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P35292

- RAB17_MOUSE

UniProt

P35292 - RAB17_MOUSE

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Protein
Ras-related protein Rab-17
Gene
Rab17
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 is involved in transcytosis, the directed movement of endocytosed material through the cell and its exocytosis from the plasma membrane at the opposite side. Mainly observed in epithelial cells, transcytosis mediates for instance, the transcellular transport of immunoglobulins from the basolateral surface to the apical surface. Most probably controls membrane trafficking through apical recycling endosomes in a post-endocytic step of transcytosis. Required for melanosome transport and release from melanocytes, it also regulates dendrite and dendritic spine development. May also play a role in cell migration.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338GTP By similarity
Nucleotide bindingi73 – 775GTP By similarity
Nucleotide bindingi132 – 1354GTP By similarity

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW
  3. protein binding Source: MGI

GO - Biological processi

  1. endocytic recycling Source: UniProtKB
  2. establishment of melanosome localization Source: UniProtKB
  3. filopodium assembly Source: UniProtKB
  4. immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor Source: UniProtKB
  5. melanosome transport Source: UniProtKB
  6. protein transport Source: UniProtKB-KW
  7. regulation of dendrite development Source: UniProtKB
  8. regulation of filopodium assembly Source: UniProtKB
  9. regulation of synapse assembly Source: UniProtKB
  10. small GTPase mediated signal transduction Source: InterPro
  11. transcytosis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-17
Gene namesi
Name:Rab17
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:104640. Rab17.

Subcellular locationi

Recycling endosome membrane; Lipid-anchor; Cytoplasmic side. Cell projectiondendrite
Note: According to a report the protein is localized at the basolateral and apical plasma membrane of kidney epithelial cells (1 Publication). It was later shown to localize to the apical recycling endosome in epithelial cells (1 Publication). In neurons, localizes to the cell body and dendritic shaft and spine.5 Publications

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. basolateral plasma membrane Source: UniProtKB
  3. dendrite Source: UniProtKB
  4. melanosome Source: UniProtKB
  5. neuronal cell body Source: UniProtKB
  6. recycling endosome Source: UniProtKB
  7. recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi77 – 771Q → L: Probable constitutively active mutant unable to hydrolyze GTP; increases dendrite number and length. 2 Publications
Mutagenesisi211 – 2122CC → AA: Loss of association with membranes and redistribution to the cytosol. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 214214Ras-related protein Rab-17
PRO_0000121192Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi211 – 2111S-geranylgeranyl cysteine1 Publication
Lipidationi212 – 2121S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

MaxQBiP35292.
PaxDbiP35292.
PRIDEiP35292.

PTM databases

PhosphoSiteiP35292.

Expressioni

Tissue specificityi

Expressed in kidney, liver, and intestine mainly by epithelial cells. Expressed in hippocampus (at protein level).2 Publications

Developmental stagei

Expression starts at E5 and gradually increases from P5 to adulthood (at protein level).1 Publication

Gene expression databases

ArrayExpressiP35292.
BgeeiP35292.
CleanExiMM_RAB17.
GenevestigatoriP35292.

Interactioni

Protein-protein interaction databases

BioGridi202535. 2 interactions.
MINTiMINT-1340501.

Structurei

3D structure databases

ProteinModelPortaliP35292.
SMRiP35292. Positions 21-207.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi47 – 559Effector region By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP35292.
KOiK07909.
OMAiSVCHLYY.
OrthoDBiEOG7J9VQP.
PhylomeDBiP35292.
TreeFamiTF300199.

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.

P35292-1 [UniParc]FASTAAdd to Basket

« Hide

MAQAAGLPQA STASGQPYVS KLVLLGSSSV GKTSLALRYM KQDFSNVLPT    50
VGCAFFTKVL DLGSSSLKLE IWDTAGQEKY QSVCHLYFRG ANAALLVYDI 100
TRKDSFHKAQ QWLEDLEKEF QPGEVVVMLV GNKTDLGEER EVTFQEGKEF 150
AESKSLLFME TSAKLNYQVS EIFNTVAQEL LQRAGDTGSS RPQEGEAVAL 200
NQEPPIRQRQ CCAR 214
Length:214
Mass (Da):23,640
Last modified:February 1, 1994 - v1
Checksum:i11052D3EC730EFAB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191V → L in BAC35842. 1 Publication
Sequence conflicti57 – 571T → K in BAB26452. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70804 mRNA. Translation: CAA50071.1.
AK009707 mRNA. Translation: BAB26452.1.
AK075591 mRNA. Translation: BAC35842.1.
BC013170 mRNA. Translation: AAH13170.1.
BC051071 mRNA. Translation: AAH51071.1.
M79307 mRNA. Translation: AAK14831.1.
CCDSiCCDS15156.1.
PIRiA46434.
RefSeqiNP_001153197.2. NM_001159725.2.
NP_033024.1. NM_008998.4.
XP_006529326.1. XM_006529263.1.
UniGeneiMm.279780.

