ARFG1_RAT
ID ARFG1_RAT Reviewed; 415 AA.
AC Q62848;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 1;
DE Short=ARF GAP 1;
DE AltName: Full=ADP-ribosylation factor 1 GTPase-activating protein;
DE Short=ARF1 GAP;
DE AltName: Full=ARF1-directed GTPase-activating protein;
GN Name=Arfgap1; Synonyms=Arf1gap;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ARF1, AND PROTEIN
RP SEQUENCE OF 82-95; 140-160; 183-191; 246-255; 264-278; 297-306 AND 361-375.
RC TISSUE=Liver;
RX PubMed=7890632; DOI=10.1074/jbc.270.10.5232;
RA Makler V., Cukierman E., Rotman M., Admon A., Cassel D.;
RT "ADP-ribosylation factor-directed GTPase-activating protein. Purification
RT and partial characterization.";
RL J. Biol. Chem. 270:5232-5237(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), CHARACTERIZATION, AND
RP MUTAGENESIS OF CYS-22 AND CYS-25.
RC TISSUE=Liver;
RX PubMed=8533093; DOI=10.1126/science.270.5244.1999;
RA Cukierman E., Huber I., Rotman M., Cassel D.;
RT "The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex
RT localization.";
RL Science 270:1999-2002(1995).
RN [3]
RP INTERACTION WITH KDELR1.
RX PubMed=9405360; DOI=10.1093/emboj/16.24.7305;
RA Aoe T., Cukierman E., Lee A., Cassel D., Peters P.J., Hsu V.W.;
RT "The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a
RT GTPase-activating protein for ARF1.";
RL EMBO J. 16:7305-7316(1997).
RN [4]
RP CHARACTERIZATION, AND MUTAGENESIS OF CYS-22.
RX PubMed=9733781; DOI=10.1074/jbc.273.38.24786;
RA Huber I., Cukierman E., Rotman M., Aoe T., Hsu V.W., Cassel D.;
RT "Requirement for both the amino-terminal catalytic domain and a
RT noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-
RT activating protein.";
RL J. Biol. Chem. 273:24786-24791(1998).
RN [5]
RP INTERACTION WITH KDELR1 AND TMED2.
RX PubMed=11703931; DOI=10.1016/s1534-5807(01)00004-1;
RA Majoul I., Straub M., Hell S.W., Duden R., Soling H.D.;
RT "KDEL-cargo regulates interactions between proteins involved in COPI
RT vesicle traffic: measurements in living cells using FRET.";
RL Dev. Cell 1:139-153(2001).
RN [6]
RP INTERACTION WITH RNP24.
RX PubMed=11748249; DOI=10.1083/jcb.200108017;
RA Lanoix J., Ouwendijk J., Stark A., Szafer E., Cassel D., Dejgaard K.,
RA Weiss M., Nilsson T.;
RT "Sorting of Golgi resident proteins into different subpopulations of COPI
RT vesicles: a role for ArfGAP1.";
RL J. Cell Biol. 155:1199-1212(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135; SER-347; SER-360 AND
RP SER-379, AND IDENTIFICATION BY 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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF CATALYTIC DOMAIN IN COMPLEX WITH
RP HUMAN ARF1.
RX PubMed=10102276; DOI=10.1016/s0092-8674(00)80598-x;
RA Goldberg J.;
RT "Structural and functional analysis of the ARF1-ARFGAP complex reveals a
RT role for coatomer in GTP hydrolysis.";
RL Cell 96:893-902(1999).
CC -!- FUNCTION: GTPase-activating protein (GAP) for the ADP ribosylation
CC factor 1 (ARF1). Involved in membrane trafficking and /or vesicle
CC transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is
CC required for the dissociation of coat proteins from Golgi-derived
CC membranes and vesicles, a prerequisite for vesicle's fusion with target
CC compartment. Probably regulates ARF1-mediated transport via its
CC interaction with the KDELR proteins and TMED2. Overexpression induces
CC the redistribution of the entire Golgi complex to the endoplasmic
CC reticulum, as when ARF1 is deactivated. Its activity is stimulated by
CC phosphoinosides and inhibited by phosphatidylcholine.
CC {ECO:0000269|PubMed:7890632}.
CC -!- SUBUNIT: Interacts with ARF1. Interacts with the COPI coat proteins,
CC KDELR1 and TMED2. It is probably a component of the COPI coat protein
CC complex. The interaction with TMED2 inhibits the GAP activity.
