ID A0A452ER18_CAPHI Unreviewed; 1128 AA.
AC A0A452ER18;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Rho GTPase activating protein 45 {ECO:0000313|Ensembl:ENSCHIP00000014612.1};
GN Name=ARHGAP45 {ECO:0000313|Ensembl:ENSCHIP00000014612.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000014612.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000014612.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000014612.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; LWLT01000008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452ER18; -.
DR Ensembl; ENSCHIT00000022411.1; ENSCHIP00000014612.1; ENSCHIG00000015532.1.
DR GeneTree; ENSGT00950000183110; -.
DR OMA; PLACLCR; -.
DR Proteomes; UP000291000; Chromosome 7.
DR Bgee; ENSCHIG00000015532; Expressed in thymus and 17 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228:SF18; RHO GTPASE-ACTIVATING PROTEIN 45; 1.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 278..548
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 711..756
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 770..983
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 390..417
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 450..506
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 123745 MW; 8E0C1C8F37F770FB CRC64;
MFSRKKRELM KTPSISKKNR AGSPCPQPSG PHFTSRETEE LPRRDGADAV SLGPGLEPPS
VASNAKATGT LKRPTSLSRH ASAAGFPLSG TSTWTLGRSH RSPLSAASPA EAPIQGPCPD
TVEDISHLLA DVARFAEGLE KLKECVLRDE LLEARRPLAH ECLGEALRVM RQVISKYPLL
NTVETLTAAG TLIAKIKAFH YECNNESDKR EFEKALETIA VSFSSTVSEF LMGEVDSSIL
LSVPPGDPGQ SMENLYAQGS ESAPPSGEEC DAGCLSPEDV DTLLQRCEGG VDAALQYAKN
MAKYMKDLIG YLEKRSALEM DFAKGLQKIV QNCRQSVMQE PHMPLLSIYS LALEQDLEFG
HGLVQAVGTL LTQTFLQPLN LRRLEHEKRR KEIKESWHRA QRKLQEAESN LRKAKQGYMQ
RCEDHDKARF LVAKAEEEQA SIGPGAGGAA SKTLDKRRRL EEEAKNKAEE AMATYRTCVA
DAKTQKQELE DTKVTALRQI QEVIRQSDQT IKSATISYYQ MMHTQTAPLP VHFHMLYESS
KLYDPGQQYA SHVRQLQRGE EPDVHYDFEP HVPASAWSPV LRTRKSSFNV SDAVGAEAAS
SPPEDGGPSE GEIAKERRSG RGHQVHKSWP ISISDSEASL DPSPGSEDFK KFERMSSCGT
MLSNEELADQ EGSAGASAFD QADLNGMTPE LPVAMPSGPF RHVGLSKAAR THRLRKLRTP
AKCRECNSYV YFQGAECEEC CLACHKKCLE TLAIQCGHKK LQGHLQLFGQ DFSHAARSTP
DGVPFIIKKC IFEIEQRALR TKGIYRVNGV KTRVEKLCQA FENGKELVEL SQASPHDISN
VLKLYLRQLP EPLISFRLYH ELVGMAKDSL KAEAEAKAAS RGRPDATESE AAAMAMAGRL
RELLRDLPRE NWATLRYLMR HLRRIVEVEQ DNKMTPGNLG IVFGPTLLRP RPTEATVSLS
SLVDYPHQAC IVETLITHFS LVFEEEPEEA PGGQDGVSSQ RPEVVVQAPY LGGSGGAAFP
LTEEAEDGGL EPHVTSNDSD SELEEASDLQ SPAGGAALHR LSFLERQGGD AGTEGSQGSR
SGSEEQLGAT AGEYGPGCTT TSQYNATNRL RGGRLVGGNS CKRQPEFV
//
