ID A0A2U9CKU6_SCOMX Unreviewed; 1509 AA.
AC A0A2U9CKU6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative rho GTPase-activating protein 23-like {ECO:0000313|EMBL:AWP17157.1};
GN ORFNames=SMAX5B_016690 {ECO:0000313|EMBL:AWP17157.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP17157.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP17157.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP026260; AWP17157.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000032138; -.
DR Proteomes; UP000246464; Chromosome 18.
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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 55..165
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 785..902
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 988..1179
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 23..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1509 AA; 166487 MW; 53C9D4D81E9BD3D2 CRC64;
MWVSGVGRVV RRVDSLTLSM KAKGRRDGMV SSNGNRRRPL SSGEVEGVSW QGPRTIFLQK
NSQGFGFTLR HFIVYPPESS LHSIKDEENG NATGSGCRWS RLEPMDTIFV KSVKENGPAH
QAGLCTGDRL VKVNGESILG RTYSQVIALI QNSENILELS IMPKDEDVLQ LAYSQDAYLK
GNEPYSGEAQ NLPEPPPPCY ASPKPSSAAS EPSHHLPGLP DNWQCRSGPT TSPLDNHPPS
ASTPTSGWPG GPKDSSGHFS LPGRHRGISA LDFHFANHNA AIASATLPPP RKSSLPASAR
AHADALCHQA LSEWYYSQAE AAEHMSPRHR SISQDRLVEL GLGLALGPGP TSVPATSSEQ
RRRESLLHHQ QAAAASHDSF WLGGWGGVSG SASRSCSEGL LAAYAEYEHN YGRSVETLAQ
ASALVSPRHE NTSKSSQMKK LSKQTDHKAA EGHQHQTTVT PPATIASTVP PSGRQSGQQV
AEPQTRRVKE EEPVGYKSYS PSFSHKADHL LQQAQSFREP SYSGPHLTWS PSDRCGPAEG
KGLVVPRPQS TPALSTSEEE RALLGEDREV ISPISLNQEV VLRQKPPSGR RTSDQPLRHP
HYSTRAESPD PPALTPSPGI PSPVSVGPGP NRRANGSLAQ HAYDSLSSIP FIDEPTSPST
DQQACYVPAH SVVSGSQAST MAILTSTSVS PTLFSISSFV RLHCQDCSSI KGRRSSYLLA
ITTERSKSCD EGLNTFREEG RVFSKLPKRV KSFFTDGSLE SLRAQEEARS KRHSTSELGT
ITFSDVRKEG WLHYKQILTE KGKKVGGGMR PWKRVFSVLR SNLLFLYKDK REAVLHGAGA
GPSQDEHPPV GIRGCLIDIA YSETKRKHTL RLTTQDFCEY LLQAEDRDDM LAWIRVIREN
SKTDNEEIGF SRQALINKKL NDYRKHSLTG SKPDSSPRVH RMMPPFLLAK TDNASVNRAS
RADDYKALWG INLMKKAKKT GSPKAFGVRL EDCQPAVNHK FVPLTVEMCC DMVEATGLEY
TGIYRVPGNN AMVSNLQEHL NKGMDINTAE ERWQDLNVIS SLLKSFFRKL PEPLFTDDKY
IDFIDANRIE DAEDRLKTMK KLLHDLPDHY YHTLKFLVGH LKKVADNAEK NKMEPRNLAL
VFGPTLVRTS EDNMTDMVTH MPDRYKIVET LILHCDWFFS DGAIDKEEKA PEDKRDMQPV
PNIDHLLSNI GRPGMPGEAS DSTTSDSLKS KHSLSSKKDL NARDLMPKSI ITAVTRKRKK
CLSVHLPSSS ADEDSEHEPF KAINYRGGEG GGGGEEFKGE EEVVKGEHIP KKEKWDEKGN
CLKNAKKTAE KDSLVEGEEA GKDVEKEMAN GTPNSKRESM QRMTLPGTQL PRRPHSYLYS
HPHIHNTHPI PSPVISPPSH LRSDSLATGR PTVPLWISPT RLPSLYHASS VQGNQQADRN
QSAPVRYRKT RGGRTRAVSM NLDLELGRND DRMDRSKLPG NFHCSPEEIG TGPTGQDESA
SSPYRGSLT
//
