Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00351
Entry Name
UniProt Accession
Theoretical PI
5.63
Molecular Weight
20417.53
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
ADP-ribosylation factor-like protein 1
Protein Synonyms/Alias
Gene Name
ARL1
Gene Synonyms/Alias
Created Date
01-FEB-1995
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGGFFSSIF
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Lin CY, Huang PH, Liao WL, Cheng HJ, Huang CF, Kuo JC, Patton WA, MassenburgD, Moss J, Lee FJ. ARL4, an ARF-like protein that is developmentally regulatedand localized to nuclei and nucleoli. J Biol Chem. 2000 Dec 1;275(48):37815-23.[PMID:10980193]
Functional Description
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.
Sequence Annotation
Nucleotide-binding: 24 31 GTP.
Nucleotide-binding: 45 48 GTP.
Nucleotide-binding: 67 71 GTP.
Nucleotide-binding: 126 129 GTP.
Nucleotide-binding: 160 161 GTP.
Metal binding site: 31 31 Magnesium.
Metal binding site: 48 48 Magnesium.
Binding site: 70 70 GTP; via amide nitrogen.
Protein Length
181 AA.
Protein Sequence
(Canonical)
MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN  60
LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI  120
LVVFANKQDM EQAMTSSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR  180
Q                                                                  181
FASTA
(Canonical)
>LipidDB-9606-00351|P40616
MGGFFSSIFSSLFGTREMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKN
LKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRDRIGISKSELVAMLEEEELRKAI
LVVFANKQDMEQAMTSSEMANSLGLPALKDRKWQIFKTSATKGTGLDEAMEWLVETLKSR
Q
Gene Ontology
GO:0005737; C:cytoplasm; ISS:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005794; C:Golgi apparatus; IDA:UniProtKB
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005802; C:trans-Golgi network; ISS:UniProtKB
GO:0008047; F:enzyme activator activity; IDA:UniProtKB
GO:0005525; F:GTP binding; IDA:UniProtKB
GO:0003924; F:GTPase activity; IDA:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0019904; F:protein domain specific binding; IPI:UniProtKB
GO:0031584; P:activation of phospholipase D activity; IDA:UniProtKB
GO:0007030; P:Golgi organization; ISS:UniProtKB
GO:0048193; P:Golgi vesicle transport; IEA:Ensembl
GO:0006184; P:GTP catabolic process; IDA:UniProtKB
GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB
GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro
GO:0009404; P:toxin metabolic process; IDA:UniProtKB
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR024156; Small_GTPase_ARF
InterPro; IPR006689; Small_GTPase_ARF/SAR
Pfam
Pfam; PF00025; Arf;
SMART
SMART; SM00177; ARF;
PROSITE
PROSITE; PS51417; ARF;
PRINTS
PRINTS; PR00328; SAR1GTPBP;