CHIN_MOUSE
ID CHIN_MOUSE Reviewed; 459 AA.
AC Q91V57; A2ATM0; Q3UGY3; Q7TQE5; Q8BWU6; Q9D9B3;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 175.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, Colon, and Eye;
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 [5]
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH EPHA4.
RX PubMed=17719550; DOI=10.1016/j.cell.2007.07.022;
RA Iwasato T., Katoh H., Nishimaru H., Ishikawa Y., Inoue H., Saito Y.M.,
RA Ando R., Iwama M., Takahashi R., Negishi M., Itohara S.;
RT "Rac-GAP alpha-chimerin regulates motor-circuit formation as a key mediator
RT of EphrinB3/EphA4 forward signaling.";
RL Cell 130:742-753(2007).
RN [6]
RP FUNCTION IN EPHA4 SIGNALING, INTERACTION WITH EPHA4; EPHB1 AND EPHB2, AND
RP PHOSPHORYLATION.
RX PubMed=17785183; DOI=10.1016/j.neuron.2007.07.036;
RA Beg A.A., Sommer J.E., Martin J.H., Scheiffele P.;
RT "alpha2-Chimaerin is an essential EphA4 effector in the assembly of
RT neuronal locomotor circuits.";
RL Neuron 55:768-778(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: GTPase-activating protein for p21-rac and a phorbol ester
CC receptor. May play an important role in neuronal signal-transduction
CC mechanisms (By similarity). Involved in the assembly of neuronal
CC locomotor circuits as a direct effector of EPHA4 in axon guidance.
CC {ECO:0000250, ECO:0000269|PubMed:17785183}.
CC -!- SUBUNIT: Interacts with EPHA4; effector of EPHA4 in axon guidance
CC linking EPHA4 activation to RAC1 regulation. May also interact with
CC EPHB1 and EPHB2. {ECO:0000269|PubMed:17719550,
CC ECO:0000269|PubMed:17785183}.
CC -!- INTERACTION:
CC Q91V57-1; Q03137: Epha4; NbExp=2; IntAct=EBI-1539203, EBI-1539152;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q91V57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91V57-2; Sequence=VSP_020145;
CC Name=3;
CC IsoId=Q91V57-3; Sequence=VSP_020146;
CC -!- PTM: Phosphorylated. Phosphorylation is EPHA4 kinase activity-
CC dependent. {ECO:0000269|PubMed:17785183}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile but display a loss of
CC coordination of limb movement which phenocopies the one of Epha4 mutant
CC mice. {ECO:0000269|PubMed:17719550}.
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DR EMBL; AF332069; AAK56097.1; -; mRNA.
DR EMBL; AF332070; AAK56098.1; -; mRNA.
DR EMBL; AK049943; BAC33996.1; -; mRNA.
DR EMBL; AK007182; BAB24888.1; -; mRNA.
DR EMBL; AK075606; BAC35853.1; -; mRNA.
DR EMBL; AK147686; BAE28074.1; -; mRNA.
DR EMBL; AL928889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010825; AAH10825.1; -; mRNA.
DR EMBL; BC024796; AAH24796.1; -; mRNA.
DR EMBL; BC025023; AAH25023.1; -; mRNA.
DR EMBL; BC054770; AAH54770.1; -; mRNA.
DR CCDS; CCDS16133.1; -. [Q91V57-2]
DR CCDS; CCDS38145.1; -. [Q91V57-3]
DR CCDS; CCDS50608.1; -. [Q91V57-1]
DR RefSeq; NP_001106717.2; NM_001113246.2. [Q91V57-1]
DR RefSeq; NP_083992.1; NM_029716.3. [Q91V57-3]
DR RefSeq; NP_786928.2; NM_175752.3. [Q91V57-2]
DR AlphaFoldDB; Q91V57; -.
DR SMR; Q91V57; -.
DR BioGRID; 224378; 5.
DR IntAct; Q91V57; 1.
DR MINT; Q91V57; -.
DR STRING; 10090.ENSMUSP00000107655; -.
DR iPTMnet; Q91V57; -.
DR PhosphoSitePlus; Q91V57; -.
DR MaxQB; Q91V57; -.
DR PaxDb; Q91V57; -.
DR PRIDE; Q91V57; -.
