ARFG3_MACFA
ID ARFG3_MACFA Reviewed; 516 AA.
AC Q4R4C9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 3;
DE Short=ARF GAP 3;
GN Name=ARFGAP3 {ECO:0000250|UniProtKB:Q9NP61}; ORFNames=QtsA-10902;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000312|EMBL:BAE02036.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1
CC (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of
CC coatomer from Golgi-derived membranes to allow fusion with target
CC membranes (By similarity). {ECO:0000250|UniProtKB:Q9NP61}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2). {ECO:0000250|UniProtKB:Q9NP61}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NP61}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q9NP61}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9NP61}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9NP61}. Note=Also found on peripheral punctate
CC structures likely to be endoplasmic reticulum-Golgi intermediate
CC compartment. {ECO:0000250|UniProtKB:Q9NP61}.
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DR EMBL; AB178985; BAE02036.1; -; mRNA.
DR RefSeq; NP_001270363.1; NM_001283434.1.
DR AlphaFoldDB; Q4R4C9; -.
DR SMR; Q4R4C9; -.
DR STRING; 9541.XP_005567145.1; -.
DR GeneID; 101866546; -.
DR CTD; 26286; -.
DR eggNOG; KOG0706; Eukaryota.
DR OrthoDB; 1155557at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..516
FT /note="ADP-ribosylation factor GTPase-activating protein 3"
FT /id="PRO_0000314053"
FT DOMAIN 10..126
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 25..48
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 170..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..264
FT /evidence="ECO:0000255"
FT COMPBIAS 170..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
SQ SEQUENCE 516 AA; 56823 MW; 042FF922F42BBD7A CRC64;
MGDPSKQDIL TIFKRLRSVP TNKVCFDCGA KNPSWASITY GVFLCIDCSG SHRSLGVHLS
FIRSTELDSN WSWFQLRCMQ VGGNANASSF FHQHGCSTSD TNAKYNSRAA QLYREKIKSL
ASQATRKHGT DLWLDSCVVP PLSPPPKEED FFASHVSPEV SDTAWASAIA EPSSLTSRPV
ETTLENNEGG QEQGPSVEGL NVPSKAALEV SSIIKKKPNQ AKKGLGAKKG SLGAQKLANT
CFNEIEKQAQ AADKMKEQED LAKAAPKEES IVSSLRLAYK DLEIQMKKDE KLNISGKKNV
DSDRLGMGFG NCRSGISHSV TSDMQTIEQE SPIMAKPRKK YNDDSDDSYF TSSSRYFDEA
VELRSSSFSS WDDSSDSYWK KETSKDTETI LKTTGYSDRP TARRKPDYEP VENTDEAQKK
FGNVKAISSD MYFGRQAQAD YETRARLERL SASSSISSAD LFEEQRKQAA GNYSLSNVLP
SAPNMAQFKQ GVRSVAGKLS VFANGVVTSI QDRYGS
