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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
 
 
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