ARFG3_PONAB
ID ARFG3_PONAB Reviewed; 516 AA.
AC Q5R787;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 3;
DE Short=ARF GAP 3;
GN Name=ARFGAP3 {ECO:0000250|UniProtKB:Q9NP61};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH92373.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:CAH92373.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860231; CAH92373.1; -; mRNA.
DR RefSeq; NP_001126398.1; NM_001132926.2.
DR AlphaFoldDB; Q5R787; -.
DR SMR; Q5R787; -.
DR STRING; 9601.ENSPPYP00000013284; -.
DR Ensembl; ENSPPYT00000013823; ENSPPYP00000013284; ENSPPYG00000011903.
DR GeneID; 100173380; -.
DR KEGG; pon:100173380; -.
DR CTD; 26286; -.
DR eggNOG; KOG0706; Eukaryota.
DR GeneTree; ENSGT00940000158466; -.
DR HOGENOM; CLU_023062_6_2_1; -.
DR InParanoid; Q5R787; -.
DR OMA; ENGPSKV; -.
DR OrthoDB; 1155557at2759; -.
DR TreeFam; TF313985; -.
DR Proteomes; UP000001595; Chromosome 22.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0009306; P:protein secretion; IEA:Ensembl.
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_0000314054"
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 393..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..264
FT /evidence="ECO:0000255"
FT COMPBIAS 170..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
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; 56933 MW; 74A7364820674939 CRC64;
MGDPSKQDIL TIFKRLRSVP TNKVCFDCGA KNPSWASITY GVFLCIDCSG SHRSLGVHLS
FIRSTELDSN WSWFQLRCMQ VGGNANASSF FHQHGCSTND TNAKYNSRAA QLYREKIKSL
ASQATRKHGT DLWLDSCVVP PLSPPPKEED FFASHVSPEV SDTAWASAIA EPSSLTSRPA
ETTLENNEGG QEQGPCVEGL NVPTKATLEV SSIIKKKPNQ AKKGLGAKKR SLGAQKLANT
CFNEIEKQAQ AADKMKEQED LAKAAPKEES IVSSLRLAYK DLEIQMKKDE KMNISGKKNV
DSDRLGMGFG NCRSGISHSV TSDMQTIEQE SPIMAKPRKK YNDDGDDSYF TSSSRYFDEP
VELRSGSFSS WDDSSDSYWK KETSKDTETV LKTTGYSDRP TARHKPDYEP VENTDEAQKK
FGNVKAISSD MYFGRQAQAD YETRARLERL SASSSISSAD LFEEQRKQAA GNYSLSSVLP
NAPDMAQFKQ GVRSVAGKLS VFANGVVTSI QDRYGS
