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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
 
 
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