RHG25_MOUSE
ID RHG25_MOUSE Reviewed; 648 AA.
AC Q8BYW1; B2RS69; Q2VPR2; Q3TE04; Q3TVX0; Q3UVB7; Q6A0E0; Q8BX98;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Rho GTPase-activating protein 25;
DE AltName: Full=Rho-type GTPase-activating protein 25;
GN Name=Arhgap25; Synonyms=Kiaa0053;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Dendritic cell, and Thymus;
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] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 117-648 (ISOFORMS 1/2/3).
RC TISSUE=Jaw, Limb, and Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-648 (ISOFORMS 1/2/3).
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND THR-407, AND
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-403 AND SER-537, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
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 activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BYW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BYW1-2; Sequence=VSP_019233;
CC Name=3;
CC IsoId=Q8BYW1-3; Sequence=VSP_019234;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29857.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK037710; BAC29857.1; ALT_INIT; mRNA.
DR EMBL; AK137444; BAE23353.1; -; mRNA.
DR EMBL; AK159941; BAE35498.1; -; mRNA.
DR EMBL; AK159598; BAE35218.1; -; mRNA.
DR EMBL; AK169897; BAE41444.1; -; mRNA.
DR EMBL; BC108400; AAI08401.1; -; mRNA.
DR EMBL; BC138751; AAI38752.1; -; mRNA.
DR EMBL; AK172878; BAD32156.1; -; mRNA.
DR CCDS; CCDS20321.1; -. [Q8BYW1-1]
DR CCDS; CCDS20322.1; -. [Q8BYW1-3]
DR CCDS; CCDS71790.1; -. [Q8BYW1-2]
DR RefSeq; NP_001032816.1; NM_001037727.2. [Q8BYW1-1]
DR RefSeq; NP_001273539.1; NM_001286610.1. [Q8BYW1-2]
DR RefSeq; NP_780685.2; NM_175476.4. [Q8BYW1-3]
DR AlphaFoldDB; Q8BYW1; -.
DR SMR; Q8BYW1; -.
DR BioGRID; 231227; 2.
DR STRING; 10090.ENSMUSP00000109267; -.
DR iPTMnet; Q8BYW1; -.
DR PhosphoSitePlus; Q8BYW1; -.
DR EPD; Q8BYW1; -.
DR jPOST; Q8BYW1; -.
DR MaxQB; Q8BYW1; -.
DR PaxDb; Q8BYW1; -.
DR PRIDE; Q8BYW1; -.
DR ProteomicsDB; 255206; -. [Q8BYW1-1]
DR ProteomicsDB; 255207; -. [Q8BYW1-2]
DR ProteomicsDB; 255208; -. [Q8BYW1-3]
DR Antibodypedia; 30948; 430 antibodies from 27 providers.
DR DNASU; 232201; -.
DR Ensembl; ENSMUST00000071024; ENSMUSP00000068964; ENSMUSG00000030047. [Q8BYW1-2]
DR Ensembl; ENSMUST00000101197; ENSMUSP00000098758; ENSMUSG00000030047. [Q8BYW1-3]
DR Ensembl; ENSMUST00000113637; ENSMUSP00000109267; ENSMUSG00000030047. [Q8BYW1-1]
DR GeneID; 232201; -.
DR KEGG; mmu:232201; -.
DR UCSC; uc009ctl.2; mouse. [Q8BYW1-1]
DR CTD; 9938; -.
DR MGI; MGI:2443687; Arhgap25.
DR VEuPathDB; HostDB:ENSMUSG00000030047; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00950000183015; -.
DR HOGENOM; CLU_020795_1_0_1; -.
DR InParanoid; Q8BYW1; -.
DR OMA; NWDFNLR; -.
DR OrthoDB; 917149at2759; -.
DR PhylomeDB; Q8BYW1; -.
DR TreeFam; TF323577; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 232201; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Arhgap25; mouse.
DR PRO; PR:Q8BYW1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BYW1; protein.
DR Bgee; ENSMUSG00000030047; Expressed in granulocyte and 123 other tissues.
DR Genevisible; Q8BYW1; MM.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
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 Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..648
FT /note="Rho GTPase-activating protein 25"
FT /id="PRO_0000056717"
FT DOMAIN 46..151
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 160..354
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 356..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 540..641
FT /evidence="ECO:0000255"
FT COMPBIAS 391..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 407
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019233"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_019234"
FT CONFLICT 144
FT /note="K -> N (in Ref. 2; AAI08401)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="M -> T (in Ref. 1; BAE41444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 73383 MW; CBDFE75515BB2C51 CRC64;
MSLKLPRNWD FNLKAEASKI ARSRSVMTGE QMAAFHPPTT PNPLERPIKV GWLKKQRSIV
KNWQQRYFVL RAQQLYYYKD EEDSKPQGCM YLPGSTVKEI ATNPEEAGKF VFEVIPASSD
QNRIGQDSYV LMASSQVEME EWVKFLRRVA GTPSGAVFGQ RLDETVAYEQ KFGPHLVPIL
VEKCAEFILE HGVSEEGIFR LPGQDNLVKQ LRDAFDAGER PSFDRDTDVH TVASLLKLYL
RDLPEPVVPW SQYEGFLLCG QLMNADEAKA QQELVKQLST LPRDNYNLLS YICRFLHEIQ
LNCAVNKMSV DNLATVIGVN LIRSKVEDPA VIMRGTPQIQ RVMTMMIRDH EVLFPKSKDA
PISPPAQKND AKKAPVPRSS VGWDATEDPP LSRTDSFSNT ASSPDATSPT GPLPSDQHQE
DSGKAPRENP GDWKMQSRKR TQTLPNRKCF LTSAFQGTTS SKLEIFKNEF WSPSSEAKAG
EGHRRTMSQD LRHLSNDQRT STYDNVPTSP QSQGNPAGAL SPPASDSKRD ALVSTDSEME
AGSKNSGEDD LDSLQRTVQS LQKEIETQKQ VYEEQIKNLE KENYDVWAKV VRLNEELERE
RKKFAALEIS LRNVERSRED VEKRNRVLEE EVKEFVKSME KPKTKTDP
