ID A0A3B1KC13_ASTMX Unreviewed; 1802 AA.
AC A0A3B1KC13;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Rho GTPase-activating protein 23-like {ECO:0000313|Ensembl:ENSAMXP00000052247.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000052247.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000052247.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSAMXT00000053222.1; ENSAMXP00000052247.1; ENSAMXG00000042175.1.
DR GeneTree; ENSGT00940000157982; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000042175; Expressed in zone of skin and 13 other cell types or tissues.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
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:UP000018467}.
FT DOMAIN 80..162
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 862..979
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1069..1260
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 16..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1709..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..624
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1407
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1802 AA; 198367 MW; 4B90BC124530E143 CRC64;
MNGVAFCLVG IPPRAETEAK GRRDGTSSSS ENPRPVVVGG SDGRGMSWQG PRTLLLQKNS
QGFGFTLRHF IVYPPESALH TSLKDEENGN EKGLQRSRLE PMDTIFVKNV RERGPAHQAG
LCTGDRLVKV NGESVLGKTY SQVIALIQNS ESVLELSIMP KDEDVLQLAY SQDAYLRGNE
PYKGGAQCLP PPPPLCYPPR SKSQPPTSHT SCPTSSRVQM GQNQLDNWSR WPGSTSSGPS
PPLDNRITVP AHATVWAAEG RACDPGGVGH SSPPHRTEEI RYGMTDRGQQ AMGQMRGRTY
SSSSSSGGAL ASPLHHGPYG NYGVGTAQGW ASPPQPTHTP PSSHNERTQQ ALSNWYYSQV
NERERERPSV RSLHPRHRSF SQDRLGEFNR TRRTQRSDFP HSVSQDTLLY LQQPGPGARG
HWQGENIPIS AFNCTRSENL LQTRYGHSGR SLEALDRAPS MLSPCQERPS WGGHQPQSRA
EAYQRQSTQY SLAQTPPGAR HTQAPQHEQK RTKPLVSQHP SQHQNLPYSP QHSTQAPQPQ
QAMPQTRRLP SCQSLDEQPM SMGYRSYSPS FNRKTGRILQ HAHSFRDPSY MGPALSWTPT
PKTSPPEGVA PPSTPSPAPP TSSATPTAPE GQDRTHRPTN HEREGGEIKE VQAQVQEVVL
RQKPPMGRRG GNTNRHPHYG MAIEDDDPLL FTSDPTEAPP KAESTISQRR SNGNLAPLSV
EDDSLASIPF IDEPTSPGVD LRACHVPASS VVSSGLKSAP AVAASPASPT FTFPLSRLFS
HDCSSIKSSR RSSYLLAITT ERSKSCDEGL NTFRDDSRIF TRLPKRVKSF FGDGSLESLK
AAEDARSKRH STSELGSFNY SDVRREGWLH YKQIHTEKGK KVGSAMRPWR RVFSVLRSNS
LYLYKDKREA LLKGSSLGGG SEDEQPISIR GCLVDIAYSE TKRKNALRLT TQDFCEYLLQ
AEDRDDMLDW IKVIGESSKT DSEELGFSRQ ALINKKLNDY RKQSPTGNKP DSSPRVPRMN
FLLTKPDNSS APPRSPKHEG KEESSPPKSP WGINFMKKVK KAGPKAFGVR LEDCQPGASN
KFIPLIVEIC CGLVEEMGLE YTGIYRVPGN NAVVSSLQEQ LDKGSDINTA EERWQDLNVV
SSLLKSFFRK LPEPLFTDDK YNDFIEANRM ENASDRLKTL KKLIHDLPDH YFHTLKFLVG
HLKTVADHSE KNKMEPRNLA LVFGPTLVRT SEDNMTDMVT HMPDRYKIVE TLIQHYTWFF
SEEHDKDEKT PVDTEDVQPA PNIDHLLSNI GRTGLLGDAS DSTNSDSAKS KGSGGSKRDL
SAKDFLTTLS IMSAVARRRR KRPTANLLGS STDDDSEQEP IRAGLTAEAE EKEAELIQPD
TAPCAEAEEV EDEEEDDEEE EEEGDTECVQ KEQPSPSMPC REESQSVLLS EEEDQRTDAK
RPGGWRGEDA RSIVSGYSTL STLGRSLASE GRGEDADDEQ SELVSETDNE SGFASRSLTQ
ERPEKHTSTP TSPQRAHTTH TSPGPTAPRS FLYSNYKSPT LSPAPEPTSA PTNSKSLTPE
PTERVSEGTA RSSTPSTSSY SSSASQRLHS RPSFNSHRLI QCDTLARRRL KSDKAKARSL
DLLELSSTST TENEGQASIG QTKTQIPNFS LSPSPSSRTK LNPGSDPESS PAPTLPSEGR
FFAPSGATLA EQVRARLLGS AEDLRAASLR KPISPETRRK RRAWRRHTVV ASPTDASTKS
LPLTSVVAAA TGNNNNNKPP VPPPKPPGIV GRPGAQIVPP SPEADAQSAR RAPPTSRFHE
CL
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