CC {ECO:0000269|PubMed:10102276, ECO:0000269|PubMed:11703931,
CC ECO:0000269|PubMed:11748249, ECO:0000269|PubMed:7890632,
CC ECO:0000269|PubMed:9405360}.
CC -!- INTERACTION:
CC Q62848; Q5S007: LRRK2; Xeno; NbExp=7; IntAct=EBI-4398879, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus. Note=Associates with
CC the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q62848-1; Sequence=Displayed;
CC Name=2; Synonyms=W15;
CC IsoId=Q62848-2; Sequence=VSP_000300;
CC Name=3; Synonyms=Z5;
CC IsoId=Q62848-3; Sequence=VSP_000301, VSP_000302;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain and
CC liver.
CC -!- DOMAIN: The region downstream of Arf-GAP domain is essential to GAP
CC activity in vivo. This region may be required for its targeting to
CC Golgi membranes.
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DR EMBL; U35776; AAC52337.1; -; mRNA.
DR RefSeq; NP_659558.1; NM_145090.3. [Q62848-1]
DR RefSeq; XP_017446953.1; XM_017591464.1. [Q62848-1]
DR AlphaFoldDB; Q62848; -.
DR BMRB; Q62848; -.
DR SMR; Q62848; -.
DR BioGRID; 251587; 13.
DR IntAct; Q62848; 7.
DR MINT; Q62848; -.
DR STRING; 10116.ENSRNOP00000013900; -.
DR BindingDB; Q62848; -.
DR ChEMBL; CHEMBL2146307; -.
DR iPTMnet; Q62848; -.
DR PhosphoSitePlus; Q62848; -.
DR SwissPalm; Q62848; -.
DR jPOST; Q62848; -.
DR PaxDb; Q62848; -.
DR PRIDE; Q62848; -.
DR DNASU; 246310; -.
DR GeneID; 246310; -.
DR KEGG; rno:246310; -.
DR CTD; 55738; -.
DR RGD; 708452; Arfgap1.
DR VEuPathDB; HostDB:ENSRNOG00000043150; -.
DR eggNOG; KOG0704; Eukaryota.
DR HOGENOM; CLU_044516_0_0_1; -.
DR InParanoid; Q62848; -.
DR PhylomeDB; Q62848; -.
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-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q62848; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000043150; Expressed in pancreas and 19 other tissues.
DR ExpressionAtlas; Q62848; baseline and differential.
DR Genevisible; Q62848; RN.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; GTPase activation; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..415
FT /note="ADP-ribosylation factor GTPase-activating protein 1"
FT /id="PRO_0000074192"
FT DOMAIN 7..124
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 22..45
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 126..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT MOD_RES 231
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPJ9"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 349
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPJ9"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 21..57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8533093"
FT /id="VSP_000300"
FT VAR_SEQ 280..283
FT /note="QGVG -> GLPC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8533093"
FT /id="VSP_000301"
FT VAR_SEQ 284..415
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8533093"
FT /id="VSP_000302"
FT MUTAGEN 22
FT /note="C->A: Loss of GAP activity."
FT /evidence="ECO:0000269|PubMed:8533093,
FT ECO:0000269|PubMed:9733781"
FT MUTAGEN 25
FT /note="C->A: Loss of GAP activity."
FT /evidence="ECO:0000269|PubMed:8533093"
SQ SEQUENCE 415 AA; 45442 MW; 90015417E3E717BB CRC64;
MASPRTRKVL KEVRAQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR GLGVHLSFVR
SVTMDKWKDI ELEKMKAGGN AKFREFLEAQ DDYEPSWSLQ DKYSSRAAAL FRDKVATLAE
GKEWSLESSP AQNWTPPQPK TLQFTAHRPA GQPQNVTTSG DKAFEDWLND DLGSYQGAQE
NRYVGFGNTV PPQKREDDFL NSAMSSLYSG WSSFTTGASK FASAAKEGAT KFGSQASQKA
SELGHSLNEN VLKPAQEKVK EGRIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAED
TSDRPLEGHS YQNSSGDNSQ NSTIDQSFWE TFGSAEPPKA KSPSSDSWTC ADASTGRRSS
DSWDIWGSGS ASNNKNSNSD GWESWEGASG EGRAKATKKA APSTAADEGW DNQNW
