ID A0A3P9C0R8_9CICH Unreviewed; 1168 AA.
AC A0A3P9C0R8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=RAS protein activator like-3 {ECO:0000313|Ensembl:ENSMZEP00005015687.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005015687.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005015687.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005015687.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_004538844.1; XM_004538787.2.
DR AlphaFoldDB; A0A3P9C0R8; -.
DR STRING; 106582.ENSMZEP00005015687; -.
DR Ensembl; ENSMZET00005016194.1; ENSMZEP00005015687.1; ENSMZEG00005011764.1.
DR GeneID; 101475179; -.
DR KEGG; mze:101475179; -.
DR CTD; 64926; -.
DR GeneTree; ENSGT00940000165433; -.
DR OrthoDB; 22721at2759; -.
DR Proteomes; UP000265160; LG6.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR CDD; cd04013; C2_SynGAP_like; 1.
DR CDD; cd13262; PH_RasSynGAP-like; 1.
DR CDD; cd05136; RasGAP_DAB2IP; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR PANTHER; PTHR10194:SF96; RAS PROTEIN ACTIVATOR LIKE-3; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160}.
FT DOMAIN 367..401
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 610..802
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1039..1098
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 129585 MW; 1BB0D76AC44A5E9E CRC64;
MGTEEKDPEP AAQPASKEQG SPEKENEPPQ TSETSDPLNT YKWHTGSKGT LNEQKEEGEG
TPASSTSTME KIQKASSNKW SKMQNWRKAL SEDPGEKNSS NGKSSDAAKP EKASGGTRKN
PFRRALSEPP GSLFAALSTA NSAHAGSSSA AATSAGTEAS GAASSDPSQK GGGGALFKKY
LRSVSQKLKK PKLQPRNSTP SLAGLNEVVP TPAGPCELSR LQWVPPQEVP LWDISNCCLE
DGQILISPEE EPTMWTRNRV SSCLSNLSMQ NLVDIDTECS PDHGGQLGPR PKAQDGGVRG
LIKRRLENKA KRNSNTQLNQ QGLNKGRRLY ESRESVSIPV SPVGTLDLSA DTSTVIRPVH
SSILGEKYCF EVINSENTHC FGCSSAAERD RWIEDLRRAA QPNKDNIERT ENSLSLWVNE
AKDLPPKKRY YCEVHLDGTL FARTTSRAVG KLPNRSSLAA DGSAGSSGGL GASGGATGGC
QLFWGEFFEL DNLPCISQIS LHLFREEDPK KKRHSRDDSS LHPLGSVTIP LADIRGRTYQ
EKWYPITPYK ASGSAGNKEA LGPQASLRIK ARFQNLQVLP MEKYKEFAEY VTVDYVEMCR
NLEPLLNVKE KEELAGALVH VLQSIGKAKE FLIDLGNDEV ERLGEKEAMI FRENTLATKA
IDEYMKLVGQ KYLIDTLGEF INRLYASTEN CEVDPRKCPA AELSSNQKHL RETCEEVVQK
IIELHGPFPE ELNRIFSSWV EVCEDQGKPE IGHRLISASL FLRFLCPAIL SPSLFGLTQP
YPEPNTLRTL TLTAKVIQNL ANFTLFGEKE EYMLFMNEFL EQHWDGMRGF LQTVSSGDTE
IAMTSFDGYV DLPLRLAVLH GLLVDIIYQK DQQTVDKLHP LPSILNQITE SLGPEAPRID
INSQTGHIKP AYIPPKDLSK YSPLQSSLQH IPQESKSTRD NRSQRRKPIA RTQSAPHRRP
AQVKREMKRQ TSSEALPTSD QEQEAEPNQP LISPPNTSVS VKRAPAPVPW IKPGDPNPPG
SHTRQPSEIK TENEQFSLLD KHAQELSELR LGIEQVTERE LDMAKRLEDF IIQSQDQNAI
LQEEVNELRN VLAMREEQLA SATFRLGVIE EEREEDERKL SVAIAAAERV NVLEEQFAGL
LSDLQQLSEA YKSSQNNTQH PEKPLNTT
//
