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Database: UniProt
Entry: H9ETX3_MACMU
LinkDB: H9ETX3_MACMU
Original site: H9ETX3_MACMU 
ID   H9ETX3_MACMU            Unreviewed;       468 AA.
AC   H9ETX3; A0A1D5RC06;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Chimaerin {ECO:0000256|PIRNR:PIRNR038015};
DE   AltName: Full=Chimerin {ECO:0000256|PIRNR:PIRNR038015};
GN   Name=CHN2 {ECO:0000313|EMBL:AFE65832.1,
GN   ECO:0000313|Ensembl:ENSMMUP00000057848.2,
GN   ECO:0000313|VGNC:VGNC:80861};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE65832.1};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|EMBL:AFE65832.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE65832.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
RN   [3] {ECO:0000313|Ensembl:ENSMMUP00000057848.2}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000057848.2};
RG   Ensembl;
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; JU322076; AFE65832.1; -; mRNA.
DR   RefSeq; NP_001248506.1; NM_001261577.1.
DR   PaxDb; 9544-ENSMMUP00000035186; -.
DR   Ensembl; ENSMMUT00000073602.2; ENSMMUP00000057848.2; ENSMMUG00000008329.4.
DR   GeneID; 697231; -.
DR   KEGG; mcc:697231; -.
DR   CTD; 1124; -.
DR   VEuPathDB; HostDB:ENSMMUG00000008329; -.
DR   VGNC; VGNC:80861; CHN2.
DR   eggNOG; KOG1453; Eukaryota.
DR   GeneTree; ENSGT01030000234635; -.
DR   HOGENOM; CLU_015883_0_0_1; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000008329; Expressed in cerebellum and 22 other cell types or tissues.
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; 1.
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   2: Evidence at transcript level;
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:UP000006718};
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..468
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   468 AA;  53854 MW;  7C451F4992DB8E17 CRC64;
     MAASSNSSLS GSSVSSDAEE YQPPIWKSYL YQLQQEAPRP KRIICPREVE NRPKYYGREF
     HGIISREQAD ELLGGVEGAY ILRESQRQPG CYTLALRFGN QTLNYRLFHD GKHFVGEKRF
     ESIHDLVTDG LITLYIETKA AEYISKMTTN PIYEHIGYAT LLREKVSRKL SKSKNEPRKT
     NVTHEEHTAV DKISSLVRRA ALTHNDNHFN YEKTHNFKVH TFRGPHWCEY CANFMWGLIA
     QGVRCSDCGL NVHKQCSKHV PNDCQPDLKR IKKVYCCDLT TLVKAHNTQR PMVVDICIRE
     IEARGLKSEG LYRVSGFTEH IEDVKMAFDR DGEKADISAN VYPDINIITG ALKLYFRDLP
     IPVITYDTYS KFIDAAKISN ADERLEAVHE VLMLLPPAHY ETLRYLMIHL KKVTMNEKDN
     FMNAENLGIV FGPTLMRPPE DSTLTTLHDM RYQKLIVQIL IENEDVLF
//
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