ID M3Y0N2_MUSPF Unreviewed; 494 AA.
AC M3Y0N2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Chimaerin {ECO:0000256|PIRNR:PIRNR038015};
DE AltName: Full=Chimerin {ECO:0000256|PIRNR:PIRNR038015};
GN Name=CHN2 {ECO:0000313|Ensembl:ENSMPUP00000004883.1,
GN ECO:0000313|RefSeq:XP_044918765.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000004883.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000004883.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_044918765.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044918765.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: GTPase-activating protein for p21-rac.
CC {ECO:0000256|PIRNR:PIRNR038015}.
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DR EMBL; AEYP01056392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_044918765.1; XM_045062830.1.
DR STRING; 9669.ENSMPUP00000004883; -.
DR Ensembl; ENSMPUT00000004967.1; ENSMPUP00000004883.1; ENSMPUG00000004923.1.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_015883_0_0_1; -.
DR OMA; HCKTIFA; -.
DR OrthoDB; 5395569at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20857; C1_betaCHN; 1.
DR CDD; cd04372; RhoGAP_chimaerin; 1.
DR CDD; cd10352; SH2_a2chimerin_b2chimerin; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035840; Chimaerin_SH2.
DR InterPro; IPR017356; CHN1/CHN2.
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 InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR46075:SF4; BETA-CHIMAERIN; 1.
DR PANTHER; PTHR46075; CHIMERIN FAMILY MEMBER; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF038015; N-chimaerin; 2.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|PIRNR:PIRNR038015};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038015};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 59..127
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 214..264
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 277..494
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 56601 MW; 9BA421DB736B9041 CRC64;
MAASSNSSLS GSSVSSDAEE YQPPIWKSYL YQLQQEAPRP KRIICAGEVE NRPKYYGREF
HGIISREQAD ELLGGVEGAY ILRESQRQPG CYTLALRFGN QTLNYRLFYD GKHFVGEKRF
ESIHDLVTDG LITLYIETKA SEYISKMTTN PIYEHIGYAT LLREKVSRRL SRSKNESRKT
SVTNEEHTTV EKISSLVRRA ALTHNDNHFN YEKTHNFKVH TFRGPHWCEY CANFMWGLIA
QGVRCSDCGL NVHKQCSKHV PNDCQPDLKR IKKVYCCDLT TLVKAHNTQR PMVVDICIRE
IEARGLKSEG LYRVSGFTEH IEDVKMAFDR DGEKADISAN IYPDINIITG ALKLYFRDLP
IPVITYDTYP KFIEAAKISN ADERLEAVHD VLMLLPPAHY ETLRYLMIHL KNSTTNIQKT
SIPENKNLGD CNFIPLGRVT LNEKDNLMNA ENLGIVFGPT LMRSPEDSTL TTLHDMRYQK
LIVQILIENE DVLF
//
