CHIN_BOVIN
ID CHIN_BOVIN Reviewed; 334 AA.
AC Q17QN0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=N-chimaerin;
DE AltName: Full=A-chimaerin;
DE AltName: Full=Alpha-chimerin;
DE AltName: Full=N-chimerin;
DE Short=NC;
DE AltName: Full=Rho GTPase-activating protein 2;
GN Name=CHN1; Synonyms=ARHGAP2, CHN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase-activating protein for p21-rac and a phorbol ester
CC receptor. Involved in the assembly of neuronal locomotor circuits as a
CC direct effector of EPHA4 in axon guidance (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EPHA4; effector of EPHA4 in axon guidance
CC linking EPHA4 activation to RAC1 regulation. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent
CC (By similarity). {ECO:0000250}.
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DR EMBL; BC118265; AAI18266.1; -; mRNA.
DR RefSeq; NP_001068817.1; NM_001075349.1.
DR AlphaFoldDB; Q17QN0; -.
DR SMR; Q17QN0; -.
DR STRING; 9913.ENSBTAP00000010556; -.
DR PaxDb; Q17QN0; -.
DR PRIDE; Q17QN0; -.
DR GeneID; 508266; -.
DR KEGG; bta:508266; -.
DR CTD; 1123; -.
DR eggNOG; KOG1453; Eukaryota.
DR InParanoid; Q17QN0; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
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 GTPase activation; Metal-binding; Neurogenesis; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..334
FT /note="N-chimaerin"
FT /id="PRO_0000248046"
FT DOMAIN 143..334
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 80..130
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15882"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30337"
SQ SEQUENCE 334 AA; 38247 MW; B72383C5AC82E3A1 CRC64;
MPSKESWSGR KTNRATVHKS KQEGRQQDLL IAALGMKLGS QKSSVTIWQP LKLFAYSQLT
SLVRRATLKE NEQIPKYEKV HNFKVHTFRG PHWCEYCANF MWGLIAQGVK CADCGLNVHK
QCSKMVPNDC KPDLKHVKKV YSCDLTTLVK ARTTKRPMVV DMCIREIEAR GLNSEGLYRV
SGFSDLIEDV KMAFDRDGEK ADISVNMYED INIITGALKL YFRDLPIPLI TYDAYPKFIE
SAKIMDPDEQ LETLHEALKL LPPAHCETLR YLMAHLKRVT LHEKENLMNA ENLGIVFGPT
LMRSPELDAM AALNDIRYQR LVVELLIKNE DILF