DR ProteomicsDB; 281666; -. [Q91V57-1]
DR ProteomicsDB; 281667; -. [Q91V57-2]
DR ProteomicsDB; 281668; -. [Q91V57-3]
DR Antibodypedia; 33886; 451 antibodies from 29 providers.
DR DNASU; 108699; -.
DR Ensembl; ENSMUST00000070579; ENSMUSP00000070301; ENSMUSG00000056486. [Q91V57-3]
DR Ensembl; ENSMUST00000102677; ENSMUSP00000099738; ENSMUSG00000056486. [Q91V57-2]
DR Ensembl; ENSMUST00000112024; ENSMUSP00000107655; ENSMUSG00000056486. [Q91V57-1]
DR Ensembl; ENSMUST00000180045; ENSMUSP00000137106; ENSMUSG00000056486. [Q91V57-3]
DR Ensembl; ENSMUST00000229731; ENSMUSP00000155037; ENSMUSG00000056486. [Q91V57-3]
DR GeneID; 108699; -.
DR KEGG; mmu:108699; -.
DR UCSC; uc008kda.2; mouse. [Q91V57-2]
DR UCSC; uc008kdb.2; mouse. [Q91V57-1]
DR CTD; 1123; -.
DR MGI; MGI:1915674; Chn1.
DR VEuPathDB; HostDB:ENSMUSG00000056486; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_015883_0_0_1; -.
DR InParanoid; Q91V57; -.
DR OMA; QQGVKCE; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q91V57; -.
DR TreeFam; TF342052; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 108699; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Chn1; mouse.
DR PRO; PR:Q91V57; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91V57; protein.
DR Bgee; ENSMUSG00000056486; Expressed in dentate gyrus of hippocampal formation granule cell and 211 other tissues.
DR ExpressionAtlas; Q91V57; baseline and differential.
DR Genevisible; Q91V57; MM.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0050770; P:regulation of axonogenesis; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd04372; RhoGAP_chimaerin; 1.
DR CDD; cd10352; SH2_a2chimerin_b2chimerin; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.505.10; -; 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 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; SSF48350; SSF48350; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF57889; SSF57889; 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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; GTPase activation; Metal-binding;
KW Neurogenesis; Phosphoprotein; Reference proteome; SH2 domain; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P15882"
FT CHAIN 2..459
FT /note="N-chimaerin"
FT /id="PRO_0000056695"
FT DOMAIN 49..135
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 268..459
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 205..255
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P15882"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15882"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30337"
FT VAR_SEQ 1..249
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020146"
FT VAR_SEQ 1..183
FT /note="MALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRVTCTCEVENRPKYYGREYHG
FT MISREETDQLLSVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFE
FT SIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHIGYTTLNREPAYKQHMAVLKETHDE
FT KEATGQDGVSEKR -> MPSKESWSGRKANRATVHKAKPEGRQQGLLIAALGMKLGSQK
FT SSVTIWQPLKLFAYSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11471062,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_020145"
FT CONFLICT 253
FT /note="N -> I (in Ref. 4; AAH54770)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="K -> E (in Ref. 2; BAE28074)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="N -> K (in Ref. 2; BAC33996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 53193 MW; EE10CCDA8229C0B0 CRC64;
MALTLFDTDE YRPPVWKSYL YQLQQEAPHP RRVTCTCEVE NRPKYYGREY HGMISREETD
QLLSVAEGSY LIRESQRQPG TYTLALRFGS QTRNFRLYYD GKHFVGEKRF ESIHDLVTDG
LITLYIETKA AEYIAKMTIN PIYEHIGYTT LNREPAYKQH MAVLKETHDE KEATGQDGVS
EKRLTSLVRR ATLKENEQIP KYEKVHNFKV HTFRGPHWCE YCANFMWGLI AQGVKCADCG
LNVHKQCSKM VPNDCKPDLK HVKKVYSCDL TTLVKAHITK RPMVVDMCIR EIESRGLNSE
GLYRVSGFSD LIEDVKMAFD RDGEKADISV NMYEDINIIT GALKLYFRDL PIPLITYDAY
PKFIESAKIM DPDEQLETLH EALRSLPPAH CETLRYLMAH LKRVTLHEKE NLMSAENLGI
VFGPTLMRSP ELDPMAALND IRYQRLVVEL LIKNEDILF
