ID A0A3Q3G8R5_KRYMA Unreviewed; 1486 AA.
AC A0A3Q3G8R5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Rho GTPase-activating protein 23-like {ECO:0000313|Ensembl:ENSKMAP00000020452.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000020452.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000020452.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_017293392.1; XM_017437903.1.
DR Ensembl; ENSKMAT00000020720.1; ENSKMAP00000020452.1; ENSKMAG00000015162.1.
DR GeneTree; ENSGT00940000157982; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01253; PH_ARHGAP21-like; 1.
DR CDD; cd04395; RhoGAP_ARHGAP21; 1.
DR Gene3D; 2.30.42.10; -; 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; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
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; PTHR23175; PDZ DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23175:SF5; RHO GTPASE-ACTIVATING PROTEIN 23; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50106; PDZ; 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:UP000264800}.
FT DOMAIN 52..162
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 760..877
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 963..1154
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 9..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1486 AA; 165459 MW; 0D27D11FC1BA0EA7 CRC64;
MNGAAFCLVG TPPYPDSEAK GQRDGMVSSR ENRRRPLSSG EVEGVSWQGP RTIFLKKNLQ
GFGFTLRHFI VYPPESSLHS LKDEENGNSS GKGCHRSHLE PMDTIFVKSV KENGPAHQAG
LCTGDRLVKV NGESILGKTY SQVIALIQNS ENILELSIMP KDEDVLQLVS VYSQDAYLKG
NEPYTGESQN LPEPPPLCYA STKPGSSLLD NCRTSTTSPL DNRPLPASTP SSGPPRAPEE
SSSHWSSSKQ HRGRSSSAIS ALEFHFANHS AAIASASLPP PRKNSLPASA RTHTGALCHQ
ALSDWYYSQA EATELMSPRH HSISQEYLAE LGLGLPLGPR HTATSTKQHQ RENLLQHYQA
SSASHDSYWL GDRGSGSSPG NRLCSQRLLA AYSEYEHNYG RSVETLAEAS ALVSQQYDHT
VQGSHMTKFR EQKEQTYSGV HQHQAAGTAL CSTPPSGRQS GQQVAEPQTR RLKDKELVGY
KSYSPSFSHK AGHLLQQAHS FREPTYTGPY LNWNPGRSRD SDGEIPPRPQ STPAPSASEE
EKVRLREDRV VGSPVSLTQE VVLRQKLPVN SRKPVQALQH PHYTRPANSP ELPGWNPSSG
TPSPLPGVMG PSHRANGSLA QHALDSLSSV PFIDESCSPN TDHQACSVVS TSQASTVSTL
TSTFVSHTLS MSPFVQLRSQ DCSSIKSRRS SYLLAITTER SMSYDEGLNT FREEGRVFSK
LPKRVKSFFA DRSLESLRDR EEARFKRHST SELGTITVSD VRKEGWLHYK QILTEKGKKL
GGSMRLWKRV FTVLHHNSLF LYKDKREAVL HGAGTGPCQD EHPPISIMGC LIDIAYSETK
RKHTLRLTTQ NFCEYLLQAE DRDDMLAWIR VIGEGSKTDN EEIGFSRQAL IDKKIKDYRK
HSLTGNKPDS TPRAHCMIPP FLLVKTDNSS ANRALRSEDH KALWGINIMK KNKKAGGPKA
FGVRLEDCQP AVHHKFVPLI VEKCCGVVEA TGLEYTGIYR VPGNNAMVSS LQEHLNKGMD
INAAEERCQD LNVISSLLKS FFRKLPEPLF TDDKYHKFID ANRIEDAEDR LKTMKKLIHD
LPDHYYHTMQ FLVGHLKRVA DHSEKNKMEP RNLALVFGPT LVRTSEDNMT DMVTHMPDRY
KIVETLILHY DWFFSGGELR REETESEEKQ DMQPVPNIDH LLTNIGRPGM PREMSDCTTS
GSVKSKVFSS SKRDLNAKDF LPKSIISAVT RKRKKCLSTH LAGNSADEDS EHKPVKATNY
GEEEGEEEED RGKKEPNEGV HNCSKKEKRL ENVVIAADTG TDSSAKHHPN ISLCSHQQTH
ATYIKPPPAT NTPSYLRSHS TASGRPTIPL WISPSRPPNL HWASGSPGFQ QPDWSQAAPV
HYRKTRGGRI RATSMNLDLD LGLSEDRVRG WMSSRMKVIR VSEGKPPDHG SIIRSSSAQQ
TDPFPLSSSS GRINSGSQES YSVVLRRSAH DPRDKTRVWR RHTVVV
//