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Database: UniProt
Entry: A0A3B1KC13_ASTMX
LinkDB: A0A3B1KC13_ASTMX
Original site: A0A3B1KC13_ASTMX 
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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