AGAP3_MOUSE
ID AGAP3_MOUSE Reviewed; 910 AA.
AC Q8VHH5; Q812F7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3;
DE Short=AGAP-3;
DE AltName: Full=CRAM-associated GTPase;
DE Short=CRAG;
DE AltName: Full=Centaurin-gamma-3;
DE Short=Cnt-g3;
DE AltName: Full=MR1-interacting protein;
DE Short=MRIP-1;
GN Name=Agap3; Synonyms=Centg3;
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 2), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, MUTAGENESIS OF SER-140 AND 368-LYS-ARG-369, ACTIVITY REGULATION, AND
RP FUNCTION.
RX PubMed=16461359; DOI=10.1083/jcb.200505079;
RA Qin Q., Inatome R., Hotta A., Kojima M., Yamamura H., Hirai H.,
RA Yoshizawa T., Tanaka H., Fukami K., Yanagi S.;
RT "A novel GTPase, CRAG, mediates promyelocytic leukemia protein-associated
RT nuclear body formation and degradation of expanded polyglutamine protein.";
RL J. Cell Biol. 172:497-504(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gong L., Wu K.;
RT "Characterization of MRIP-1, a novel ADP-ribosylation factor GTPase-
RT activating protein.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=15381706; DOI=10.1074/jbc.m410565200;
RA Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S.;
RT "AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl
RT cyclase.";
RL J. Biol. Chem. 279:49346-49354(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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 for the ADP ribosylation factor
CC family (Potential). GTPase which may be involved in the degradation of
CC expanded polyglutamine proteins through the ubiquitin-proteasome
CC pathway. {ECO:0000269|PubMed:16461359, ECO:0000305}.
CC -!- ACTIVITY REGULATION: GTPase activity is stimulated by oxidative stress.
CC {ECO:0000269|PubMed:16461359}.
CC -!- SUBUNIT: Interacts with PML. Interacts with expanded polyglutamine
CC proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Upon oxidative stress,
CC translocates to PML nuclear bodies. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VHH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VHH5-2; Sequence=VSP_018543, VSP_018544, VSP_018545;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in brain.
CC {ECO:0000269|PubMed:15381706, ECO:0000269|PubMed:16461359}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the developing brain.
CC {ECO:0000269|PubMed:16461359}.
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family. {ECO:0000305}.
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DR EMBL; AB078345; BAC55242.1; -; mRNA.
DR EMBL; AF459091; AAL68640.1; -; mRNA.
DR CCDS; CCDS19122.1; -. [Q8VHH5-1]
DR AlphaFoldDB; Q8VHH5; -.
DR SMR; Q8VHH5; -.
DR IntAct; Q8VHH5; 2.
DR MINT; Q8VHH5; -.
DR STRING; 10090.ENSMUSP00000024123; -.
DR iPTMnet; Q8VHH5; -.
DR PhosphoSitePlus; Q8VHH5; -.
DR SwissPalm; Q8VHH5; -.
DR EPD; Q8VHH5; -.
DR MaxQB; Q8VHH5; -.
DR PaxDb; Q8VHH5; -.
DR PeptideAtlas; Q8VHH5; -.
DR PRIDE; Q8VHH5; -.
DR ProteomicsDB; 296080; -. [Q8VHH5-1]
DR ProteomicsDB; 296081; -. [Q8VHH5-2]
DR UCSC; uc008wru.2; mouse. [Q8VHH5-2]
DR MGI; MGI:2183446; Agap3.
DR eggNOG; KOG0705; Eukaryota.
DR InParanoid; Q8VHH5; -.
DR PhylomeDB; Q8VHH5; -.
DR ChiTaRS; Agap3; mouse.
DR PRO; PR:Q8VHH5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VHH5; protein.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; GTP-binding;
KW GTPase activation; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..910
FT /note="Arf-GAP with GTPase, ANK repeat and PH domain-
FT containing protein 3"
FT /id="PRO_0000235916"
FT DOMAIN 402..640
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 661..781
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 783..812
FT /note="ANK 1"
FT REPEAT 820..849
FT /note="ANK 2"
FT REPEAT 853..882
FT /note="ANK 3"
FT ZN_FING 676..699
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..410
FT /note="Small GTPase-like"
FT REGION 462..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 177..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 233..236
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 359
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96P47"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96P47"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P47"
FT VAR_SEQ 17..45
FT /note="LAAPGGGGAAAQQLVCGGQFGGAGPGAGG -> RGC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16461359"
FT /id="VSP_018543"
FT VAR_SEQ 376..395
FT /note="SRKGADLDREKKAAECRVDS -> ICATVSNFSSTKRPFQLLPN (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16461359"
FT /id="VSP_018544"
FT VAR_SEQ 396..910
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16461359"
FT /id="VSP_018545"
FT MUTAGEN 140
FT /note="S->N: Abolishes interaction with PML."
FT /evidence="ECO:0000269|PubMed:16461359"
FT MUTAGEN 368..369
FT /note="KR->EE: Abolishes translocation to PML nuclear
FT bodies upon oxidative stress."
FT /evidence="ECO:0000269|PubMed:16461359"
SQ SEQUENCE 910 AA; 97965 MW; 0778B420DFD7ACDB CRC64;
MNFQAGGGQS PQQQQSLAAP GGGGAAAQQL VCGGQFGGAG PGAGGGGPSQ QLAGGPPQQF
ALSNSAAIRA EIQRFESVHP NIYAIYDLIE RIEDLALQNQ IREHVISIED SFVNSQEWTL
SRSVPELKVG IVGNLSSGKS ALVHRYLTGT YVQEESPEGG RFKKEIVVDG QSYLLLIRDE
GGPPELQFAA WVDAVVFVFS LEDEISFQTV YNYFLRLCSF RNASEVPMVL VGTQDAISAA
NPRVIDDSRA RKLSTDLKRC TYYETCATYG LNVERVFQDV AQKVVALRKK QQLAIGPCKS
LPNSPSHSAV SAASIPAVHI NQATNGGSSA FSDYSSSVPS TPSISQRELR IETIAASSTP
TPIRKQSKRR SNIFTSRKGA DLDREKKAAE CRVDSIGSGR AIPIKQGILL KRSGKSLNKE
WKKKYVTLCD NGLLTYHPSL HDYMQNIHGK EIDLLRTTVK VPGKRLPRAT PTTAPGTSPR
ANGLAMERSN TQLGGATGAP HSASSTSLHS ERPHSSAWAG SRPGPEGLHQ RSCSVSSTDQ
WSEAAALPAS MQHPASGPAE SLSSSPKLEP PPSPHSNRKK HRGKKSTGTP RPDGPSSAAE
EAEESFEFVV VSLTGQTWHF EASTAEEREL WVQSVQAQIL ASLQGCRSAK DKTRLGNQNT
ALAVQAVRTV RGNSLCIDCE APNPDWASLN LGALMCIECS GIHRHLGAHL SRVRSLDLDD
WPPELLAVMT AMGNALANSV WEGALDGYSK PGPEACREEK ERWIRAKYEQ KLFLAPLPSS
DVPLGQQLLR AVVEDDLRLL VMLLAHGSKE EVNETYGDGD GRTALHLSSA MANVVFTQLL
IWYGVDVRSR DARGLTPLAY ARRAGSQECA DILIQHGCPG EGCGLAPTPN REPANGTNPS
AELHRSPSIL
