ID A0A087Y0V2_POEFO Unreviewed; 1652 AA.
AC A0A087Y0V2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 2 {ECO:0000313|Ensembl:ENSPFOP00000011655.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000011655.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000011655.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; AYCK01004378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01004379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01004380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01004381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01004382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007551389.1; XM_007551327.2.
DR RefSeq; XP_007551390.1; XM_007551328.2.
DR RefSeq; XP_007551391.1; XM_007551329.2.
DR RefSeq; XP_007551392.1; XM_007551330.2.
DR RefSeq; XP_016526583.1; XM_016671097.1.
DR STRING; 48698.ENSPFOP00000011655; -.
DR Ensembl; ENSPFOT00000011672.2; ENSPFOP00000011655.2; ENSPFOG00000011485.2.
DR GeneID; 103137544; -.
DR KEGG; pfor:103137544; -.
DR CTD; 116984; -.
DR eggNOG; KOG1117; Eukaryota.
DR GeneTree; ENSGT00940000167169; -.
DR OMA; FAHSCET; -.
DR OrthoDB; 4835at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 5.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR45899:SF1; ARF-GAP WITH RHO-GAP DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR45899; RHO GTPASE ACTIVATING PROTEIN AT 15B, ISOFORM C; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 3.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 5.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 5.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 4.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 6..65
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 440..532
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 550..639
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 636..769
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT DOMAIN 850..960
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1078..1254
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1286..1380
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1392..1495
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 69..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1120..1152
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 71..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1652 AA; 185988 MW; F82AE4EFD25ED5EF CRC64;
MLEPRESRYN IEEWLMTLRL SQYISFFQKA GYRVVEDCRG LTDERLLELQ VLPTGHRKRI
LWSLEAQGLK QEGGERGESE QDTRESDGNQ KKPPLLPRHV FRNYRSTGVS CQHNQPKENR
DYNVEGSQTL PAGAGLTPDP ENQPGRRHII PPVPAPRNPQ LTQTSVSSRP CFPTSMLSSS
SNESLPTSET PSDFEASSEE QCQWNYDSVP SATDALRLVL AEDQEDFYGE MVENSIYEAQ
PAGPRLTRSY RLRHRPVPEI PSEPAAALLD RSAQTTSPEH LTGSERPTGA NGIQKAPLQR
TLTPIAPYGE IFLYNKPGSA PEKGAKDGLQ GFKARMKPKK KRKKAKEKGS PPSPPVPDAD
GYSTVKMCAS MLPRASLDTA FSTTPDTAPA GLASPVPEDE SMIMVECDLY TESANCRGIV
TDSAEPDISP YACFYGAPKQ AVKVGWLDKL SPQGNCVFQR RWVRFDGESL GYYNNDKEMY
SKGLILVSAI RQVKGLGENK FEVITGLRTF TFRAEKEGER QEWMETLQTA VRPPACSSQK
CTDSLPHLSS TNKRGLLELR GYKGRLLVSL VGSKVRLCKT EQDFRAGLGI CEVELSAANI
KEVDRRGFEI NTPFKNFCFV ADSEREKEEW FEAIKESIAE TLYDYEVAEK IWFNEANRSC
ADCGESQPEW ASVNLGVVIC KKCAGQHRSL GPSLSKVRSL KLDSSIWSNE LVELFLEVGN
QNANSFWAAN LPLEEELHSR ASTEQRATFM RRKYRERKYR KVLEDFTNLD ELNKALCAAV
VSSDVLQTME LVFSGADVMC ATGDPVYSTP YLLAQRAGQK LQMEFLHQNK LSDFPRLDQW
SENASLSDVS VFMDGFLYVS SGPAKTMPDR RGRDDMGRRW CTLEGGFLSY YENERSPSAI
GRVDVSEVVS LAVSNSETMT GVGAVFTVEL YLRTERALTV GAETQDTQHD WIQALAKCFV
PPKVEGLVRK RSELIGRLQY KEGHDLYHWR TGWFMLEGSA LHFSSGDEAG EEEVLHLKQL
QELTVSTHVE GEDKIQVLLM VESGRTIYIH GFNRMDFSLW HSAITLAAGT DGRALGDQQL
TKNGVPIIVD SCIAFVTQYG LCQEGIYQSP GDPARVSLLL EEFTRDARNV KLRNKEHQLE
DVTDTLKRFL SQLEDALLTK ELYPYWVSAL DETDEKQRVK KYSTFIESLP KIYKSTLHAL
LQHLYRIQQC SHLNGMPSEK LAAVFSSCLF QTQGQTPQEM SVIRDLISNY VTLFSVNEDQ
VQQMETENSF ITRWNEKKDT AFCPAGDLIF EVYLEKREPE QCCLIKLSPS MRSCELAETA
LSMRSDTFKA DDLWTTFEVI ENGELERPLH HSEKILEQVL EWSALDCPSS AFLVIKKFAG
AKRMAGGKDP RQFLKSDYLK FSDGSSKLLS GHKFQDKYVV LRSEKLLLYR DIKNTKAEKE
IQLKMVKCYL GLKKKLKPPC NWGFTVYTDK HQWHFCCDRR ETQISWVADI IALKHGSDLQ
MNTSGFKETA DLKTSRGGAI TETSKVPSYN HTFTTQLTDR RVSLGDADLR TPRVSGLHLK
TNTIPKCLKP DYLSQTPEVP QRRTSVDICQ PQRLPPPAVP RHTKPMPLPV LPQTGNKAPC
KKPIPGVGGA MPPNLLNELN LVLSKNARKT TE
//
