RHG22_MOUSE
ID RHG22_MOUSE Reviewed; 702 AA.
AC Q8BL80; Q6QHH6; Q8BVH4; Q8CHY5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Rho GTPase-activating protein 22;
DE AltName: Full=Rho-type GTPase-activating protein 22;
DE AltName: Full=p68RacGAP;
GN Name=Arhgap22;
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), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-201.
RX PubMed=14966113; DOI=10.1074/jbc.m311721200;
RA Aitsebaomo J., Wennerberg K., Der C.J., Zhang C., Kedar V., Moser M.,
RA Kingsley-Kallesen M.L., Zeng G.-Q., Patterson C.;
RT "p68RacGAP is a novel GTPase-activating protein that interacts with
RT vascular endothelial zinc finger-1 and modulates endothelial cell capillary
RT formation.";
RL J. Biol. Chem. 279:17963-17972(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Olfactory bulb;
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 MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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: Rho GTPase-activating protein involved in the signal
CC transduction pathway that regulates endothelial cell capillary tube
CC formation during angiogenesis. Acts as a GTPase activator for the RAC1
CC by converting it to an inactive GDP-bound state. Inhibits RAC1-
CC dependent lamellipodia formation. May also play a role in transcription
CC regulation via its interaction with VEZF1, by regulating activity of
CC the endothelin-1 (EDN1) promoter. {ECO:0000269|PubMed:14966113}.
CC -!- SUBUNIT: Interacts with VEZF1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14966113}. Nucleus
CC {ECO:0000269|PubMed:14966113}. Note=Mainly cytoplasmic. Some fraction
CC is nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BL80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BL80-2; Sequence=VSP_023706;
CC Name=3;
CC IsoId=Q8BL80-3; Sequence=VSP_023706, VSP_023707;
CC -!- TISSUE SPECIFICITY: Predominantly present in endothelial cells (at
CC protein level). {ECO:0000269|PubMed:14966113}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32603.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC37178.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY541447; AAS47033.1; -; mRNA.
DR EMBL; AK046097; BAC32603.1; ALT_FRAME; mRNA.
DR EMBL; AK078218; BAC37178.1; ALT_FRAME; mRNA.
DR EMBL; BC038272; AAH38272.1; -; mRNA.
DR CCDS; CCDS26926.2; -. [Q8BL80-1]
DR RefSeq; NP_722495.3; NM_153800.4. [Q8BL80-1]
DR RefSeq; XP_011243355.1; XM_011245053.2. [Q8BL80-1]
DR AlphaFoldDB; Q8BL80; -.
DR SMR; Q8BL80; -.
DR BioGRID; 232034; 6.
DR CORUM; Q8BL80; -.
DR IntAct; Q8BL80; 1.
DR STRING; 10090.ENSMUSP00000107587; -.
DR iPTMnet; Q8BL80; -.
DR PhosphoSitePlus; Q8BL80; -.
DR REPRODUCTION-2DPAGE; Q8BL80; -.
DR jPOST; Q8BL80; -.
DR MaxQB; Q8BL80; -.
DR PaxDb; Q8BL80; -.
DR PeptideAtlas; Q8BL80; -.
DR PRIDE; Q8BL80; -.
DR ProteomicsDB; 255329; -. [Q8BL80-1]
DR ProteomicsDB; 255330; -. [Q8BL80-2]
DR ProteomicsDB; 255331; -. [Q8BL80-3]
DR Antibodypedia; 58456; 156 antibodies from 26 providers.
DR DNASU; 239027; -.
DR Ensembl; ENSMUST00000111956; ENSMUSP00000107587; ENSMUSG00000063506. [Q8BL80-1]
DR GeneID; 239027; -.
DR KEGG; mmu:239027; -.
DR UCSC; uc007szm.2; mouse. [Q8BL80-1]
DR CTD; 58504; -.
DR MGI; MGI:2443418; Arhgap22.
DR VEuPathDB; HostDB:ENSMUSG00000063506; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00950000183015; -.
DR HOGENOM; CLU_020795_0_0_1; -.
DR InParanoid; Q8BL80; -.
DR OMA; NEDLACS; -.
DR OrthoDB; 917149at2759; -.
DR PhylomeDB; Q8BL80; -.
DR TreeFam; TF323577; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 239027; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Arhgap22; mouse.
DR PRO; PR:Q8BL80; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BL80; protein.
DR Bgee; ENSMUSG00000063506; Expressed in ectoplacental cone and 94 other tissues.
DR ExpressionAtlas; Q8BL80; baseline and differential.
DR Genevisible; Q8BL80; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
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; Angiogenesis; Coiled coil; Cytoplasm;
KW Developmental protein; Differentiation; GTPase activation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..702
FT /note="Rho GTPase-activating protein 22"
FT /id="PRO_0000280470"
FT DOMAIN 43..151
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 161..355
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 360..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 594..691
FT /evidence="ECO:0000255"
FT COMPBIAS 373..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5H3"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5H3"
FT VAR_SEQ 1..131
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14966113,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023706"
FT VAR_SEQ 226..295
FT /note="STTDVHTVASLLKLYLRELPEPVIPFARYEDFLSCAQLLTKDEGEGTVELAK
FT QVSNLPQANYNLLRYICK -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023707"
FT MUTAGEN 201
FT /note="R->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:14966113"
FT CONFLICT 487
FT /note="L -> R (in Ref. 2; BAC32603/BAC37178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 702 AA; 77786 MW; 48D0D339C89C2BED CRC64;
MLPTASSKRR TFAARYFTRS KSLVMGEQSR SPGRPLVPHK LGPVLKAGWL RKQRSIMKNW
QQRWFVLRGD QLFYYKDKDE SKPQGFISLQ GTQVTELLPD PEDPGKHLFE ITPGGATERE
KVPANPEALL LMASSQRDME DWVQAIRRVI WAPLGRGIFG QRLEDTVHHE RKFGPRLAPL
LVEQCVDFIR ERGLSEEGLF RMPGQANLVR DLQDSFDCGE KPLFDSTTDV HTVASLLKLY
LRELPEPVIP FARYEDFLSC AQLLTKDEGE GTVELAKQVS NLPQANYNLL RYICKFLDEV
QAHSDVNKMS VQNLATVFGP NILRPQIEDP VTIMEGTSLV QHLMTVLIRK HGQLFAATSL
EEPASPHGTV EWGSEEVTRD HRGEPGSPGL PTHRTSSLDG PAAAVLSRTS PPRLGSQTGP
AATSPGKKMH TLPVWKSSFR QQGSRSESPK GVNSSLEVPI ISSGGNWLIN GLSSLRSHRR
ASSGDRLKDT GSAQRLSTYD NVPPSSQFSS TASVASTSWS VASSSREASV SSCTACRASN
SSACSSLHTE WALEPSPLPS SSEGHQSPDL GHSLDEPCVG SGSSEPNDPG SPTQAHVRRC
RALQGQVAEL RAELCQQRTE YKRSLKSIEE GSADLRKQMS RLEEELDQER KKYAMLEIKL
RNSERAREDA ERRNQLLQRE MEEFFSTLGS LTTGTKGSRA PE
