ARFG3_MOUSE
ID ARFG3_MOUSE Reviewed; 523 AA.
AC Q9D8S3; Q544V6; Q8BW06; Q99KN8;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 3;
DE Short=ARF GAP 3;
GN Name=Arfgap3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Amnion, Pancreas, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Olfactory epithelium;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-331, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Also found on peripheral punctate structures
CC likely to be endoplasmic reticulum-Golgi intermediate compartment.
CC {ECO:0000250}.
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DR EMBL; AK007732; BAB25220.1; -; mRNA.
DR EMBL; AK028990; BAC26229.1; -; mRNA.
DR EMBL; AK075788; BAC35959.1; -; mRNA.
DR EMBL; AK169107; BAE40889.1; -; mRNA.
DR EMBL; BC004081; AAH04081.1; -; mRNA.
DR EMBL; BC060369; AAH60369.1; -; mRNA.
DR CCDS; CCDS88818.1; -.
DR RefSeq; NP_079721.2; NM_025445.4.
DR RefSeq; XP_006521316.2; XM_006521253.3.
DR RefSeq; XP_006521318.2; XM_006521255.3.
DR AlphaFoldDB; Q9D8S3; -.
DR SMR; Q9D8S3; -.
DR BioGRID; 211327; 1.
DR IntAct; Q9D8S3; 1.
DR MINT; Q9D8S3; -.
DR STRING; 10090.ENSMUSP00000064893; -.
DR iPTMnet; Q9D8S3; -.
DR PhosphoSitePlus; Q9D8S3; -.
DR EPD; Q9D8S3; -.
DR jPOST; Q9D8S3; -.
DR MaxQB; Q9D8S3; -.
DR PaxDb; Q9D8S3; -.
DR PeptideAtlas; Q9D8S3; -.
DR PRIDE; Q9D8S3; -.
DR ProteomicsDB; 283255; -.
DR Antibodypedia; 34963; 286 antibodies from 37 providers.
DR DNASU; 66251; -.
DR Ensembl; ENSMUST00000226124; ENSMUSP00000154712; ENSMUSG00000054277.
DR GeneID; 66251; -.
DR KEGG; mmu:66251; -.
DR UCSC; uc007xag.1; mouse.
DR CTD; 26286; -.
DR MGI; MGI:1913501; Arfgap3.
DR VEuPathDB; HostDB:ENSMUSG00000054277; -.
DR eggNOG; KOG0706; Eukaryota.
DR GeneTree; ENSGT00940000158466; -.
DR InParanoid; Q9D8S3; -.
DR OrthoDB; 1155557at2759; -.
DR PhylomeDB; Q9D8S3; -.
DR TreeFam; TF313985; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 66251; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Arfgap3; mouse.
DR PRO; PR:Q9D8S3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D8S3; protein.
DR Bgee; ENSMUSG00000054277; Expressed in lacrimal gland and 251 other tissues.
DR ExpressionAtlas; Q9D8S3; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
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:0009306; P:protein secretion; ISS:UniProtKB.
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 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..523
FT /note="ADP-ribosylation factor GTPase-activating protein 3"
FT /id="PRO_0000074194"
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 162..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..421
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 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0007744|PubMed:21183079"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT MOD_RES 435
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 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 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP61"
FT CONFLICT 208
FT /note="P -> PA (in Ref. 1; BAB25220)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="S -> SS (in Ref. 1; BAB25220/BAC26229 and 2;
FT AAH04081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 57456 MW; FC093B11DB765BC3 CRC64;
MGDPSKQDIL AIFKRLRSVP TNKVCFDCGA KNPSWASISY GVFLCIDCSG SHRSLGVHLS
FIRSTELDSN WSWFQLRCMQ VGGNSNASSF FHQHGCATKD TNAKYNSRAA QLYREKIKTL
ATQATRRHGT DLWLDSCAAP PVSPPPKEED FFASHASLEV SGAMQASAQP ESASSTPWGL
ETTPEKHEGG PGQGPSVEGL NTPGKAAPEV SSIIKKKPNQ AKKGLGAKKG SLGAQKLTNT
SFTEIEKQAQ AVDKRKEQED LARGAPKEES IVSSLRLAYK DLEISRKKDE RLNLSGQKKV
EAERLGMGFG SCRSGISHSV TSDMQTIEQE SPTLAKPRRK YQEDPEDSYF SSSSKWSEQS
SRYFDDPMEL RSSSFSSWDD GADSYWKKDS SRDPEPAMRS TGSSDRPSAR RKPEYEPIGS
TDEAQKKFGN VKAISSDMYF GIQAQTDFET RARLERLSTS SSISSADLFD EQRKQTAGNY
NLSNVLPNAP DMAQFKQGVR SVAGKLSVFA NGVMTSIQDR YGS
