ID L5K9F4_PTEAL Unreviewed; 682 AA.
AC L5K9F4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Rho GTPase-activating protein 22 {ECO:0000313|EMBL:ELK08339.1};
GN ORFNames=PAL_GLEAN10004414 {ECO:0000313|EMBL:ELK08339.1};
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:ELK08339.1, 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; KB030894; ELK08339.1; -; Genomic_DNA.
DR AlphaFoldDB; L5K9F4; -.
DR STRING; 9402.L5K9F4; -.
DR eggNOG; KOG4270; Eukaryota.
DR InParanoid; L5K9F4; -.
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; cd13378; PH_RhoGAP2; 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:SF22; RHO GTPASE-ACTIVATING PROTEIN 22; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT DOMAIN 19..127
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 137..331
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 334..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 591..667
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 355..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 74651 MW; 4C54142262231478 CRC64;
MGEQSRSPGR LSCPQKLGPV LKAGWLKKQR SIMKNWQQRW FVLRGDQLFY YKDKDETKPQ
GFISLQGTQV TELLPGPEDV GKHLFEISPG GAGEREKVPA NPEALLLMAS SQRDMEDWVQ
AIRRVIWAPF GGGIFGQRLE DTVHQERKYG PRLAPLLVEQ CVDFIRERGL TEEGLFRMPG
QANLVRDLQD SFDCGEKPLF DSTTDVHTVA SLLKLYLREL PEPVVPFARY EDFLSCAQLL
TKDEGEGTLE LAKQVSSLPL ANYNLLRYIC KFLDEVQSHS NVNKMSVQNL ATVFGPNILR
PQIEDPVTIM EGTSLVQHLM TVLIRRHGQL FTARATEGPA SPHGGTPCTV GWGSEEVTRD
SQAEPSSPGT PGLPSHRTSS LDGATVAALS RNSPLGPATS SSGKRMQTLP NWKSSFRQSG
SRSGSLKMGS SSLEVPIISS GGNWLMNGLS SLRGHRRASS GDRLKDSGSS QRLSTYDNVP
PPSLFPSTPS VASMAWSGAS SCEASAGGSI SSCTACRASD SSACSSLHTE AGLEPSPLPS
SSEDRRSPDL GHSQDEVGTC LSSSEPSNPG SPAQDHARRS EALQGLVTEL RAELCRQRTE
YETSVKRLEE ASADLKKRMS WLEEELDQEK KKYTMLEIKL RNSERAREDA EKRNQLLQKE
MEEFFSTLGS LTVGAKGAGA PK
//