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P40617 (ARL4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 4A
Gene names
Name:ARL4A
Synonyms:ARL4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.9 Ref.11

Subunit structure

Interacts with CYTH2. Interacts with KPNA2; the interaction is direct. Does not interacts with ARL4A. Ref.9 Ref.10 Ref.11

Subcellular location

Cell membrane. Cytoplasm. Nucleusnucleolus. Note: Localization in the nucleolus is dependent by nucleotide binding. Ref.8 Ref.9 Ref.11

Post-translational modification

Myristoylated.

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Myristate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processsmall GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay Ref.9. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular functionGTP binding

Inferred from direct assay Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9Ref.11. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 200199ADP-ribosylation factor-like protein 4A
PRO_0000207459

Regions

Nucleotide binding27 – 348GTP By similarity
Nucleotide binding75 – 795GTP By similarity
Nucleotide binding134 – 1374GTP By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine Potential

Natural variations

Natural variant1391R → K.
Corresponds to variant rs2953325 [ dbSNP | Ensembl ].
VAR_024367

Experimental info

Mutagenesis341T → N: Inhibits relocalization of CYTH2 to the plasma membrane. Strongly localized in the nucleolus. Ref.9 Ref.11
Mutagenesis791Q → L: Localized in the nucleus and nucleolus. Ref.9 Ref.11

Sequences

Sequence LengthMass (Da)Tools
P40617 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 8D93A8C003BD16CF

FASTA20022,615
        10         20         30         40         50         60 
MGNGLSDQTS ILSNLPSFQS FHIVILGLDC AGKTTVLYRL QFNEFVNTVP TKGFNTEKIK 

        70         80         90        100        110        120 
VTLGNSKTVT FHFWDVGGQE KLRPLWKSYT RCTDGIVFVV DSVDVERMEE AKTELHKITR 

       130        140        150        160        170        180 
ISENQGVPVL IVANKQDLRN SLSLSEIEKL LAMGELSSST PWHLQPTCAI IGDGLKEGLE 

       190        200 
KLHDMIIKRR KMLRQQKKKR 

« Hide

References

« Hide 'large scale' references
[1]Rosenwald A.G., Kahn R.A.
Submitted (JAN-1995) to UniProtKB
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Umbilical vein endothelial cell.
[2]Choe I.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed: 12690205] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Melanoma.
[8]"ADP-ribosylation factor (ARF)-like 4, 6, and 7 represent a subgroup of the ARF family characterization by rapid nucleotide exchange and a nuclear localization signal."
Jacobs S., Schilf C., Fliegert F., Koling S., Weber Y., Schurmann A., Joost H.-G.
FEBS Lett. 456:384-388(1999) [PubMed: 10462049] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli."
Lin C.Y., Huang P.H., Liao W.L., Cheng H.J., Huang C.F., Kuo J.C., Patton W.A., Massenburg D., Moss J., Lee F.J.
J. Biol. Chem. 275:37815-37823(2000) [PubMed: 10980193] [Abstract]
Cited for: FUNCTION, MYRISTOYLATION, INTERACTION WITH KPNA2, MUTAGENESIS OF THR-34 AND GLN-79, SUBCELLULAR LOCATION.
[10]"ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin."
Bhamidipati A., Lewis S.A., Cowan N.J.
J. Cell Biol. 149:1087-1096(2000) [PubMed: 10831612] [Abstract]
Cited for: ABSENCE OF INTERACTION WITH ARL4A.
[11]"The Arl4 family of small G proteins can recruit the cytohesin Arf6 exchange factors to the plasma membrane."
Hofmann I., Thompson A., Sanderson C.M., Munro S.
Curr. Biol. 17:711-716(2007) [PubMed: 17398095] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CYTH2, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-34 AND GLN-79.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73960 mRNA. Translation: AAB39713.1.
AK313233 mRNA. Translation: BAG36044.1.
AF493890 mRNA. Translation: AAM12604.1.
CH236948 Genomic DNA. Translation: EAL24295.1.
CH471073 Genomic DNA. Translation: EAW93650.1.
BC001111 mRNA. Translation: AAH01111.1.
BC003027 mRNA. Translation: AAH03027.1.
IPIIPI00029596.
RefSeqNP_001032241.1. NM_001037164.2.
NP_001182325.1. NM_001195396.1.
NP_005729.1. NM_005738.4.
NP_997625.1. NM_212460.3.
UniGeneHs.245540.
Hs.729252.

3D structure databases

ProteinModelPortalP40617.
SMRP40617. Positions 15-187.
ModBaseSearch...

Protein-protein interaction databases

IntActP40617. 1 interaction.
STRINGP40617.

Polymorphism databases

DMDM1168495.

Proteomic databases

PRIDEP40617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356797; ENSP00000349250; ENSG00000122644.
ENST00000396662; ENSP00000379897; ENSG00000122644.
ENST00000396663; ENSP00000379898; ENSG00000122644.
ENST00000396664; ENSP00000379899; ENSG00000122644.
ENST00000404894; ENSP00000385236; ENSG00000122644.
GeneID10124.
KEGGhsa:10124.
UCSCuc003ssp.1. human.

Organism-specific databases

CTD10124.
GeneCardsGC07P012726.
H-InvDBHIX0006491.
HGNCHGNC:695. ARL4A.
MIM604786. gene.
neXtProtNX_P40617.
PharmGKBPA24988.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00600000084228.
HOGENOMHBG745225.
HOVERGENHBG002073.
InParanoidP40617.
OMACFHIVIL.
OrthoDBEOG483D5M.
PhylomeDBP40617.

Gene expression databases

ArrayExpressP40617.
BgeeP40617.
CleanExHS_ARL4A.
GenevestigatorP40617.
GermOnlineENSG00000122644. Homo sapiens.

Family and domain databases

InterProIPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
KOK07945.
PANTHERPTHR11711. ARF/SAR. 1 hit.
PfamPF00025. Arf. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00177. ARF. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. Small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio38291.
SOURCESearch...

Entry information

Entry nameARL4A_HUMAN
AccessionPrimary (citable) accession number: P40617
Secondary accession number(s): A4D119, P80418, Q49AF5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families