ID L5KT95_PTEAL Unreviewed; 620 AA.
AC L5KT95;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Rho GTPase-activating protein 25 {ECO:0000313|EMBL:ELK14642.1};
GN ORFNames=PAL_GLEAN10021174 {ECO:0000313|EMBL:ELK14642.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK14642.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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DR EMBL; KB030567; ELK14642.1; -; Genomic_DNA.
DR RefSeq; XP_006909591.1; XM_006909529.1.
DR AlphaFoldDB; L5KT95; -.
DR STRING; 9402.L5KT95; -.
DR eggNOG; KOG4270; Eukaryota.
DR InParanoid; L5KT95; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13263; PH_RhoGap25-like; 1.
DR CDD; cd04390; RhoGAP_ARHGAP22_24_25; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228:SF20; RHO GTPASE-ACTIVATING PROTEIN 25; 1.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT DOMAIN 20..125
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 134..328
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 330..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 70196 MW; 17108BC5837BB284 CRC64;
MTGEQMAAFH QSSTPNPLER PIKMGWLKKQ RSIVKNWQQR YFVLRAQQLY YYKDEEDVKP
QGYMYLPGST IKEIATNPEE AGKFVFEVIP ASWDQSRTGQ DSYILMASSQ AEMEEWVKFL
RRVAGTPSGA VFGQRLDETV AYEQKFGPHL VPILVEKCAE FILEHGLNEE GIFRLPGQDN
LVKQLRDAFD AGERPSFDRD TDVHTVASLL KLYLRDLPEP VIPWSQYEGF LLCGQLMNAD
EAKAQQELMK QLSILPQDNY SLLSYICRFL HEIQLNCAVN KMSVDNLATV IGVNLIRSKV
EDPAVIMKGT PQIQRVMTMM IRDHEVLFPK SKDAPLSPPA QKNDPKKPPV ARSSVGWDAT
EDAPISRTDS FSNMTKDSEA TSPTGQQPND GCLGDGSKPP REKPGDWKLQ SRKRTQTLPN
RKCFLTAAFQ GANSNKVEIF KNEFWSPSSE VKAEEGHRRT LSQGVPNFSD IQRTSTYDNV
PTLPGSPGNE AGAVSFHACD SKKDTLASPS SETGPGTKNS GEEELESLQR MVQELQKEIE
TQKKMYEEQI KNLEKENYDV WAKVVRLSEE LEKEKKNSAA LEISLRNVER CREDVERRNK
ALEEEVKEFV KSMKEPKTDA
//