ID   CHIO_RAT                Reviewed;         295 AA.
AC   Q03070;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 143.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Testis;
RX   PubMed=8440677; DOI=10.1016/s0021-9258(18)53543-2;
RA   Leung T., How B.E., Manser E., Lim L.;
RT   "Germ cell beta-chimaerin, a new GTPase-activating protein for p21rac, is
RT   specifically expressed during the acrosomal assembly stage in rat testis.";
RL   J. Biol. Chem. 268:3813-3816(1993).
CC   -!- FUNCTION: GTPase-activating protein for p21-rac.
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=2;
CC       Name=Beta-1;
CC         IsoId=Q03070-1; Sequence=Displayed;
CC       Name=Beta-2;
CC         IsoId=Q03070-2; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Found in cerebellum and testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed specifically in late stage
CC       spermatocytes. In the cerebellum, emergence of beta-2 isoform coincides
CC       with granule cells maturation and exhibits postnatal developmental
CC       increases. Expression is specifically reduced in weaver mutant.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X69489; CAA49244.1; -; mRNA.
DR   EMBL; L07494; AAA40809.1; -; mRNA.
DR   PIR; A45485; S29956.
DR   RefSeq; NP_114473.1; NM_032084.1. [Q03070-1]
DR   AlphaFoldDB; Q03070; -.
DR   SMR; Q03070; -.
DR   STRING; 10116.ENSRNOP00000012655; -.
DR   PaxDb; Q03070; -.
DR   PRIDE; Q03070; -.
DR   GeneID; 84031; -.
DR   KEGG; rno:84031; -.
DR   UCSC; RGD:620140; rat. [Q03070-1]
DR   CTD; 1124; -.
DR   RGD; 620140; Chn2.
DR   eggNOG; KOG1453; Eukaryota.
DR   InParanoid; Q03070; -.
DR   OrthoDB; 1300981at2759; -.
DR   Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR   PRO; PR:Q03070; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001565; F:phorbol ester receptor activity; TAS:RGD.
DR   GO; GO:0001675; P:acrosome assembly; IEP:RGD.
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   2: Evidence at transcript level;
KW   Alternative splicing; GTPase activation; Membrane; Metal-binding;
KW   Reference proteome; SH2 domain; Zinc; Zinc-finger.
FT   CHAIN           1..295
FT                   /note="Beta-chimaerin"
FT                   /id="PRO_0000056699"
FT   DOMAIN          104..295
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   ZN_FING         41..91
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
SQ   SEQUENCE   295 AA;  33837 MW;  D7692D957B4816BD CRC64;
     MLCTSPVNCL DSVCCTSINI SSLVRRAALT HNDNHFNYEK THNFKVHTFR GPHWCEYCAN
     FMWGLIAQGV RCSDCGLNVH KQCSKHVPND CQPDLKRIKK VYCCDLTTLV KAHNTQRPMV
     VDICIREIEA RGLKSEGLYR VSGFTEHIED VKMAFDRDGE KADISANIYP DINIITGALK
     LYFRDLPIPI ITYDTYTKFI EAAKISNADE RLEAVHEVLM LLPPAHYETL RYLMIHLKKV
     TMNEKDNLMN AENLGIVFGP TLMRPPEDST LTTLHDMRYQ KLIVQILIEN EDVLF