ID A0A096M3F2_POEFO Unreviewed; 1763 AA.
AC A0A096M3F2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Rho GTPase activating protein 21b {ECO:0000313|Ensembl:ENSPFOP00000025943.1};
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:ENSPFOP00000025943.1, 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:ENSPFOP00000025943.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; AYCK01007801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000025943; -.
DR Ensembl; ENSPFOT00000029236.1; ENSPFOP00000025943.1; ENSPFOG00000007122.2.
DR eggNOG; KOG4407; Eukaryota.
DR GeneTree; ENSGT00940000155406; -.
DR OMA; FCENDCP; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
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; 1.20.5.220; -; 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; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
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:SF24; RHO GTPASE-ACTIVATING PROTEIN 21 ISOFORM X1; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00683; SPECTRINPH.
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:UP000028760}.
FT DOMAIN 51..158
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 805..919
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1030..1223
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1763 AA; 194953 MW; 006AFB247BAFD105 CRC64;
ISATDRDTIN ASSSNSSHCG KDSAERQSLA DCPAVQYSTE EEPFAWPRPK TVRLRRTSLG
FGFTLRHFIV YPPESSLHCF PEEDCGRRGR QRNRLEPMDT IFVKQVKEGG PAHEAGLCTG
DRIVKVNGAS IIGKAYSEVI TLIQDSGDVL ELCVMPKDED VLQLAYSQDA YLRGYNSYSG
NASHIPDPPV VCYPRVDCKP TGMAQATDPS GQVCRGPAAS LDYGYRKEIT VPPSPPRQYS
KSQTAVCMRN DSVRTVVVPP NSAHMGRVVS AQRVDFMDPA YVRGRPGSLA QYPFPRKADI
YPSGPGMVPF ASQAPNYPSN HQNIDWRTYQ TYREYIDNKG IHSHGSRTIQ ERLDNFRIAG
QPSFAAASHI PRGDWVPKGI RRRSTSHERS YHGPPPHFQA APRSASQDRM RNSEKISNPR
NWPPRSVSQD ALVLKARSHS IDYVEPIELS RPSERRAGYP RADQGTRPSR QAMPRNAVPF
RPSAGYSSSM RGAPNPHFFS KGPDSLQTRS SPMLSDMLFG KSTEHSFTNQ RVSVPAHHLG
HTSQPGQNRM RSETIQISEA GRDATVVGIR SSSSSAAREI PQRPGILKTA HQDSQSQVNG
QSPSEPAVVM REKPHSGKNP SPLRHPSYIL AVNDEGADST ADVAACWLPN DTRREIHMRR
LEEQRHNSCS SNLDESLDAI PFIDEPVSPS VDREAAPIPP SAVISVAPSI ATAPSSQGSP
CPTIHRQLSH DQESMRSALL DSDSAGKTER SKSYDEGLDN YQEERRGSTS KHMASFRGLR
KTLDGHKPAG DSGSRRESSL DVFADSSKEG LLNFRQLSTD KNKRVGGGMR SWKQMYAILQ
GHTLTLYKDK KDALSHAASQ SDEDPLRISI KACLIDISYS ETRRKNVLRL TTSDCEYLFQ
AEGREDMLSW IRVIQENSNP DEENGSVTSQ DLISRKIKEY NMMRLTSAPS SRSEPSPKSS
RQSLSIKQAF LGGKTEGRSH SSHSPRTGED RRALKDESSP PRDRGAWKIG IAGIMKKPFE
KKQAGITFGV RLEDCPPAQT NRFVPLLVEV CCQVVEERGL EYTGIYRVPG NNAAISNMQE
ELNTKGMADI DIQEDKWRDI NVIGSLLKAF FRKLPEPLFT NEKYDKFIEA SRTEDSVERL
KELKRLVYEL PTHHLETLKF LCAHLKKVSD NCEQNKMEPR NLAIVFGPTL VRTSEDNMTD
MVNHMPDQCK IVENLVQQFD WFFMEDGSED PVAVVEQEST VQSQPVPNIG HLLTNISRVP
ASSSEVSDTA CPDSNKSKGL WISGNQCSKE MLRSSIFANR KRKKNKEKSQ LSSSDDDLDS
GFNKKELPEG GQQPLWSQVS QAEDSGQTDE DGEKDKHRNS SEETISHQMP PYASPSSSPN
LNYRMAVTHQ SSLSDPPSNY DDTVSDLGTM NSTSSQASVP RARRNKSAVL GADACPGGLG
AEVCSITSDY STTSSMTFLT GAETCTLSPE VQSVSESRGG EDADDERSEL ISEGRPVETD
SESDLSVFTI GKAEKSELPE STRPLPSHRL IECDTLSRKK SSKQKTESET SLDDKDPSRL
SQAVGSAKGR SSGSLSSSSR SEQDKTEPAW KLKITDRLKV RLRMSVDDMF GVGSQRSRSP
EGRSKKKNIR RRHTMGGQRD FAELSVLGDW SQPVGSRSEL SAVDRLKPKC SSQDFSIGDW
IARERHRTSN PEVSLDLSEQ LGALCGSNSQ NSGAPSSSEL ARGPAEALNG EISQSKNLSL
SATAHPHKLT SSQVVHSRFY QYL
//