Genome annotation databases

EnsembliENSMUST00000027529; ENSMUSP00000027529; ENSMUSG00000026304.
ENSMUST00000131428; ENSMUSP00000122178; ENSMUSG00000026304.
GeneIDi19329.
KEGGimmu:19329.
UCSCiuc007bzn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70804 mRNA. Translation: CAA50071.1 .
AK009707 mRNA. Translation: BAB26452.1 .
AK075591 mRNA. Translation: BAC35842.1 .
BC013170 mRNA. Translation: AAH13170.1 .
BC051071 mRNA. Translation: AAH51071.1 .
M79307 mRNA. Translation: AAK14831.1 .
CCDSi CCDS15156.1.
PIRi A46434.
RefSeqi NP_001153197.2. NM_001159725.2.
NP_033024.1. NM_008998.4.
XP_006529326.1. XM_006529263.1.
UniGenei Mm.279780.

3D structure databases

ProteinModelPortali P35292.
SMRi P35292. Positions 21-207.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202535. 2 interactions.
MINTi MINT-1340501.

PTM databases

PhosphoSitei P35292.

Proteomic databases

MaxQBi P35292.
PaxDbi P35292.
PRIDEi P35292.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027529 ; ENSMUSP00000027529 ; ENSMUSG00000026304 .
ENSMUST00000131428 ; ENSMUSP00000122178 ; ENSMUSG00000026304 .
GeneIDi 19329.
KEGGi mmu:19329.
UCSCi uc007bzn.2. mouse.

Organism-specific databases

CTDi 64284.
MGIi MGI:104640. Rab17.

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi P35292.
KOi K07909.
OMAi SVCHLYY.
OrthoDBi EOG7J9VQP.
PhylomeDBi P35292.
TreeFami TF300199.

Miscellaneous databases

NextBioi 296301.
PROi P35292.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35292.
Bgeei P35292.
CleanExi MM_RAB17.
Genevestigatori P35292.

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

« Hide 'large scale' publications
  1. "Rab17, a novel small GTPase, is specific for epithelial cells and is induced during cell polarization."
    Luetcke A., Jansson S., Parton R.G., Chavrier P., Valencia A., Huber L.A., Lehtonen E., Zerial M.
    J. Cell Biol. 121:553-564(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Kidney.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney and Tongue.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Olfactory epithelium.
  4. "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed by a PCR cloning approach."
    Chavrier P., Simons K., Zerial M.
    Gene 112:261-264(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-78.
    Tissue: Kidney.
  5. "Rab17 localizes to recycling endosomes and regulates receptor-mediated transcytosis in epithelial cells."
    Hunziker W., Peters P.J.
    J. Biol. Chem. 273:15734-15741(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCYTOSIS, SUBCELLULAR LOCATION, TOPOLOGY, ISOPRENYLATION AT CYS-211 AND CYS-212, MUTAGENESIS OF 211-CYS-CYS-212.
  6. "Rab17 regulates membrane trafficking through apical recycling endosomes in polarized epithelial cells."
    Zacchi P., Stenmark H., Parton R.G., Orioli D., Lim F., Giner A., Mellman I., Zerial M., Murphy C.
    J. Cell Biol. 140:1039-1053(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "The recycling endosome protein Rab17 regulates melanocytic filopodia formation and melanosome trafficking."
    Beaumont K.A., Hamilton N.A., Moores M.T., Brown D.L., Ohbayashi N., Cairncross O., Cook A.L., Smith A.G., Misaki R., Fukuda M., Taguchi T., Sturm R.A., Stow J.L.
    Traffic 12:627-643(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MELANOSOME TRANSPORT, SUBCELLULAR LOCATION.
  8. "Small GTPase Rab17 regulates dendritic morphogenesis and postsynaptic development of hippocampal neurons."
    Mori Y., Matsui T., Furutani Y., Yoshihara Y., Fukuda M.
    J. Biol. Chem. 287:8963-8973(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DENDRITOGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLN-77.

Entry informationi

Entry nameiRAB17_MOUSE
AccessioniPrimary (citable) accession number: P35292
Secondary accession number(s): Q921D2, Q9D723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 128 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi