CHIN_RAT
ID CHIN_RAT Reviewed; 334 AA.
AC P30337; Q505J4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 25-MAY-2022, entry version 145.
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 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=Brain;
RX PubMed=1445199; DOI=10.1042/bj2870415;
RA Lim H.H., Michael G.J., Smith P., Lim L., Hall C.;
RT "Developmental regulation and neuronal expression of the mRNA of rat n-
RT chimaerin, a p21rac GAP:cDNA sequence.";
RL Biochem. J. 287:415-422(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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.
CC -!- SUBUNIT: Interacts with EPHA4; effector of EPHA4 in axon guidance
CC linking EPHA4 activation to RAC1 regulation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In neurons in brain regions that are involved in
CC learning and memory processes.
CC -!- DEVELOPMENTAL STAGE: Increases in amount during brain development
CC coincident with synaptogenesis.
CC -!- PTM: Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent
CC (By similarity). {ECO:0000250}.
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DR EMBL; X67250; CAA47672.1; -; mRNA.
DR EMBL; BC094519; AAH94519.1; -; mRNA.
DR PIR; S29128; S29128.
DR RefSeq; NP_114472.1; NM_032083.1.
DR AlphaFoldDB; P30337; -.
DR SMR; P30337; -.
DR DIP; DIP-39378N; -.
DR IntAct; P30337; 2.
DR STRING; 10116.ENSRNOP00000060544; -.
DR iPTMnet; P30337; -.
DR PhosphoSitePlus; P30337; -.
DR PaxDb; P30337; -.
DR GeneID; 84030; -.
DR KEGG; rno:84030; -.
DR UCSC; RGD:620139; rat.
DR CTD; 1123; -.
DR RGD; 620139; Chn1.
DR eggNOG; KOG1453; Eukaryota.
DR HOGENOM; CLU_015883_0_0_1; -.
DR InParanoid; P30337; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; P30337; -.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:P30337; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P30337; RN.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
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:0001565; F:phorbol ester receptor activity; TAS:RGD.
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; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; TAS:RGD.
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 GTPase activation; Metal-binding; Neurogenesis; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..334
FT /note="N-chimaerin"
FT /id="PRO_0000056696"
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:0007744|PubMed:16641100"
FT CONFLICT 21
FT /note="K -> N (in Ref. 1; CAA47672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 38224 MW; D4DB599737D171FB CRC64;
MPSKESWSGR KTNRATVHKS KQEGRQQDLL IAALGMKLGS QKSSVTIWQP LKLFAYSQLT
SLVRRATLKE NEQIPKYEKV HNFKVHTFRG PHWCEYCANF MWGLIAQGVK CADCGLNVHK
QCSKMVPNDC KPDLKHVKKV YSCDLTTLVK AHITKRPMVV DMCIREIESR GLNSEGLYRV
SGFSDLIEDV KMAFDRDGEK ADISVNMYED INIITGALKL YFRDLPIPLI TYDAYPKFIE
SAKIVDPDEQ LETLHEALRS LPPAHCETLR YLMAHLKRVT LHEKENLMSA ENLGIVFGPT
LMRSPELDPM AALNDIRYQR LVVELLIKNE DILF
