RHG21_XENTR
ID RHG21_XENTR Reviewed; 1935 AA.
AC A2RUV4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Rho GTPase-activating protein 21;
DE AltName: Full=Rho-type GTPase-activating protein 21;
GN Name=arhgap21;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase-activating protein (GAP) for rhoa and cdc42.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell junction {ECO:0000250}.
CC Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
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DR EMBL; BC133058; AAI33059.1; -; mRNA.
DR RefSeq; NP_001090761.1; NM_001097292.1.
DR AlphaFoldDB; A2RUV4; -.
DR SMR; A2RUV4; -.
DR STRING; 8364.ENSXETP00000032292; -.
DR PaxDb; A2RUV4; -.
DR PRIDE; A2RUV4; -.
DR DNASU; 100037846; -.
DR GeneID; 100037846; -.
DR KEGG; xtr:100037846; -.
DR CTD; 57584; -.
DR Xenbase; XB-GENE-1011028; arhgap21.
DR eggNOG; KOG4407; Eukaryota.
DR InParanoid; A2RUV4; -.
DR OrthoDB; 142586at2759; -.
DR Reactome; R-XTR-9013026; RHOB GTPase cycle.
DR Reactome; R-XTR-9013106; RHOC GTPase cycle.
DR Reactome; R-XTR-9013148; CDC42 GTPase cycle.
DR Reactome; R-XTR-9013149; RAC1 GTPase cycle.
DR Reactome; R-XTR-9013404; RAC2 GTPase cycle.
DR Reactome; R-XTR-9013406; RHOQ GTPase cycle.
DR Reactome; R-XTR-9013409; RHOJ GTPase cycle.
DR Reactome; R-XTR-9013423; RAC3 GTPase cycle.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
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:0051645; P:Golgi localization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Golgi apparatus; GTPase activation; Membrane; Reference proteome.
FT CHAIN 1..1935
FT /note="Rho GTPase-activating protein 21"
FT /id="PRO_0000305249"
FT DOMAIN 78..163
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 920..1033
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1140..1332
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1637..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1838..1925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1870..1911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1935 AA; 215607 MW; 7F7B9B700A8CC0F4 CRC64;
MATRRATVPE QQQQQPSSPG SEISKNKDGQ EQSEMVSPTE EEGFCWPGPK SVALRRASEG
FGFTLRHFIV YPPESAVHTT VKDEENGNRG VNAGRPRNRL EPMDTIFVKQ VKEGGPAHEA
GLCTGDRIIK VNGESVIGKT YSQVIALIQN SDSTLELSVM PKDEDILQLA YSQDAYLKGN
DSYSGNAQNI PEPPPICYPR TKPAASVMAQ PVEVPPSGTS LTKQQSSRPV RTATTQPDRS
YRVEIQVPPS PTDIVKSNTA VCVCNEAVRT VILPSEKVVD LSSNRTNRAG PLHRTEEVRY
GLADPSMLKR TTSPPSSTPS VPMVPASRQF DNAGVIGKPP SYGGHSESMF STRPSQAEES
PSPTNHYASP GSHQQIDWRN YKTYKEYIDN RRMQMYGCRT IQERLDSLRA ASQNTTDYDQ
MLPNRSSGQV RRRSTSHDRV PQSVQMRQRS VSQERLEDPV LMKEWPRSAS QDTLTSLTVA
PRNHRSESWD YLTRKEDFDQ FIVDTQSNGE QKHNYKWTGF TEQDDQRGIY EIPRQHSFHM
SLRSPNYTMA PLPYPSDSRR AGTRVLAPAR PLQKVHPDLK TIQPTRNFQN SYRSPHPRPA
VSERLVFPIS KSNSVKIPAT YASKPYSPSV GSEDGIVKDQ KAVNYIHVSG PQNFQRKPQT
ESALGFQLDS LKTSTSASSS SPAHTKPAKQ AKHSTATSQN VDGKKTQSPE ANAGDSNSVL
TSIDQVVLRE KPSPGQQTSQ PIRQPSYIFA VSDVEGASDT TCWLPNDARR EVHIKRIEQK
KASGSDSPGD SLASIPFIDE PTSPSIDHEI ANIPASAVIS ISVQPLPTIT TVPPSPTSPV
PLIRRHFSHD HDSIRPSILE VNSKTERSKS CDEGLDDYKD EGKLSLKQGS SLKGIKAREN
VPSSEDSESR KDSSSDVFSD SNKEGFLYFR QLTTEKGKRV SGSMRPWKQM YVVLRGSALY
LQKDKKEQSG HSSAQSDEEQ LIGINGCLID ISYSETKRKN VFRLTTSDRE FLFQAEDRDD
MLAWIKAIQE NGNLNDEQTD QASRVLISKR IKEYNTMMSS SSNKSEQSPK PSRQTLSIRQ
PFRATKPEGK LQSPHSPKQE SERRLFSKDD ISPPKDKGSW RRIMKKPFEK KPTTGGTFGV
RLDDCPPAHN NKYVPLIVDV CCKLVEDRGL ETTGIYRVPG NNAAISSMQE ELNKGSTDID
IQDDKWRDLN VISSLLKSFF RKLPDPLFTN EKYNDFIEAN RTEDPVERLK TLKRLILDLP
DHHYETLKYL SAHLKAVAEN SEKNKMEPRN LAIVFGPTLV RTSEDNMTHM VTHMPDQYKI
VETLIQQHDW FFSEESADEP ITAVQEESTV ESQPVPNIDH LLPNIGRTGL SPGDVSDSAS
DSAKSKGSWG SGKDQYSREL LVSSLFAAAS RKRKKQRDKP QPSSSEDELD NVFYQKELLQ
VEFQRPDKQN VDKDVDLKAN ALSLKDADNI KGTNIIKEDK LEKDIMHSEA TSPCPPKLSE
PPIVNHRLPP DDKNIPQISF QMEESMSDSG TMLSTSSQAS AQRSKPKVVS PELKGSDFLT
ADVSSITSDY STTSSTIYIV GLDQNLISPE VQSVAESKGE EADDERSELI SEGRPMETDS
ENDFPIFASS IAFDRQHRSK VEEPTRNVQV NSEGSPSCTE GSITPRMDRR RFSSHKLIEC
DTLSRKKSIR QKTDSECSAE SKNEETLSDA QEAVKKGRSL SIGDTTTNNE PEEPAWRIKI
TERLKLRLKA SADDMFGIGS QKAQAAETRK KKNIRRRHTL GGQRDFAEIS VLNAWKINEP
SSKEAELSAV DRLKPKCPSQ DLSISDWLAR ERLRTSTSEL SMVEPEEKRI SDATSQKEPA
SPSPPPASSP SQVSTAIVTA GSESPSQGTA PPPDDQMNGD SFQSKNKNNF SPAVDAHPHK
LSGTQVVRSR FYQYL