ID A0A087XNV4_POEFO Unreviewed; 1689 AA.
AC A0A087XNV4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Rho GTPase activating protein 21b {ECO:0000313|Ensembl:ENSPFOP00000007457.2};
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:ENSPFOP00000007457.2, 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:ENSPFOP00000007457.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; AYCK01007801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000007469.2; ENSPFOP00000007457.2; ENSPFOG00000007122.2.
DR GeneTree; ENSGT00940000155406; -.
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 32..143
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 791..905
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1013..1206
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1356
FT /note="Basic and acidic 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 1689 AA; 187528 MW; B7DE1FE8BF9A6C74 CRC64;
PTSFFSVQKD SAERQMQYST EEEPFAWPRP KTVRLRRTSL GFGFTLRHFI VYPPESSLHC
FPEEDCGRRV CNAWRQRNRL EPMDTIFVKQ VKEGGPAHEA GLCTGDRIVK VNGASIIGKA
YSEVITLIQD SGDVLELCVM PKDEDVLQLA YSQDAYLRGY NSYSGNASHI PDPPVVCYPR
VDCKPTGMAQ ATDPSGQVCR GPAASLDYGY RKEITVPPSP PRQYSKSQTA VCMRNDSVRT
VVVPPNSAHM GRVVSAQRVD FMDPAYVRGR PGSLAQYPFP RKADIYPSGP GMVPFASQAP
NYPSNHQNID WRTYQTYREY IDNKGIHSHG SRTIQERLDN FRIAGQPSFA AASHIPRGDW
VPKGIRRRST SHERSYHGPP PHFQAAPRSA SQDRMRNSEK ISNPRNWPPR SVSQDALVLK
ARSHSIDYVE PIELSRPSER RAGYPRADQG TRPSRQAMPR NAVPFRPSAG YSSSMRGAPN
PHFFSKGPDS LQTRSSPMLS DMLFGKSTEH SFTNQRVSVP AHHLGHTSQP GQNRMRSETI
QISEAGRDAT VVGIRSSSSS AAREIPQRPG ILKTAHQDSQ SQVNGQSPSE PAVVMREKPH
SGKNPSPLRH PSYILAVNDE GADSTADVAA CWLPNDTRRE IHMRRLEEQR HNSCSSNLDE
SLDAIPFIDE PVSPSVDREA APIPPSAVIS VAPSIATAPS SQGSPCPTIH RQLSHDQESM
RSALLDSDSA GKTERSKSYD EGLDNYQEHC EKRSTSKHMA SFRGLRKTLD GHKPAGDSGS
RRESSLDVFA DSSKEGLLNF RQLSTDKNKR VGGGMRSWKQ MYAILQGHTL TLYKDKKDAL
SHAASQSDED PLRISIKACL IDISYSETRR KNVLRLTTSD CEYLFQAEGR EDMLSWIRVI
QENSNPDEEN GSVTSQDLIS RKIKEYNMMS APSSRSEPSP KSSRQSLSIK QAFLGGKTEG
RSHSSHSPRT GEDRRALKDE SSPPRDRGAW KIGIAGIMKK PFEKKQAGIT FGVRLEDCPP
AQTNRFVPLL VEVCCQVVEE RGLEYTGIYR VPGNNAAISN MQEELNTKGM ADIDIQEDKW
RDINVIGSLL KAFFRKLPEP LFTNEKYDKF IEASRTEDSV ERLKELKRLV YELPTHHLET
LKFLCAHLKK VSDNCEQNKM EPRNLAIVFG PTLVRTSEDN MTDMVNHMPD QCKIVENLVQ
QFDWFFMEDG SEDPVAVVEQ ESTVQSQPVP NIGHLLTNIS RVPASSSEVS DTACPDSNKS
KGLWISGNQC SKEMLRSSIF ANRKRKKNKE KSQLSSSDDD LDSGFNKKEL PEGGQQPLWS
QVSQAEDSGQ TDEDGEKDKH RNSSEETIRK DSESVASLPG EHIPSGHQMP 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
IARERHRTS
//
