ADP-ribosylation factor-like protein 1

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Reviewed, UniProtKB/Swiss-Prot P40616 (ARL1_HUMAN)

Last modified June 16, 2009. Version 90. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
ADP-ribosylation factor-like protein 1

Gene names

Name:

ARL1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	GTP-binding protein that has very low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus. Ref.5
Subunit structure	The GTP-bound form interacts with GOLGA1 and POR1 By similarity. Interacts with SCOC. The GTP-bound form interacts with GOLGA4.
Subcellular location	Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Tissue specificity	Detected in heart, liver, lung and liver (at protein level). Detected in fetal heart, lung, liver and kidney. Detected in adult heart, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.5
Sequence similarities	Belongs to the small GTPase superfamily. Arf family.

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Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Ligand	GTP-binding Metal-binding Nucleotide-binding
PTM	Lipoprotein Myristate
Technical term	3D-structure
Gene Ontology (GO)
Biological process	small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Ref.5 Traceable author statement. Source: ProtInc enzyme activator activity Ref.5 Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDK5RAP3	Q96JB5	1	EBI-1052746,EBI-718818
RIOK3	O14730	1	EBI-1052746,EBI-1047061

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Potential

Chain

2 – 181

180

ADP-ribosylation factor-like protein 1

PRO_0000207450

Regions

Nucleotide binding

24 – 31

GTP

Nucleotide binding

45 – 48

GTP

Nucleotide binding

67 – 71

GTP By similarity

Nucleotide binding

126 – 129

GTP

Nucleotide binding

160 – 161

GTP

Sites

Metal binding

Magnesium

Metal binding

Magnesium

Binding site

GTP; via amide nitrogen

Amino acid modifications

Lipidation

N-myristoyl glycine By similarity

Secondary structure

181

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P40616-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 9FB736C8ED60DC3D
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FASTA

181

20,418

        10         20         30         40         50         60 
MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN 

        70         80         90        100        110        120 
LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI 

       130        140        150        160        170        180 
LVVFANKQDM EQAMTSSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR 


Q

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References

	« Hide 'large scale' referencesShow '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]	"Different ARF domains are required for the activation of cholera toxin and phospholipase D." Zhang G.-F., Patton W.A., Lee F.-J.S., Liyange M., Han J.-S., Rhee S.G., Moss J., Vaughan M. J. Biol. Chem. 270:21-24(1995) [PubMed: 7814376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Urinary bladder.
[5]	"Phospholipid- and GTP-dependent activation of cholera toxin and phospholipase D by human ADP-ribosylation factor-like protein 1 (HARL1)." Hong J.-X., Lee F.-J.S., Patton W.A., Lin C.Y., Moss J., Vaughan M. J. Biol. Chem. 273:15872-15876(1998) [PubMed: 9624189] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]	"ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins." Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A. J. Biol. Chem. 276:22826-22837(2001) [PubMed: 11303027] [Abstract] Cited for: INTERACTION WITH SCOC.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus." Panic B., Perisic O., Veprintsev D.B., Williams R.L., Munro S. Mol. Cell 12:863-874(2003) [PubMed: 14580338] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-181 IN COMPLEX WITH MAGNESIUM; GTP AND GOLGA4.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

L28997 mRNA. Translation: AAC37567.1.
AF493887 mRNA. Translation: AAM12601.1.
BC007000 mRNA. Translation: AAH07000.1.

IPI

IPI00219518.

RefSeq

NP_001168.1.

UniGene

Hs.372616

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UPT	X-ray	1.70	A/C/E/G	15-181	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P40616. 10 interactions.

Proteomic databases

PRIDE

P40616.

Genome annotation databases

Ensembl

ENSG00000120805. Homo sapiens. [Contig view]

GeneID

400.

KEGG

hsa:400.

Organism-specific databases

GeneCards

GC12M100289.

H-InvDB

HIX0010921.

HGNC

HGNC:692. ARL1.

MIM

603425. gene.

PharmGKB

PA24985.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P40616.

HOVERGEN

P40616.

Gene expression databases

ArrayExpress

P40616.

Bgee

P40616.

CleanEx

HS_ARL1.

GermOnline

ENSG00000120805. Homo sapiens.

Family and domain databases

InterPro

IPR006688. ARF.
IPR006689. ARF/SAR.
IPR005225. Small_GTP_bd.
[Graphical view]

PANTHER

PTHR11711. ARF/SAR. 1 hit.

Pfam

PF00025. Arf. 1 hit.
[Graphical view]

PRINTS

PR00328. SAR1GTPBP.

SMART

SM00177. ARF. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51417. ARF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

1677.

SOURCE

Search...

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Entry information

Entry name

ARL1_HUMAN

Accession

Primary (citable) accession number: P40616
Secondary accession number(s): P80417

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents