Primary Information |
---|
BoMiProt ID | Bomi3736 |
---|
Protein Name | ADP-ribosylation factor GTPase-activating protein 3/ARF GAP 3 |
---|
Organism | Bos taurus |
---|
Uniprot ID | Q17R07 |
---|
Milk Fraction | Whey |
---|
Ref Sequence ID | NP_001069442.1 |
---|
Aminoacid Length | 517 |
---|
Molecular Weight | 56766 |
---|
FASTA Sequence |
Download |
---|
Gene Name | ARFGAP3 |
---|
Gene ID | 532778 |
---|
Protein Existence Status | Reviewed |
---|
Secondary Information |
---|
Protein Function | ARFGAP3 colocalized with COPI subunits in the Golgi complex and peripheral punctate structures and associated with COPI-coated vesicles generated from Golgi membranes.It is a GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1) |
---|
Biochemical Properties | ARFGAP3 has an N-terminal GATA1 (305371)-type zinc finger motif containing 4 cysteines that is highly conserved among ARFGAPs, as well as multiple potential phosphorylation sites. |
---|
PTMs | Phosphorylation on ser |
---|
Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q17R07|ARFG3_BOVIN ADP-ribosylation factor GTPase-activating protein 3 OS=Bos taurus OX=9913 GN=ARFGAP3 PE=2 SV=1
MGDPSKQDILTIFKRLRSVPTNKVCFDCGAKNPSWASITYGVFLCIDCSGSHRSLGVHLS
FIRSTELDSNWSWFQLRCMQVGGNANASSFFHQHGCDTNDTNAKYNSRAAQLYRERIKAL
ASQATRKHGTDLWLDSCVVPPSSPPPKEEDFFASHASPEVSSTGWASAQPEPSLTPRNVD
APAASSEGVPEQGPSVEGLNVPTKAAVGEVSSIIKKKPNQAKRGLGAKKGS*231LGAQKLSNT
CFNEIEKQAQAVDKMNAQEDLLSRAAPKEES*271IVSS*275LRLAYKDLEIQMKKDEKMNMSGKKK
AESERLGMGFGNSRSGISHSVTSDMQTIEQETPITAKPRKKYGDDSDDSYFTSSSRFFDE
PMELRSSSFSS*371WDDSSDSYWKKETIKDTDPIPKNTGYTDRPTTRRKPDSEPAENTDEAQK
KFGNVKAIS*429SDMYFGRQAKADYEARARLERLS*452AS*454SS*456IS*458S*459ADLFDEQRKQTAGSYNLTSVLPTAPDMAQFKQGVRSVAGKLSVFANGVMTSIQDRYGS
|
---|
Predicted Disorder Regions | 134-244, 258-269, 287-302, 321-425, 457-466 |
---|
DisProt Annotation | |
---|
TM Helix Prediction | No TM helices |
---|
Bibliography | Holden, J. L., Nur-E-Kamal, M. S., Fabri, L., Nice, E., Hammacher, A., & Maruta, H. (1991). Rsr1 and Rap1 GTPases are activated by the same GTPase-activating protein and require threonine 65 for their activation. The Journal of biological chemistry, 266(26), 16992–16995. |