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Protein

Ras-related protein Rab-12

Gene

Rab12

Organism
Rattus norvegicus (Rat)
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 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. Involved in autophagy (By similarity).By similarity

Enzyme regulationi

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 569GTPBy similarity
Nucleotide bindingi96 – 1005GTPBy similarity
Nucleotide bindingi154 – 1585GTPBy similarity
Nucleotide bindingi186 – 1872GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: GO_Central
  3. GTP binding Source: RGD

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. cellular protein catabolic process Source: UniProtKB
  3. endosome to lysosome transport Source: UniProtKB
  4. GTP catabolic process Source: GO_Central
  5. intracellular protein transport Source: GO_Central
  6. positive regulation of macroautophagy Source: Ensembl
  7. protein localization to plasma membrane Source: GO_Central
  8. protein secretion Source: GO_Central
  9. Rab protein signal transduction Source: GO_Central
  10. regulation of exocytosis Source: GO_Central
  11. vesicle docking involved in exocytosis Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-12
Gene namesi
Name:Rab12
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3527. Rab12.

Subcellular locationi

Recycling endosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Lysosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Golgi apparatus membrane By similarity. Cytoplasmic vesicleautophagosome By similarity

GO - Cellular componenti

  1. autophagic vacuole Source: UniProtKB-SubCell
  2. endosome membrane Source: GO_Central
  3. Golgi apparatus Source: GO_Central
  4. Golgi membrane Source: UniProtKB-SubCell
  5. lysosomal membrane Source: UniProtKB-SubCell
  6. lysosome Source: UniProtKB
  7. recycling endosome membrane Source: UniProtKB
  8. secretory granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Golgi apparatus, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243Ras-related protein Rab-12PRO_0000121181Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei105 – 1051PhosphoserineBy similarity
Lipidationi242 – 2421S-geranylgeranyl cysteineBy similarity
Lipidationi243 – 2431S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP35284.
PRIDEiP35284.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

ExpressionAtlasiP35284. baseline.
GenevestigatoriP35284.

Interactioni

Subunit structurei

Interacts with RABIF and OPTN.By similarity

Protein-protein interaction databases

DIPiDIP-36918N.
IntActiP35284. 1 interaction.
STRINGi10116.ENSRNOP00000060884.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi70 – 789Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
HOVERGENiHBG009351.
InParanoidiP35284.
KOiK07907.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35284-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPSAALHRR PAGGGLGAVS PALSGGQARR RKQPPRPADF KLQVIIIGSR
60 70 80 90 100
GVGKTSLMER FTDDTFCEAC KSTVGVDFKI KTVELRGKKI RLQIWDTAGQ
110 120 130 140 150
ERFNSITSAY YRSAKGIILV YDITKKETFD DLPKWMKMID KYASEDAELL
160 170 180 190 200
LVGNKLDCET DREISRQQGE KFAQQITGMR FCEASAKDNF NVDEIFLKLV
210 220 230 240
DDILKKMPLD VLRSELSNSI LSLQPEPEIP PELPPPRPHV RCC
Length:243
Mass (Da):27,271
Last modified:February 6, 2013 - v2
Checksum:i237A9421E6784584
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521V → A in AAA41992 (PubMed:1313420).Curated
Sequence conflicti181 – 1811F → L in AAA41992 (PubMed:1313420).Curated
Sequence conflicti182 – 1821C → S in AAA41992 (PubMed:1313420).Curated
Sequence conflicti184 – 1841A → P in AAA41992 (PubMed:1313420).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83676 mRNA. Translation: AAA41992.1.
PIRiC42148.
RefSeqiNP_037149.1. NM_013017.1.
UniGeneiRn.11021.

Genome annotation databases

GeneIDi25530.
KEGGirno:25530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83676 mRNA. Translation: AAA41992.1.
PIRiC42148.
RefSeqiNP_037149.1. NM_013017.1.
UniGeneiRn.11021.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36918N.
IntActiP35284. 1 interaction.
STRINGi10116.ENSRNOP00000060884.

Proteomic databases

PaxDbiP35284.
PRIDEiP35284.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25530.
KEGGirno:25530.

Organism-specific databases

CTDi201475.
RGDi3527. Rab12.

Phylogenomic databases

eggNOGiCOG1100.
HOVERGENiHBG009351.
InParanoidiP35284.
KOiK07907.

Miscellaneous databases

NextBioi607023.

Gene expression databases

ExpressionAtlasiP35284. baseline.
GenevestigatoriP35284.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 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. "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.

Entry informationi

Entry nameiRAB12_RAT
AccessioniPrimary (citable) accession number: P35284
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 6, 2013
Last modified: March 4, 2015
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.