P40616 (ARL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

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

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.9
Subunit structure	The GTP-bound form interacts with GOLGA1 and POR1 By similarity. Interacts with SCOC. The GTP-bound form interacts with GOLGA4. Ref.10
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.9
Sequence similarities	Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Ligand	GTP-binding Metal-binding Nucleotide-binding
PTM	Lipoprotein Myristate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Golgi organization Inferred from sequence or structural similarity. Source: UniProtKB activation of phospholipase D activity Inferred from direct assay Ref.9. Source: UniProtKB protein localization in Golgi apparatus Inferred from mutant phenotype. Source: UniProtKB retrograde transport, endosome to Golgi Inferred from mutant phenotype. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro toxin metabolic process Inferred from direct assay Ref.9. Source: UniProtKB
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	GTP binding Inferred from direct assay Ref.9. Source: UniProtKB GTPase activity Inferred from direct assay Ref.9. Source: UniProtKB enzyme activator activity Inferred from direct assay Ref.9. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein domain specific binding Inferred from physical interaction Ref.12. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Potential

Chain

2 – 181

180

ADP-ribosylation factor-like protein 1

PRO_0000207450

Regions

Nucleotide binding

24 – 31

8

GTP

Nucleotide binding

45 – 48

4

GTP

Nucleotide binding

67 – 71

5

GTP By similarity

Nucleotide binding

126 – 129

4

GTP

Nucleotide binding

160 – 161

2

GTP

Sites

Metal binding

31

1

Magnesium

Metal binding

48

1

Magnesium

Binding site

70

1

GTP; via amide nitrogen

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

181

Helix Strand Turn

Details...

Beta strand

18 – 23

6

Helix

30 – 39

10

Beta strand

49 – 58

10

Beta strand

61 – 68

8

Helix

72 – 81

10

Beta strand

86 – 93

8

Helix

100 – 111

12

Helix

114 – 116

3

Beta strand

120 – 126

7

Helix

136 – 143

8

Helix

145 – 147

3

Beta strand

153 – 157

5

Turn

160 – 162

3

Helix

166 – 178

13

Sequences

	Sequence		Length	Mass (Da)
	P40616 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 9FB736C8ED60DC3D	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

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]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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. , 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]. Tissue: Placenta.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Retina.
[7]	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. , 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].
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L28997 mRNA. Translation: AAC37567.1.
AF493887 mRNA. Translation: AAM12601.1.
BT007260 mRNA. Translation: AAP35924.1.
AK311793 mRNA. Translation: BAG34736.1.
BX537387 mRNA. Translation: CAD97629.1.
CH471054 Genomic DNA. Translation: EAW97658.1.
BC007000 mRNA. Translation: AAH07000.1.

IPI

IPI00219518.

RefSeq

NP_001168.1. NM_001177.4.

UniGene

Hs.372616.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P40616.

SMR

P40616. Positions 15-181.

ModBase

Search...

Protein-protein interaction databases

IntAct

P40616. 4 interactions.

STRING

P40616.

Polymorphism databases

DMDM

728888.

Proteomic databases

PRIDE

P40616.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261636; ENSP00000261636; ENSG00000120805.

GeneID

400.

KEGG

hsa:400.

UCSC

uc001tib.1. human.

Organism-specific databases

CTD

400.

GeneCards

GC12M101786.

H-InvDB

HIX0010921.

HGNC

HGNC:692. ARL1.

MIM

603425. gene.

neXtProt

NX_P40616.

PharmGKB

PA24985.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10139.

GeneTree

ENSGT00600000084214.

HOGENOM

HBG745225.

HOVERGEN

HBG002073.

InParanoid

P40616.

OMA

FANKQDQ.

OrthoDB

EOG4K9BDC.

PhylomeDB

P40616.

Gene expression databases

ArrayExpress

P40616.

Bgee

P40616.

CleanEx

HS_ARL1.

Genevestigator

P40616.

GermOnline

ENSG00000120805. Homo sapiens.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]

KO

K07942.

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

NextBio

1677.

SOURCE

Search...

Entry information

Entry name

ARL1_HUMAN

Accession

Primary (citable) accession number: P40616
Secondary accession number(s): P80417, Q53XB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.