Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ras-related protein Rab-17

Gene

Rab17

Organism
Mus musculus (Mouse)
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 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 – 338GTPBy similarity
Nucleotide bindingi73 – 775GTPBy similarity
Nucleotide bindingi132 – 1354GTPBy similarity

GO - Molecular functioni

GO - Biological processi

  • cilium assembly Source: MGI
  • endocytic recycling Source: UniProtKB
  • establishment of melanosome localization Source: UniProtKB
  • filopodium assembly Source: UniProtKB
  • immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor Source: UniProtKB
  • intracellular protein transport Source: GO_Central
  • melanosome transport Source: UniProtKB
  • metabolic process Source: MGI
  • Rab protein signal transduction Source: GO_Central
  • regulation of dendrite development Source: UniProtKB
  • regulation of endocytosis Source: GO_Central
  • regulation of filopodium assembly Source: UniProtKB
  • regulation of synapse assembly Source: UniProtKB
  • 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 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:104640. Rab17.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB
  • dendrite Source: UniProtKB
  • endocytic vesicle Source: MGI
  • extracellular exosome Source: MGI
  • intracellular Source: MGI
  • melanosome Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • plasma membrane Source: GO_Central
  • recycling endosome Source: UniProtKB
  • 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. 1 Publication
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-17PRO_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

BgeeiP35292.
CleanExiMM_RAB17.
ExpressionAtlasiP35292. baseline and differential.
GenevisibleiP35292. MM.

Interactioni

Protein-protein interaction databases

BioGridi202535. 2 interactions.
MINTiMINT-1340501.
STRINGi10090.ENSMUSP00000027529.

Structurei

3D structure databases

ProteinModelPortaliP35292.
SMRiP35292. Positions 21-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

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

        10         20         30         40         50
MAQAAGLPQA STASGQPYVS KLVLLGSSSV GKTSLALRYM KQDFSNVLPT
60 70 80 90 100
VGCAFFTKVL DLGSSSLKLE IWDTAGQEKY QSVCHLYFRG ANAALLVYDI
110 120 130 140 150
TRKDSFHKAQ QWLEDLEKEF QPGEVVVMLV GNKTDLGEER EVTFQEGKEF
160 170 180 190 200
AESKSLLFME TSAKLNYQVS EIFNTVAQEL LQRAGDTGSS RPQEGEAVAL
210
NQEPPIRQRQ CCAR
Length:214
Mass (Da):23,640
Last modified:February 1, 1994 - v1
Checksum:i11052D3EC730EFAB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191V → L in BAC35842 (PubMed:15489334).Curated
Sequence conflicti57 – 571T → K in BAB26452 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006529263.2.
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:
EMBLi
GenBanki
DDBJi
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_006529263.2.
UniGeneiMm.279780.

3D structure databases

ProteinModelPortaliP35292.
SMRiP35292. Positions 21-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202535. 2 interactions.
MINTiMINT-1340501.
STRINGi10090.ENSMUSP00000027529.

PTM databases

PhosphoSiteiP35292.

Proteomic databases

MaxQBiP35292.
PaxDbiP35292.
PRIDEiP35292.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi64284.
MGIiMGI:104640. Rab17.

Phylogenomic databases

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

Miscellaneous databases

NextBioi296301.
PROiP35292.
SOURCEiSearch...

Gene expression databases

BgeeiP35292.
CleanExiMM_RAB17.
ExpressionAtlasiP35292. baseline and differential.
GenevisibleiP35292. MM.

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. "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: June 24, 2015
This is version 137 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

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.