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Q99PE9 (ARL4D_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. 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:
ADP-ribosylation factor-like protein 4D
Alternative name(s):
ADP-ribosylation factor-like protein 4L
ADP-ribosylation factor-like protein 5
Gene names
Name:Arl4d
Synonyms:Arf4l, Arl5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form By similarity.

Subunit structure

Interacts with CYTH2; the interaction is direct and ARL4D GTP-dependent. Does not interact with ARL4D By similarity.

Subcellular location

Nucleusnucleolus By similarity. Cell membrane. Nucleus By similarity. Cytoplasm By similarity Ref.1.

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 201200ADP-ribosylation factor-like protein 4D
PRO_0000207465

Regions

Nucleotide binding28 – 358GTP By similarity
Nucleotide binding76 – 805GTP By similarity
Nucleotide binding135 – 1384GTP By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine Potential

Experimental info

Sequence conflict71E → D in AAG53667. Ref.1
Sequence conflict1061T → I in AAG53667. Ref.1
Sequence conflict113 – 1142RM → KV in AAG53667. Ref.1
Sequence conflict1671G → A in AAG53667. Ref.1
Sequence conflict1781P → Q in AAG53667. Ref.1
Sequence conflict1821H → R in AAG53667. Ref.1
Sequence conflict1961S → G in AAG53667. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99PE9 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: A6462A22B3AD451A

FASTA20122,270
        10         20         30         40         50         60 
MGNHLTEMAP TASSFLPHFQ ALHVVVIGLD SAGKTSLLYR LKFKEFVQSV PTKGFNTEKI 

        70         80         90        100        110        120 
RVPLGGSRGI TFQVWDVGGQ EKLRPLWRSY TRRTDGLVFV VDSAETERLE EARMELHRIS 

       130        140        150        160        170        180 
KASDNQGVPV LVLANKQDQP GALSAAEVEK RLAVRELAAA TLTHVQGCSA VDGLGLQPGL 

       190        200 
EHLYEMILKR KKAPRSSKKR R 

« Hide

References

« Hide 'large scale' references
[1]"A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1."
Lin C.-Y., Li C.-C., Huang P.-H., Lee F.-J.S.
J. Cell Sci. 115:4433-4445(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Strain: BALB/c.
Tissue: Liver.
[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. 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.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF312686 mRNA. Translation: AAG53667.1.
AK004126 mRNA. Translation: BAB23183.1.
AK013320 mRNA. Translation: BAB28789.1.
AL590994 Genomic DNA. Translation: CAM22640.1.
CH466558 Genomic DNA. Translation: EDL34064.1.
BC016113 mRNA. Translation: AAH16113.1.
RefSeqNP_079680.1. NM_025404.3.
UniGeneMm.266840.

3D structure databases

ProteinModelPortalQ99PE9.
SMRQ99PE9. Positions 22-183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1340386.

PTM databases

PhosphoSiteQ99PE9.

Proteomic databases

PRIDEQ99PE9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000039388; ENSMUSP00000035918; ENSMUSG00000034936.
GeneID80981.
KEGGmmu:80981.
UCSCuc007lpq.2. mouse.

Organism-specific databases

CTD379.
MGIMGI:1933155. Arl4d.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00750000117434.
HOGENOMHOG000163691.
HOVERGENHBG002073.
InParanoidQ99PE9.
KOK07945.
OMAITRTSEN.
OrthoDBEOG7H793N.
TreeFamTF105464.

Gene expression databases

CleanExMM_ARL4D.
GenevestigatorQ99PE9.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamPF00025. Arf. 1 hit.
[Graphical view]
PRINTSPR00328. SAR1GTPBP.
SMARTSM00177. ARF. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio350314.
PROQ99PE9.
SOURCESearch...

Entry information

Entry nameARL4D_MOUSE
AccessionPrimary (citable) accession number: Q99PE9
Secondary accession number(s): Q9CQB1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 86 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