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Database: UniProt
Entry: A0A2Y9M880_DELLE
LinkDB: A0A2Y9M880_DELLE
Original site: A0A2Y9M880_DELLE 
ID   A0A2Y9M880_DELLE        Unreviewed;      1169 AA.
AC   A0A2Y9M880;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Rho GTPase-activating protein 20 isoform X2 {ECO:0000313|RefSeq:XP_022417271.1};
GN   Name=ARHGAP20 {ECO:0000313|RefSeq:XP_022417271.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022417271.1};
RN   [1] {ECO:0000313|RefSeq:XP_022417271.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022417271.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022417271.1; XM_022561563.1.
DR   AlphaFoldDB; A0A2Y9M880; -.
DR   Proteomes; UP000248483; 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; IPR001849; PH_domain.
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; SM00233; PH; 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   Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT   DOMAIN          173..262
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          344..530
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          912..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          959..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1028..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1120..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1045
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1130..1148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1169 AA;  130345 MW;  91668DD98FC2DE79 CRC64;
     MEAMSPQQET LGGQPARSSS LTGVSRIAGA PGTKKKMKTL AERRRSAPSL ILDKALQKRP
     STKTLLIDGR VELKRGLQRQ ERHLFLFNDL FIVAKIKYNN NFKIKNKIKL SDMWTASCVD
     EVGEGNTNAL KSFVLGWPTV NFVATFSSPE QKDRWLSLLQ RYINLEKEKD YPKSIPLKIF
     AKDIGNCAYS KTITVTNSDT ANEVINMSLP MLGITGSERE YQLWVNSGKE EAPYPLIGHE
     YPYGIKMSHL RDTTLLTQGS KDSPTPSNFQ EPFLMEQLPR EMQCQFILKP SRLAVAQQLS
     DSGQKTFKRR RSIINWAFWR GSSTHLDNLP MSPTSPVPGQ LFGVSLPNIC ENDNLPKAVL
     DMLFFLNQKG PLTKGIFRQS ANVKSCRELK EKLNSGAEVQ LDCESIFVIA SVLKDFLRNI
     PGSTFSSDLY DHWVCVMDQG NDEEKIHAVQ RLLDQLPRAN VILLRYLFGV LYNIEQHSSS
     NQMTAFNLAV CIAPSILWPP TSSSPELENE FTKKVSLLIQ FLIENCCRIF GEEITSLLGE
     VSVRCDTREN ASDISCFQLN DSSYDSLENE LNEDVDAPCS DLVKKLGQGS RSMDSVLTLS
     DYDLDQPEVE GLLTLSDFDL DHSKDEDIQM EQPLESKPVN IAVYTKEPLQ DHARAPSGMS
     TPSHLSTTAA DAPKSLRRHR RCSEPSYDYL DSKLSYLREF YQKKLRKSSC DAVLSKKDES
     HLNQNQPLQE EGKTCFKKSL VIGTDIKKNA TNKNVKKKSL SDNEGNHVKL FPKSKPVAIS
     MASYSHMSSC DHPRNQTFDT DRSGYSPPHT TDTLKSSRRH RRCSEPNIDD QHCKLTYLRG
     IHSKKQHKAS YEASLLHGEE DYLKRHKSLQ MEGQKLINQS LVMGIEVGKT SATNQNTDKV
     LPPRLNICSR TSYSSLSSPG TSPSGSSVSS QDSAFSQISE HSVFTPTETS SPIDCTFQAQ
     RKQEELSSDF SSSSLISGIP GPSSGQASGH LAYTKKDSVE WHSQMHSVTL HPSTWLRNGV
     ASLKNWSLKK KARAPRPEEN KIGSLKGHTE PPPHASGVPE ANALHERQKD MPRRAAEGLG
     AVQTARWYSS YPSQDSEKHC SSPVSLVEDR LGLCMKSPEE GEISGQCSPG TLPHGRSSPS
     SLTVDHVCSP DSGPTVVCDV EDRHLTKDI
//
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