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P35284

- RAB12_RAT

UniProt

P35284 - RAB12_RAT

Protein

Ras-related protein Rab-12

Gene

Rab12

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (06 Feb 2013)
      Previous versions | rss
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    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. GTP binding Source: RGD

    GO - Biological processi

    1. cellular protein catabolic process Source: UniProtKB
    2. endosome to lysosome transport Source: UniProtKB
    3. protein transport Source: UniProtKB-KW
    4. small GTPase mediated signal transduction Source: InterPro

    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. Golgi membrane Source: UniProtKB-SubCell
    2. lysosomal membrane Source: UniProtKB-SubCell
    3. lysosome Source: UniProtKB
    4. recycling endosome membrane Source: UniProtKB
    5. secretory granule Source: RGD

    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

    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.
    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

    MDPSAALHRR PAGGGLGAVS PALSGGQARR RKQPPRPADF KLQVIIIGSR    50
    GVGKTSLMER FTDDTFCEAC KSTVGVDFKI KTVELRGKKI RLQIWDTAGQ 100
    ERFNSITSAY YRSAKGIILV YDITKKETFD DLPKWMKMID KYASEDAELL 150
    LVGNKLDCET DREISRQQGE KFAQQITGMR FCEASAKDNF NVDEIFLKLV 200
    DDILKKMPLD VLRSELSNSI LSLQPEPEIP PELPPPRPHV RCC 243
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83676 mRNA. Translation: AAA41992.1 .
    PIRi C42148.
    RefSeqi NP_037149.1. NM_013017.1.
    UniGenei Rn.11021.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36918N.
    IntActi P35284. 1 interaction.
    STRINGi 10116.ENSRNOP00000060884.

    Proteomic databases

    PaxDbi P35284.
    PRIDEi P35284.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25530.
    KEGGi rno:25530.

    Organism-specific databases

    CTDi 201475.
    RGDi 3527. Rab12.

    Phylogenomic databases

    eggNOGi COG1100.
    HOVERGENi HBG009351.
    KOi K07907.

    Miscellaneous databases

    NextBioi 607023.

    Gene expression databases

    Genevestigatori P35284.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 107 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