ID ARFG3_RAT Reviewed; 525 AA.
AC Q4KLN7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 3;
DE Short=ARF GAP 3;
GN Name=Arfgap3 {ECO:0000250|UniProtKB:Q9NP61};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH99081.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta {ECO:0000312|EMBL:AAH99081.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC099081; AAH99081.1; -; mRNA.
DR RefSeq; NP_001037738.1; NM_001044273.1.
DR RefSeq; XP_017450552.1; XM_017595063.1.
DR AlphaFoldDB; Q4KLN7; -.
DR SMR; Q4KLN7; -.
DR STRING; 10116.ENSRNOP00000073062; -.
DR iPTMnet; Q4KLN7; -.
DR PhosphoSitePlus; Q4KLN7; -.
DR jPOST; Q4KLN7; -.
DR PaxDb; 10116-ENSRNOP00000065256; -.
DR Ensembl; ENSRNOT00000074960.3; ENSRNOP00000065256.3; ENSRNOG00000046472.3.
DR Ensembl; ENSRNOT00055054120; ENSRNOP00055044760; ENSRNOG00055031212.
DR Ensembl; ENSRNOT00060037282; ENSRNOP00060030757; ENSRNOG00060021424.
DR Ensembl; ENSRNOT00065057054; ENSRNOP00065046959; ENSRNOG00065033151.
DR GeneID; 503165; -.
DR KEGG; rno:503165; -.
DR AGR; RGD:1560066; -.
DR CTD; 26286; -.
DR RGD; 1560066; Arfgap3.
DR eggNOG; KOG0706; Eukaryota.
DR GeneTree; ENSGT00940000158466; -.
DR InParanoid; Q4KLN7; -.
DR OrthoDB; 389572at2759; -.
DR PhylomeDB; Q4KLN7; -.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR PRO; PR:Q4KLN7; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0048786; C:presynaptic active zone; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
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:0140238; P:presynaptic endocytosis; ISO:RGD.
DR GO; GO:0009306; P:protein secretion; ISO:RGD.
DR CDD; cd09028; ArfGap_ArfGap3; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR PANTHER; PTHR45686; ADP-RIBOSYLATION FACTOR GTPASE ACTIVATING PROTEIN 3, ISOFORM H-RELATED; 1.
DR PANTHER; PTHR45686:SF1; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN 3; 1.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; ER-Golgi transport; Golgi apparatus; GTPase activation;
KW Membrane; Metal-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..525
FT /note="ADP-ribosylation factor GTPase-activating protein 3"
FT /id="PRO_0000314055"
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 160..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
SQ SEQUENCE 525 AA; 57671 MW; B8E97FA335876CBB CRC64;
MGDPSKQDIL AIFKRLRSVP TNKVCFDCGA KNPSWASISY GVFLCIDCSG SHRSLGVHLS
FIRSTELDSN WSWFQLRCMQ VGGNANASSF FHQHGCATKD TNAKYNSRAA QLYREKIKTL
ATQATRRHGT DLWLDSCAAP PASPPPKEED FFASHASLEV SGATQASAQP EPASSTPWGL
ETTPEKHEGG PGQGPSVEGL NTPGKTAPAE VSSIIKKKPN QAKKGLGAKK GSLGAQKLTN
TSFTEIEKQA QAVDKRKEQE DLARGTPKEE SIVSSLRLAY KDLEIHKKQD ERLNLSGQKK
AEAERLGMGF GSCRGGISHS VTSDMQTIEQ ESPTLAKPRR KYQEDPEDSY FSSSSKWSEQ
SSSRYFDDPM ELRSSHFSSW DDSADSYWKK DSSRDPEPAT KSTGSSDRPS SRRKPEYEPV
GNTDEAQKKF GNVKAISSDM YFGIQSQTDF ETRARLERLS TSSSISSADL FDEQRKQTTG
NYNLSNVLPN APDMAQFKQG VRSVAGKLSV FANGVMTSIQ DRYGS
//
