ARFG3_BOVIN
ID ARFG3_BOVIN Reviewed; 517 AA.
AC Q17R07;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 3;
DE Short=ARF GAP 3;
GN Name=ARFGAP3 {ECO:0000250|UniProtKB:Q9NP61};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI18088.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI18088.1};
RC TISSUE=Uterus {ECO:0000312|EMBL:AAI18088.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=1910037; DOI=10.1016/s0021-9258(19)47330-4;
RA Holden J.L., Nur-E-Kamal M.S., Fabri L., Nice E., Hammacher A., Maruta H.;
RT "Rsr1 and Rap1 GTPases are activated by the same GTPase-activating protein
RT and require threonine 65 for their activation.";
RL J. Biol. Chem. 266:16992-16995(1991).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1
CC (ARF1) (PubMed:1910037). Hydrolysis of ARF1-bound GTP may lead to
CC dissociation of coatomer from Golgi-derived membranes to allow fusion
CC with target membranes (By similarity). {ECO:0000250|UniProtKB:Q9NP61,
CC ECO:0000269|PubMed:1910037}.
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; BC118087; AAI18088.1; -; mRNA.
DR RefSeq; NP_001069442.1; NM_001075974.1.
DR AlphaFoldDB; Q17R07; -.
DR SMR; Q17R07; -.
DR STRING; 9913.ENSBTAP00000050747; -.
DR PaxDb; Q17R07; -.
DR PRIDE; Q17R07; -.
DR Ensembl; ENSBTAT00000053995; ENSBTAP00000050747; ENSBTAG00000001057.
DR GeneID; 532778; -.
DR KEGG; bta:532778; -.
DR CTD; 26286; -.
DR VEuPathDB; HostDB:ENSBTAG00000001057; -.
DR VGNC; VGNC:26063; ARFGAP3.
DR eggNOG; KOG0706; Eukaryota.
DR GeneTree; ENSGT00940000158466; -.
DR HOGENOM; CLU_023062_6_2_1; -.
DR InParanoid; Q17R07; -.
DR OrthoDB; 1155557at2759; -.
DR TreeFam; TF313985; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000001057; Expressed in granulosa cell and 112 other tissues.
DR ExpressionAtlas; Q17R07; baseline and differential.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; IBA:GO_Central.
DR GO; GO:0015031; P:protein 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..517
FT /note="ADP-ribosylation factor GTPase-activating protein 3"
FT /id="PRO_0000314052"
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 139..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..263
FT /evidence="ECO:0000255"
FT COMPBIAS 156..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..420
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 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
SQ SEQUENCE 517 AA; 56766 MW; 0F1325B76C5DF9B2 CRC64;
MGDPSKQDIL TIFKRLRSVP TNKVCFDCGA KNPSWASITY GVFLCIDCSG SHRSLGVHLS
FIRSTELDSN WSWFQLRCMQ VGGNANASSF FHQHGCDTND TNAKYNSRAA QLYRERIKAL
ASQATRKHGT DLWLDSCVVP PSSPPPKEED FFASHASPEV SSTGWASAQP EPSLTPRNVD
APAASSEGVP EQGPSVEGLN VPTKAAVGEV SSIIKKKPNQ AKRGLGAKKG SLGAQKLSNT
CFNEIEKQAQ AVDKMNAQED LLSRAAPKEE SIVSSLRLAY KDLEIQMKKD EKMNMSGKKK
AESERLGMGF GNSRSGISHS VTSDMQTIEQ ETPITAKPRK KYGDDSDDSY FTSSSRFFDE
PMELRSSSFS SWDDSSDSYW KKETIKDTDP IPKNTGYTDR PTTRRKPDSE PAENTDEAQK
KFGNVKAISS DMYFGRQAKA DYEARARLER LSASSSISSA DLFDEQRKQT AGSYNLTSVL
PTAPDMAQFK QGVRSVAGKL SVFANGVMTS IQDRYGS
