ID A0A2U9CPI9_SCOMX Unreviewed; 796 AA.
AC A0A2U9CPI9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Rho GTPase-activating protein RICH2 {ECO:0000313|EMBL:AWP18103.1};
GN ORFNames=SMAX5B_020635 {ECO:0000313|EMBL:AWP18103.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP18103.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP18103.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP026260; AWP18103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CPI9; -.
DR STRING; 52904.ENSSMAP00000016055; -.
DR Proteomes; UP000246464; Chromosome 18.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 14..254
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 260..451
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 470..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..723
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 87576 MW; A0E12EF993F93E34 CRC64;
MKKQFNRMRQ LANQTVGRAE KTEVLSDDLL QVEKRLELVK QVSHSTHKKL TACLQGQQGV
DVDKKSVRSP SKKLPLTTLA QCLVEGAAVL GDESLLGKML KLCGETQDRL AQELVMFELT
VERDVVEPLY DLAEVEIPNI QKQRKHLAKL VLDMDSARTR FYQSTKSSGL SSNLQPAGAK
ADHLREEMEE AANRMEICRD QLSADMYSFV AKELDYASYF QTLIEVQAEY HRKSLELLQS
VLPQIKAHQE TWVEKPCYGK PLEEHLALSG RDIAFPIEAC VTMLLECGMQ EEGLFRIAPS
ASKLKKLKAS LDCGVLDVQE YSADPHAIAG ALKSYLRELP EPLMSFELYN DWIQASNIQD
QDKRLQALLS ACEKLPPANN NNFKYLIKFL SKLTEDQDLN KMTPGNIAIV LGPNLLWTHN
EGSNITEMMT TVSLQIVGII EPIIQHADWF FPGEIEFNVT GNYGSPVHTN HNANYSSMPS
PDIDPMDRRQ CDQSRRPLSV ATDNMMLEFY KKDGMGVRVM DTTWVSRRGS SSARKTSSTP
PSVHPPVPPT DALAPEQPGE FAISPSPTPP PTSSDRASTL KNKELSPVIG QKGLQGTMTS
SGQTQHSEHS PLTLRRAKKL APIPPKVPYC QSGAMSDQST GQPSPVSLSP TPPSTPSPYG
FSYPQGYATI GSPVQSQMAT TPCLSSPPSL AGTLTKARPT PKPPRQRPNL PPPQPPSTPG
SSPQPLENSP GLLDGLSPGE SMSTDSLCNL DIPVIDMELD SIFDLAHISP FRNSVALLGL
TKTRAESEEE TESTML
//