ARFG2_MOUSE
ID ARFG2_MOUSE Reviewed; 520 AA.
AC Q99K28; Q9D758; Q9JIH1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 2;
DE Short=ARF GAP 2;
DE AltName: Full=GTPase-activating protein ZNF289;
DE AltName: Full=Zinc finger protein 289;
GN Name=Arfgap2; Synonyms=Zfp289, Znf289;
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Mammary epithelium;
RX PubMed=11278321; DOI=10.1074/jbc.m006931200;
RA Singh J., Itahana Y., Parrinello S., Murata K., Desprez P.-Y.;
RT "Molecular cloning and characterization of a zinc finger protein involved
RT in Id-1-stimulated mammary epithelial cell growth.";
RL J. Biol. Chem. 276:11852-11858(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, and Heart;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-239, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-239 AND SER-339, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, 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). May regulate coatomer-mediated protein transport from the Golgi
CC complex to the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may
CC lead to dissociation of coatomer from Golgi-derived membranes to allow
CC fusion with target membranes (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11278321}.
CC -!- SUBUNIT: Interacts with the coatomer complex. Interacts with the C-
CC terminal appendage domain of COPG1 (By similarity). {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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99K28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99K28-2; Sequence=VSP_023305;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, heart and kidney. Low
CC expression in skeletal muscle and spleen.
CC {ECO:0000269|PubMed:11278321}.
CC -!- DEVELOPMENTAL STAGE: High levels in mammary glands of virgin mice and
CC in mammary glands of pregnant mice associated with extensive
CC proliferation of ductal cells and lobulo-alveolar development.
CC Expression declines at the beginning of lactation when the glands fully
CC differentiate. No expression after day 2 of lactation until day 21.
CC Expression may be controlled by ID1. {ECO:0000269|PubMed:11278321}.
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DR EMBL; AF229439; AAF91258.1; -; mRNA.
DR EMBL; AK009565; BAB26362.1; -; mRNA.
DR EMBL; AK168489; BAE40376.1; -; mRNA.
DR EMBL; AK169144; BAE40923.1; -; mRNA.
DR EMBL; AK149837; BAE29114.1; -; mRNA.
DR EMBL; AL732478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005495; AAH05495.1; -; mRNA.
DR CCDS; CCDS16430.1; -. [Q99K28-1]
DR CCDS; CCDS50639.1; -. [Q99K28-2]
DR RefSeq; NP_001159496.1; NM_001166024.1. [Q99K28-2]
DR RefSeq; NP_076343.2; NM_023854.2. [Q99K28-1]
DR AlphaFoldDB; Q99K28; -.
DR SMR; Q99K28; -.
DR BioGRID; 218475; 8.
DR IntAct; Q99K28; 1.
DR MINT; Q99K28; -.
DR STRING; 10090.ENSMUSP00000028691; -.
DR iPTMnet; Q99K28; -.
DR PhosphoSitePlus; Q99K28; -.
DR EPD; Q99K28; -.
DR jPOST; Q99K28; -.
DR MaxQB; Q99K28; -.
DR PaxDb; Q99K28; -.
DR PeptideAtlas; Q99K28; -.
DR PRIDE; Q99K28; -.
DR ProteomicsDB; 277276; -. [Q99K28-1]
DR ProteomicsDB; 277277; -. [Q99K28-2]
DR Antibodypedia; 13559; 186 antibodies from 27 providers.
DR DNASU; 77038; -.
DR Ensembl; ENSMUST00000028691; ENSMUSP00000028691; ENSMUSG00000027255. [Q99K28-2]
DR Ensembl; ENSMUST00000080008; ENSMUSP00000078920; ENSMUSG00000027255. [Q99K28-1]
DR GeneID; 77038; -.
DR KEGG; mmu:77038; -.
DR UCSC; uc008kvq.2; mouse. [Q99K28-1]
DR UCSC; uc008kvr.2; mouse. [Q99K28-2]
DR CTD; 84364; -.
DR MGI; MGI:1924288; Arfgap2.
DR VEuPathDB; HostDB:ENSMUSG00000027255; -.
DR eggNOG; KOG0706; Eukaryota.
DR GeneTree; ENSGT00940000155568; -.
DR HOGENOM; CLU_023062_6_2_1; -.
DR InParanoid; Q99K28; -.
DR OMA; QNVGESI; -.
DR PhylomeDB; Q99K28; -.
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 BioGRID-ORCS; 77038; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Arfgap2; mouse.
DR PRO; PR:Q99K28; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99K28; protein.
DR Bgee; ENSMUSG00000027255; Expressed in hindlimb stylopod muscle and 131 other tissues.
DR Genevisible; Q99K28; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW ER-Golgi transport; Golgi apparatus; GTPase activation; Membrane;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT CHAIN 2..520
FT /note="ADP-ribosylation factor GTPase-activating protein 2"
FT /id="PRO_0000278469"
FT DOMAIN 11..127
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 26..49
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 97..520
FT /note="Required for interaction with coatomer"
FT /evidence="ECO:0000250"
FT REGION 163..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..307
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT VAR_SEQ 206
FT /note="E -> ESMYLSAKGPSCTRE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023305"
FT CONFLICT 467
FT /note="N -> D (in Ref. 1; AAF91258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 56598 MW; 9B06038602F15014 CRC64;
MAASPSKTEI QTIFKRLRAI PTNKACFDCG AKSPSWASIT YGVFLCIDCS GVHRSLGVHL
SFIRSTELDS NWSWLQLRCM QVGGNANATA FFRQHGCMAN DANTKYTSRA AQMYREKIRQ
LGSAALTRHG TDLWIDSMNS APSHSPEKKD SDFFTEHTQA PAWDTAATDP SGTQQPALPS
ESSSLAQPEQ GPNTDLLGTS PQASLELKSS IIGKKKPAAA KKGLGAKKGL GAQKVSNQSF
TEIERQAQVA EKLREQQAAD AKKQAEESMV ASMRLAYQEL QIDRKKEEKK LQNLEGKKRE
QAERLGMGLV SRSSISHSVL SEMQMIEQET PLSAKSSRSQ LDLFDDVGTF ASGPPKYKDN
PFSLGETFGS RWDSDAAWGM DRVEEKEPEV TISSIRPISE RTASRREVET RSSGLESSEA
RQKFAGAKAI SSDMFFGREV DSEYEARSRL QQLSGSSAIS SSDLFGNMDG AHGGGTVSLG
NVLPTADIAQ FKQGVKSVAG KMAVLANGVM NSLQDRYGSY
