ID A0A0A0MQE8_MOUSE Unreviewed; 1949 AA.
AC A0A0A0MQE8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Rho GTPase activating protein 21 {ECO:0000313|Ensembl:ENSMUSP00000110241.2};
GN Name=Arhgap21 {ECO:0000313|Ensembl:ENSMUSP00000110241.2,
GN ECO:0000313|MGI:MGI:1918685};
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 {ECO:0000313|Ensembl:ENSMUSP00000110241.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:16452087}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [2] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3] {ECO:0007829|PubMed:19144319}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000110241.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110241.2,
RC ECO:0000313|Proteomes:UP000000589};
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 [5] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [6] {ECO:0007829|PubMed:24129315}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24129315;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [7] {ECO:0000313|Ensembl:ENSMUSP00000110241.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110241.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic
CC vesicle membrane {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00004284}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004395}.
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DR SMR; A0A0A0MQE8; -.
DR jPOST; A0A0A0MQE8; -.
DR ProteomicsDB; 352823; -.
DR Antibodypedia; 51888; 31 antibodies from 14 providers.
DR Ensembl; ENSMUST00000114594.8; ENSMUSP00000110241.2; ENSMUSG00000036591.17.
DR AGR; MGI:1918685; -.
DR MGI; MGI:1918685; Arhgap21.
DR VEuPathDB; HostDB:ENSMUSG00000036591; -.
DR GeneTree; ENSGT00940000155406; -.
DR HOGENOM; CLU_001776_0_0_1; -.
DR ChiTaRS; Arhgap21; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000036591; Expressed in lacrimal gland and 264 other cell types or tissues.
DR ExpressionAtlas; A0A0A0MQE8; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01253; PH_ARHGAP21-like; 1.
DR CDD; cd04395; RhoGAP_ARHGAP21; 1.
DR Gene3D; 1.20.5.220; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23175; PDZ DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23175:SF16; RHO GTPASE-ACTIVATING PROTEIN 21; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Proteomics identification {ECO:0007829|EPD:A0A0A0MQE8,
KW ECO:0007829|MaxQB:A0A0A0MQE8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 50..159
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 929..1038
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1145..1337
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1653..1798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1870..1936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1949 AA; 216449 MW; 374D29649861F5D6 CRC64;
MMATHWTGLP EEDGDKLKAC GVSKNKDGKD QGEPVSPSED EPFSWPGPKT VMLKRTSQGF
GFTLRHFIVY PPESAIQFSY KDEENGNRGG KQRNRLEPMD TIFVKQVKEG GPAFEAGLCT
GDRIIKVNGE SVIGKTYSQV IALIQNSDTT LELSVMPKDE DILQVLQFTK DVTALAYSQD
AYLKGNEAYS GNARNIPEPP PVCYPWLPST PSATAQPVET CPPDSLPNKQ QTSAPVLTQP
GRAYRMEIQV PPSPTDVAKS NTAVCVCNES VRTVIVPSEK VVDLLANRNN PSGPSHRTEE
VRYGVNEQAS TKAASRTTSP ASVPTAHLIH QTTGSRSLEP SGILLKSGNY SGHSEGISSS
RSQAVDSPPV SVNHYSANSH QHIDWKNYKT YKEYIDNRRL HIGCRTIQER LDSLRAASQS
AADYNQVVPT RTTLQVRRRS TSHDRVPQSV QIRQRSVSQE RLEDSVLMKY CPRSASQGAL
TSPPVSFNNH RTRSWDYIEG QTEATATVNS ESQIPDSNGE RKQTYKWSGF TEQDDRRGIH
ERPRQQEMHK PFRGSNLTVA PVVNSDNRRL VGRGVGPVSQ FKKIPPDLRP PHSNRNFPTT
TGVSLQRGIA QDRSPLVKVR SNSLKVPPPP VSKPSFSQHS LASMKDQRPV NHLHQHSVLS
QQTQFRSEST FEHQLETEVS SCLPGTSAKT SPQLSENLGT SDLELPAIPR NGDINLQEAE
IQQPDVLDNK ESVILREKPQ SGRQTPQPLR HQSYILAVND QETGSDTTCW LPNDARREVH
IKRMEERKAS STSPPGDSLA SIPFIDEPTS PSIDHEIAHI PASAVISAST AHVPSIATVP
PSLTTSAPLI RRQLSHDQES VGPPSLDGQH SSKTERSKSY DEGLDDYRED AKLSFKHVSS
LKGIKITDSQ KSSEDSGSRK GSSSEVFSDA AREGWLQFRP LVTDKGKRVG GSIRPWKQMY
VVLRGHSLYL YKDRREQTTP SEEEQPISVN ACLIDISYSE TKRRNVFRLT TSDCECLFQA
EDRDDMLSWI KTIQESSNLN EEDTGVTNRD LISRRIKEYN SLLSKTEQLP KTPRQSLSIR
QTLLGAKSEP KTQSPHSPKE ESERKLLSKD DTSPPKDKGT WRRGIPSIVR KTFEKKPAAT
GTFGVRLDDC PPAHTNRYIP LIVDICCKLV EERGLEYTGI YRVPGNNAAI SSMQEELNKG
MADIDIQDDK WRDLNVISSL LKSFFRKLPE PLFTNDKYAD FIEANRKEDP LDRLRTLKRL
IHDLPEHHFE TLKFLSAHLK TVAENSEKNK MEPRNLAIVF GPTLVRTSED NMTHMVTHMP
DQYKIVETLI QHHDWFFTEE GAEEPLTAVQ EENTVDSQPV PNIDHLLTNI GRTGVLPGDV
SDSATSDSAK SKGSWGSGKD QYSRELLVSS IFAAASRKRK KPKEKAQPSS SEDELDSVFF
KKENTEQSHS EIKEESKRES ETSGSKQRVV VAKESNTKKD SGTTKEEKKI PWEEPSPPHS
SKRNRSPTLS CRLAMLKEGP RSLLTQKPHC EETGSDSGTL LSTSSQASLL RSSTKKSTSP
ETKHSEFLSI AGTTTSDYST TSSTTYLTSL DSSRLSPEVQ SVAESKGDEA DDERSELVSE
GRPVETDSES EFPVFPTTLT SDRLFRGKFQ EVARVSRRNS EGSEASCTEG SLTPSLDSRR
QQFSSHRLIE CDTLSRKKSA RFKSDSGSPG DTRTEKETPA LAKMFDVMKK GKSTGSLLTP
SRSESEKQEA TWKTKIADRL KLRPRAPADD MFGVGNQKPT AETAKRKNIK RRHTLGGHRD
ATEISVLSFW KAHEQSADKE SELSAVNRLK PKCSAQDLSI SDWLARERVR TSASDLSRGE
GLEPQAESPS VLGTPISTHS PPSQQPEARV AATSTLASTS QSPLFTPPQS PDQINRESFQ
NMSQNASSTA NIHPHKQSES PDTKAETPP
//
