CHIO_MOUSE
ID CHIO_MOUSE Reviewed; 332 AA.
AC Q80XD1; Q9D9W2; Q9ER57;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Beta-chimaerin;
DE AltName: Full=Beta-chimerin;
DE AltName: Full=Rho GTPase-activating protein 3;
GN Name=Chn2; Synonyms=Arhgap3, Bch;
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 3).
RC TISSUE=Testis;
RA Prumer A., Heinlein U.A.O.;
RT "Characterization of mouse beta chimaerin.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 1).
RC TISSUE=Brain;
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=Brain, 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 p21-rac. {ECO:0000250}.
CC -!- ACTIVITY REGULATION: In the inactive state, the N terminus protrudes
CC into the active site of the Rho-GAP domain, sterically blocking Rac
CC binding. Phospholipid binding to the Phorbol-ester/DAG-type zinc-
CC finger/C1 domain triggers the cooperative dissociation of these
CC interactions, allowing the N-terminus to move out of the active site
CC and thereby activating the enzyme (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80XD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80XD1-2; Sequence=VSP_014244, VSP_014245;
CC Name=3;
CC IsoId=Q80XD1-3; Sequence=VSP_014243, VSP_014246;
CC -!- SEQUENCE CAUTION: [Isoform 3]:
CC Sequence=CAC08453.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ279014; CAC08453.1; ALT_FRAME; mRNA.
DR EMBL; AK006398; BAB24568.1; -; mRNA.
DR EMBL; BC051139; AAH51139.1; -; mRNA.
DR CCDS; CCDS20154.1; -. [Q80XD1-1]
DR CCDS; CCDS80535.1; -. [Q80XD1-2]
DR CCDS; CCDS80536.1; -. [Q80XD1-3]
DR RefSeq; NP_001298062.1; NM_001311133.1. [Q80XD1-2]
DR RefSeq; NP_001298063.1; NM_001311134.1. [Q80XD1-3]
DR RefSeq; NP_076032.2; NM_023543.2. [Q80XD1-1]
DR AlphaFoldDB; Q80XD1; -.
DR SMR; Q80XD1; -.
DR BioGRID; 213803; 71.
DR IntAct; Q80XD1; 4.
DR MINT; Q80XD1; -.
DR STRING; 10090.ENSMUSP00000035908; -.
DR PhosphoSitePlus; Q80XD1; -.
DR MaxQB; Q80XD1; -.
DR PaxDb; Q80XD1; -.
DR PRIDE; Q80XD1; -.
DR ProteomicsDB; 283828; -. [Q80XD1-1]
DR ProteomicsDB; 283829; -. [Q80XD1-2]
DR ProteomicsDB; 283830; -. [Q80XD1-3]
DR DNASU; 69993; -.
DR Ensembl; ENSMUST00000067741; ENSMUSP00000066078; ENSMUSG00000004633. [Q80XD1-1]
DR Ensembl; ENSMUST00000114401; ENSMUSP00000110043; ENSMUSG00000004633. [Q80XD1-3]
DR Ensembl; ENSMUST00000146114; ENSMUSP00000114476; ENSMUSG00000004633. [Q80XD1-2]
DR GeneID; 69993; -.
DR KEGG; mmu:69993; -.
DR UCSC; uc009bzr.2; mouse. [Q80XD1-2]
DR UCSC; uc009bzt.2; mouse. [Q80XD1-1]
DR CTD; 1124; -.
DR MGI; MGI:1917243; Chn2.
DR VEuPathDB; HostDB:ENSMUSG00000004633; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR InParanoid; Q80XD1; -.
DR PhylomeDB; Q80XD1; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 69993; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Chn2; mouse.
DR PRO; PR:Q80XD1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80XD1; protein.
DR Bgee; ENSMUSG00000004633; Expressed in cerebellum lobe and 219 other tissues.
DR ExpressionAtlas; Q80XD1; baseline and differential.
DR Genevisible; Q80XD1; MM.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd04372; RhoGAP_chimaerin; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037860; RhoGAP_chimaerin.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Membrane; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..332
FT /note="Beta-chimaerin"
FT /id="PRO_0000056698"
FT DOMAIN 141..332
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 78..128
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014243"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014244"
FT VAR_SEQ 51..56
FT /note="LFACSQ -> MALQCR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014245"
FT VAR_SEQ 56
FT /note="Q -> M (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014246"
FT CONFLICT 138
FT /note="V -> G (in Ref. 3; AAH51139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 38218 MW; 164E8E735053E744 CRC64;
MCSQELWLEN ERKCAMVRKS KPSRKRQELL AIAFGVKVGL KGGFLWSPLK LFACSQISSL
VRRAALTHND NHFNYEKTHN FKVHTFRGPH WCEYCANFMW GLIAQGVRCS DCGLNVHKQC
SKHVPNDCQP DLKRIKKVYC CDLTTLVKAH NTQRPMVVDI CIREIEARGL KSEGLYRVSG
FTEHIEDVKM AFDRDGEKAD ISANIYPDIN IITGALKLYF RDLPIPIITY DTYSKFIEAA
KISNADERLE AVHEVLMLLP PAHYETLRYL MIHLKKVTMN EKDNLMNAEN LGIVFGPTLM
RPPEDSTLTT LHDMRYQKLI VQILIENEDV LF
