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Database: UniProt
Entry: A0A2K5F7X5_AOTNA
LinkDB: A0A2K5F7X5_AOTNA
Original site: A0A2K5F7X5_AOTNA 
ID   A0A2K5F7X5_AOTNA        Unreviewed;      1233 AA.
AC   A0A2K5F7X5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Rho GTPase activating protein 20 {ECO:0000313|Ensembl:ENSANAP00000041499.1};
GN   Name=ARHGAP20 {ECO:0000313|Ensembl:ENSANAP00000041499.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000041499.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000041499.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K5F7X5; -.
DR   STRING; 37293.ENSANAP00000041499; -.
DR   Ensembl; ENSANAT00000059614.1; ENSANAP00000041499.1; ENSANAG00000038027.1.
DR   GeneTree; ENSGT00940000154633; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd13319; PH_RARhoGAP; 1.
DR   CDD; cd17115; RA_RHG20; 1.
DR   CDD; cd04402; RhoGAP_ARHGAP20; 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; IPR047886; ARHGAP20-like_RhoGAP.
DR   InterPro; IPR047887; ARHGAP20_PH.
DR   InterPro; IPR047888; ARHGAP20_RA.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23179:SF28; RHO GTPASE-ACTIVATING PROTEIN 20; 1.
DR   PANTHER; PTHR23179; T-CELL ACTIVATION RHO GTPASE ACTIVATING PROTEIN-RELATED; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020}.
FT   DOMAIN          194..295
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          365..551
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          924..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..824
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..1010
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1066
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1233 AA;  137486 MW;  260D054A4CB75D73 CRC64;
     MEAMSPQQET LGGQPGRSSS LTGVSRLAGG SGTKKKMKTL AERRRSAPSL ILDKALQKRP
     TTRESPSASV DTCTFLSSFV CSNRTLLIDG RAELKRGLQR QERHLFLFND LFVVAKIKYN
     NNFKIKNKIK LTDMWTASCV DEVGEGNTNA MKSFVLGWPI VNFVATFSSP EQKDKWLSLL
     QRYINLEKEK DYPKSIPLKI FAKDIGNCAY SKTITVMNSD TANEVINMAL PMLGITGSER
     DYQLWVNSGK EEAPYPLIGH EYPYGIKMSH LRDTALLTPG SKDSTTPFNL QEPFLMEQLP
     REMQCQFILK PSRLAAAQQL SDSGHKTFKR RRSIINWAFW RGSSTHLDNL PTSPTSPMPG
     ELFGISLPNI CENDNLPKPV LDMLFFLNQK GPLTKGIFRQ SANVKSCREL KEKLNSGVEV
     HLDCESIFVI ASVLKDFLRN IPGSIFSSDL YDHWVSVMDQ GNDEEKINAV QRLLDQLPRA
     NVVLLRYLFG VLHNIEQHSS SNQMTAFNLA VCVAPSILWP PTSSSPELEN EFTKKVSLLI
     QFLIENCCRI FGEEITSLFG EVSVRCDTRE NASDISCFQL NDSSYDSLEN ELNEDVDAPC
     SDLVKKLNQG SRSMDSVLTL SDYDLDQPEV EGLLTLSDFD LAHSRDEDVQ MKQPLEAKPV
     DILVYTKIPL RDHARAPSTC IPSYLSTAAA NAAKSLRRHR RCSEPSIDYL DSKLSYLREF
     YQKKLRKSSC DAILSQKDED YLKQNEPLQE EGKTCFKQSL VTGTDASKKN ATTQNTKKKS
     LSGSEGNHVK LFPKSKPVAI SVASYSPVSS QDHSKNQPFD VDTSGYSPPH TADALKGPRT
     HRRCSEPNIE DQNRKLTYLR GIYSKKQHKT SCEAGVLHGE EDYLKRHKSL QMEGQKLINQ
     SLVMGIEVGK SSTTNQNTEK VLPPRLNLCP RTSYSSLSSP GTSPSGSSVS SQDSAFSQIS
     EHSVFTPTET SSPIDCTFQA QKKQEELSPD FSSSSHVSGM PSPSSGQACS RMAYTKKDTM
     EWHSQMHSVT LHPSTWLRNG VASLKNWSLK KKAKAARPEE KKISSPKGPL EPPSRASGVL
     EANSLQEKQN DLPLRAAEGL APMQSAQMCS SSPCQDSERH CSSPFSLVES RLKLCMKSHE
     EVEPGSQSSS GSLPWERASA SSWTLEDVTS PDSGPTVVYD IEDSVEVFWK GFRKQSCEEK
     EENGCSFQYP FQRCLWLGTC FRNATSPIFK VTS
//
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