| Tag |
Content |
LipidDB ID |
LipidDB-559292-00328 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
6.75 |
Molecular Weight |
20529.47 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
ADP-ribosylation factor 1 |
Protein Synonyms/Alias |
|
Gene Name |
ARF1 |
Gene Synonyms/Alias |
YDL192W; D1244; |
Created Date |
01-JUL-1989 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGLFASKLF | [1][2] | N-Myristoylation |
|
Organism |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID |
559292 |
Reference |
[1] Liu Y, Kahn RA, Prestegard JH. Structure and membrane interaction ofmyristoylated ARF1. Structure. 2009 Jan 14;17(1):79-87. doi:10.1016/j.str.2008.10.020.[ PMID:19141284]
[2] Liu Y, Kahn RA, Prestegard JH. Dynamic structure of membrane-anchored Arf*GTP.Nat Struct Mol Biol. 2010 Jul;17(7):876-81. doi: 10.1038/nsmb.1853. Epub 2010 Jul4.[ PMID:20601958]
|
Functional Description |
GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA. |
Sequence Annotation |
Nucleotide-binding: 25 32 GTP. Nucleotide-binding: 126 129 GTP. Nucleotide-binding: 160 161 GTP. Binding site: 48 48 GTP. Binding site: 70 70 GTP; via amide nitrogen.
|
Protein Length |
181 AA. |
Protein Sequence (Canonical) |
MGLFASKLFS NLFGNKEMRI LMVGLDGAGK TTVLYKLKLG EVITTIPTIG FNVETVQYKN 60
ISFTVWDVGG QDRIRSLWRH YYRNTEGVIF VVDSNDRSRI GEAREVMQRM LNEDELRNAA 120
WLVFANKQDL PEAMSAAEIT EKLGLHSIRN RPWFIQATCA TSGEGLYEGL EWLSNSLKNS 180
T 181
|
FASTA (Canonical) |
>LipidDB-559292-00328|P11076
MGLFASKLFSNLFGNKEMRILMVGLDGAGKTTVLYKLKLGEVITTIPTIGFNVETVQYKN
ISFTVWDVGGQDRIRSLWRHYYRNTEGVIFVVDSNDRSRIGEAREVMQRMLNEDELRNAA
WLVFANKQDLPEAMSAAEITEKLGLHSIRNRPWFIQATCATSGEGLYEGLEWLSNSLKNS
T
|
Gene Ontology |
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Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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