ID G1PSZ1_MYOLU Unreviewed; 458 AA.
AC G1PSZ1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Chimaerin {ECO:0000256|PIRNR:PIRNR038015};
DE AltName: Full=Chimerin {ECO:0000256|PIRNR:PIRNR038015};
GN Name=CHN1 {ECO:0000313|Ensembl:ENSMLUP00000014313.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000014313.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000014313.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000014313.2}
RP IDENTIFICATION.
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; AAPE02004666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02004667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02004668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PSZ1; -.
DR STRING; 59463.ENSMLUP00000014313; -.
DR Ensembl; ENSMLUT00000015714.2; ENSMLUP00000014313.2; ENSMLUG00000015709.2.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_015883_0_0_1; -.
DR InParanoid; G1PSZ1; -.
DR OMA; HMPSLRD; -.
DR TreeFam; TF342052; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
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:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
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; cd20856; C1_alphaCHN; 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; CHIMERIN FAMILY MEMBER; 1.
DR PANTHER; PTHR46075:SF1; N-CHIMAERIN; 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 4: Predicted;
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:UP000001074};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 48..116
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 204..254
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 267..458
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
SQ SEQUENCE 458 AA; 53041 MW; C719C7E5A9C0C175 CRC64;
CLFFSDTDEY RPPVWKSYLY QLQQEAPHPR RITCTNEVEN RPKYYGREFH GRISREAADQ
LLSVAEGSYL IRESQRQPGT YTLALRFGSQ TRNFRLYYDG KHFVGEKRFE SIHDLVTDGL
ITLYIETKAA EYIAKMTINP IYEHIGYTTL NREPAYQKHM PVLKETHDDK DSTGQDGVSE
KRLTSLVRRA TLKENEQIPK YEKVHNFKVH TFRGPHWCEY CANFMWGLIA QGVKCADCGL
NVHKQCSKMV PNDCKPDLKH VKKVYSCDLT TLVKAHITKR PMVVDMCIRE IESRGLNSEG
LYRVSGFSDL IEDVKMAFDR DGEKADISVN VYEDINIITG ALKLYFRDLP IPLITYDAYP
KFIESAKIMD PDEQLETLHE ALKLLPPAHC ETLRYLMAHL KRVTLHEKEN LMNAENLGIV
FGPTLMRSPE LDAMAALNDI RYQRLVVELL IKNEDILF
//
