H. J. Biol. Chem. 267:5768-5775(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-243. Strain: Sprague-Dawley. Tissue: Brain.
[3]	"Identification of rab12 as a vesicle-associated small GTPase highly expressed in Sertoli cells of rat testis." Iida H., Noda M., Kaneko T., Doiguchi M., Mori T. Mol. Reprod. Dev. 71:178-185(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M83676 mRNA. Translation: AAA41992.1.
IPI	IPI00876621.
PIR	C42148.
RefSeq	NP_037149.1. NM_013017.1.
UniGene	Rn.11021.
3D structure databases
ProteinModelPortal	P35284.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35284. 1 interaction.
Proteomic databases
PaxDb	P35284.
PRIDE	P35284.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	25530.
KEGG	rno:25530.
Organism-specific databases
CTD	201475.
RGD	3527. Rab12.
Phylogenomic databases
eggNOG	COG1100.
HOVERGEN	HBG009351.
KO	K07907.
Gene expression databases
Genevestigator	P35284.
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
NextBio	607023.

Entry information

Entry name

RAB12_RAT

Accession

Primary (citable) accession number: P35284

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 6, 2013
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program