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P35293 (RAB18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-18
Gene names
Name:Rab18
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a role in apical endocytosis/recycling. May be implicated in transport between the plasma membrane and early endosomes. Plays a key role in eye and brain development and neurodegeneration By similarity.

Subcellular location

Apical cell membrane; Lipid-anchor Potential. Basal cell membrane; Lipid-anchor Potential. Note: Highly enriched on apical endocytic structures in polarized epithelial cells of kidney proximal tubules. Detected on both the apical and basolateral domains in epithelial cells of the intestine.

Tissue specificity

Expression is high in the brain, moderate in the pituitary, and low in the liver. Detected in all tissues.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 203203Ras-related protein Rab-18
PRO_0000121194
Propeptide204 – 2063Removed in mature form Potential
PRO_0000370762

Regions

Nucleotide binding15 – 239GTP By similarity
Nucleotide binding63 – 675GTP By similarity
Nucleotide binding122 – 1254GTP By similarity
Nucleotide binding151 – 1533GTP By similarity
Motif37 – 459Effector region By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2031Cysteine methyl ester Potential
Lipidation1991S-palmitoyl cysteine Potential
Lipidation2031S-geranylgeranyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P35293 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: D1B0F48666999B77

FASTA20623,035
        10         20         30         40         50         60 
MDEDVLTTLK ILIIGESGVG KSSLLLRFTD DTFDPELAAT IGVDFKVKTI SVDGNKAKLA 

        70         80         90        100        110        120 
IWDTAGQERF RTLTPSYYRG AQGVILVYDV TRRDTFVKLD NWLNELETYC TRNDIVNMLV 

       130        140        150        160        170        180 
GNKIDKENRE VDRNEGLKFA RKHSMLFIEA SAKTCDGVQC AFEELVEKII QTPGLWESEN 

       190        200 
QNKGVKLSHR EESRGGGACG GYCSVL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and subcellular localization of novel rab proteins reveals polarized and cell type-specific expression."
Luetcke A., Parton R.G., Murphy C., Olkkonen V.M., Dupree P., Valencia A., Simons K., Zerial M.
J. Cell Sci. 107:3437-3448(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"Gene cloning and characterization of a GTP-binding Rab protein from mouse pituitary AtT-20 cells."
Yu H., Leaf D.S., Moore H.P.
Gene 132:273-278(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: LAF1.
Tissue: Pituitary.
[3]"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. expand/collapse author list , 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, DBA/2 and NOD.
Tissue: Corpora quadrigemina, Head and Spleen.
[4]"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].
Strain: C57BL/6.
Tissue: Brain.
[5]"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 1-68.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80333 mRNA. Translation: CAA56583.1.
L04966 mRNA. Translation: AAC37632.1.
AK045514 mRNA. Translation: BAC32402.1.
AK140901 mRNA. Translation: BAE24512.1.
AK143673 mRNA. Translation: BAE25489.1.
AK146177 mRNA. Translation: BAE26955.1.
AK146397 mRNA. Translation: BAE27140.1.
AK154920 mRNA. Translation: BAE32926.1.
BC056351 mRNA. Translation: AAH56351.1.
M79308 mRNA. Translation: AAK14832.1.
CCDSCCDS29044.1.
PIRJN0874.
RefSeqNP_851415.1. NM_181070.6.
UniGeneMm.132802.

3D structure databases

ProteinModelPortalP35293.
SMRP35293. Positions 2-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202536. 1 interaction.
IntActP35293. 1 interaction.
MINTMINT-1864434.

PTM databases

PhosphoSiteP35293.

Proteomic databases

MaxQBP35293.
PaxDbP35293.
PRIDEP35293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097680; ENSMUSP00000095285; ENSMUSG00000073639.
GeneID19330.
KEGGmmu:19330.
UCSCuc008dzo.1. mouse.

Organism-specific databases

CTD22931.
MGIMGI:102790. Rab18.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP35293.
KOK07910.
OMATYTTRND.
OrthoDBEOG7CVQ04.
PhylomeDBP35293.
TreeFamTF313448.

Gene expression databases

ArrayExpressP35293.
BgeeP35293.
CleanExMM_RAB18.
GenevestigatorP35293.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR025662. Sigma_54_int_dom_ATP-bd_1.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296305.
PROP35293.
SOURCESearch...

Entry information

Entry nameRAB18_MOUSE
AccessionPrimary (citable) accession number: P35293
Secondary accession number(s): Q543V0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot