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P49703 (ARL4D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. 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 4D
Alternative name(s):
ADP-ribosylation factor-like protein 4L
Gene names
Name:ARL4D
Synonyms:ARF4L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 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.8

Subunit structure

Interacts with CYTH2; the interaction is direct and ARL4D GTP-dependent. Does not interact with ARL4D. Ref.7 Ref.8

Subcellular location

Nucleusnucleolus By similarity. Cell membrane. Nucleus. Cytoplasm Ref.8.

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_0000207464

Regions

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

Amino acid modifications

Lipidation21N-myristoyl glycine Potential

Natural variations

Natural variant911T → N. Ref.1
Corresponds to variant rs1059968 [ dbSNP | Ensembl ].
VAR_028205

Sequences

Sequence LengthMass (Da)Tools
P49703 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 18766BCF56A8127D

FASTA20122,156
        10         20         30         40         50         60 
MGNHLTEMAP TASSFLPHFQ ALHVVVIGLD SAGKTSLLYR LKFKEFVQSV PTKGFNTEKI 

        70         80         90        100        110        120 
RVPLGGSRGI TFQVWDVGGQ EKLRPLWRSY TRRTDGLVFV VDAAEAERLE EAKVELHRIS 

       130        140        150        160        170        180 
RASDNQGVPV LVLANKQDQP GALSAAEVEK RLAVRELAAA TLTHVQGCSA VDGLGLQQGL 

       190        200 
ERLYEMILKR KKAARGGKKR R 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and mapping of a gene encoding a novel human ADP-ribosylation factor on chromosome 17q12-q21."
Smith S.A., Holik P.R., Stevens J., Melis R., White R., Albertsen H.
Genomics 28:113-115(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-91.
Tissue: Retina.
[2]"Comparison of the positional cloning methods used to isolate the BRCA1 gene."
Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J., Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H., Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S. expand/collapse author list , Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H., Shattuck-Eidens D., Kamb A.
Hum. Mol. Genet. 4:1259-1266(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[3]"Two brain-related proteins are a tumor-rejection antigen recognized by HLA-A2-restriction."
Tuda N., Shichijo S., Itoh K.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Brain.
[7]"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] [Europe PMC] [Abstract]
Cited for: ABSENCE OF INTERACTION WITH ARL4D.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CYTH2, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L38490 mRNA. Translation: AAA57126.1.
U25771 mRNA. Translation: AAA93229.1.
AB060692 mRNA. Translation: BAB91080.1.
AK314951 mRNA. Translation: BAG37456.1.
CH471178 Genomic DNA. Translation: EAW51681.1.
CH471178 Genomic DNA. Translation: EAW51682.1.
BC000043 mRNA. Translation: AAH00043.1.
PIRA57646.
RefSeqNP_001652.2. NM_001661.3.
UniGeneHs.183153.
Hs.709866.

3D structure databases

ProteinModelPortalP49703.
SMRP49703. Positions 22-183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106874. 14 interactions.
IntActP49703. 14 interactions.
MINTMINT-1371837.

PTM databases

PhosphoSiteP49703.

Polymorphism databases

DMDM116241256.

Proteomic databases

PaxDbP49703.
PRIDEP49703.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320033; ENSP00000322628; ENSG00000175906.
GeneID379.
KEGGhsa:379.
UCSCuc002idt.3. human.

Organism-specific databases

CTD379.
GeneCardsGC17P041476.
HGNCHGNC:656. ARL4D.
HPAHPA060379.
MIM600732. gene.
neXtProtNX_P49703.
PharmGKBPA24938.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000163691.
HOVERGENHBG002073.
InParanoidP49703.
KOK07945.
OMAITRTSEN.
OrthoDBEOG7H793N.
PhylomeDBP49703.
TreeFamTF105464.

Enzyme and pathway databases

SignaLinkP49703.

Gene expression databases

BgeeP49703.
CleanExHS_ARL4D.
GenevestigatorP49703.

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

GeneWikiARL4D.
GenomeRNAi379.
NextBio1589.
PROP49703.
SOURCESearch...

Entry information

Entry nameARL4D_HUMAN
AccessionPrimary (citable) accession number: P49703
Secondary accession number(s): B2RC59, D3DX43
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 134 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM