ID W5N6H5_LEPOC Unreviewed; 927 AA.
AC W5N6H5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Rho GTPase activating protein 44 {ECO:0000313|Ensembl:ENSLOCP00000016234.1};
GN Name=ARHGAP44 {ECO:0000313|Ensembl:ENSLOCP00000016234.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016234.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016234.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHAT01000412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01000413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01000414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01000415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N6H5; -.
DR STRING; 7918.ENSLOCP00000016234; -.
DR Ensembl; ENSLOCT00000016264.1; ENSLOCP00000016234.1; ENSLOCG00000013174.1.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000157296; -.
DR InParanoid; W5N6H5; -.
DR OMA; SDWIQAS; -.
DR Proteomes; UP000018468; Linkage group LG10.
DR Bgee; ENSLOCG00000013174; Expressed in camera-type eye and 9 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0031256; C:leading edge membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0098886; P:modification of dendritic spine; IBA:GO_Central.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07619; BAR_Rich2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR047165; RHG17/44/SH3BP1-like.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1.
DR PANTHER; PTHR14130:SF13; RHO GTPASE-ACTIVATING PROTEIN 44; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 7..247
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 253..443
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 462..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..629
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..898
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 100790 MW; 02F0D0018025208A CRC64;
MRQLANQTVG RAEKTEVLSE DLLQVEKRLE LVKQVSHSTH KKLTACLQGQ QGVDVDKRSV
RSPSKKLPLT TLAQCLVEGA TVLGDDSLLG KMLKLCGETE DRLAQELILF EFQIERDVIE
PLFVLAEVEI PNIQKQRKHL AKLVLDMDSA RTRWQQSSKS SGLSSNLQPT GAKADALREE
MEEAANKVEI CRDQLSADMY SFVAKEIDYA NYFQTLIEVQ ADYHRKSLAL LQSVLPQIKA
HQEAWVEKPS YGKSLEEHLA ISSREIAFPI EACVTMLLEC GMQEEGLFRV APSASKLKKL
KASLDCGVLD VQEYSADPHA IAGALKSYLR ELPEPLMTFE LYDEWIQASN IQDQDKRLQA
LLSACEKLPK ANSNNFRYLI KFLAKLTEYQ DANKMTPGNI AIVLGPNLLW AQTEGNITEM
MTTVSLQIVG IIEPIIQHAD WFFPGEIEFN VTGNYGSPVH TNHNANYSSM PSPDMDHSDR
KQHDQARRPL SVATDNMMLE FYKKDGMGVR VMDTSWVSRR GSSLVRKTSS TPPSVQPPAP
PAELPSLAQS LVPEQPYELS AAPCGGPPAG GAGDRASTDD VSPNWSDSCY AYPSPEDDRP
PPPYPTCCPP PHHHYPRAQP SPRPAAPSPD SVTPASFSSS SSCSPHKWTG YSPLPPPPPS
ASPQQLDINS NPKPSFLHLP KQSSLADALH ANPETNMSPL YIKTPLVLTK HDPALSLPPN
LPSSAFPQWG SCACSRDRGT RLTRFLDLKT AVPFLKNKSV SSPGKLSGRK YLRDASGPGL
TLLLPLSLSL PAVSKKLAPI PPKVPYGQSG GMSDQSTGQP SPVSLSPTPP STPSPYGLGY
SQGYPGLSSS GQVSPAAAPS LSSPPSLSGT LTKSRPTPKP RQRPSLPPPQ PPVTPGLSGS
SPQPLDHSLL DSMSPGESMS TGDFYSI
//
