ID   RH21A_XENLA             Reviewed;        1926 AA.
AC   Q6DFG0;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Rho GTPase-activating protein 21-A;
DE   AltName: Full=Rho-type GTPase-activating protein 21-A;
GN   Name=arhgap21-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) 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; BC076778; AAH76778.1; -; mRNA.
DR   RefSeq; NP_001086541.1; NM_001093072.1.
DR   AlphaFoldDB; Q6DFG0; -.
DR   SMR; Q6DFG0; -.
DR   GeneID; 446376; -.
DR   KEGG; xla:446376; -.
DR   CTD; 446376; -.
DR   Xenbase; XB-GENE-17340893; arhgap21.S.
DR   OrthoDB; 142586at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 446376; Expressed in blastula and 19 other tissues.
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: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..1926
FT                   /note="Rho GTPase-activating protein 21-A"
FT                   /id="PRO_0000305247"
FT   DOMAIN          77..162
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          906..1019
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          1126..1318
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1330..1381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1396..1416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1512..1540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1573..1598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1626..1658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1827..1915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1067
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1357..1373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1512..1536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1641..1658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1861..1902
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1926 AA;  214713 MW;  FA7FCCF57681DD32 CRC64;
     MATRRAIVPE QQQEPSSPAS EISKNKDGQE QSEMVSPMEE EGFCWPGPKS VALRRTSDGF
     GFTLRHFIVY PPESAVHTSI KDEENGNRGV NTGRPRNKLE PMDTIFVKQV KEGGPAHEAG
     LCTGDRIIKV NGESVIGKTY SQVIALIQNS DSTLELSVMP KDEDILQLAY SQDAYLKGND
     SYSGNAHHIP EPPPLCYPRI KPAASVMAQP VEVPPSGTSL AKQQSSRPVR TATTQPDRSY
     RVEIQVPPSP TELVKSNTAV CVCNEAVRTV LVPSEKVVDL SSNRTNRAGP LHRTEEVRYG
     LADPSILKRT TSPTSSIPHV QMVPTARQFD NAGVIGKPPS YGGHAENMFS TRPTAQAEGS
     PSPTNHYSSP GPHQQIDWRN YKTYKEYIDN RRMQMYGCRT IQERLDSLKA ASQTTTDYNQ
     MLPNHFSGQS RRRSTSHDRV QQSVQMRQRS VSQERLEDPV LMKEWPRSAS QDTLSSAVAS
     RNHRSESWDY HARKGDFDQF IVETQSNGER KHNYKWSGFT EQDDRRGITE RPRQHSFHMS
     LRSPNFTMAP VPYTSFAHPL QKVHPDVKTI QPTRQNSYRS PHPRPAVSDR SGFAVSKSNS
     VKIPTPCASK SYSPSVRSDD GIVIDQKPVN YMHVSGPQNF QRKTQTESAS GFQLDSVKTS
     MSASSSPPAN TKPAKQVKHS TATSQNVDVK KTPSPEANAG DSDAVLTPVD QVVLREKPSP
     GQQTSPPIRQ QSYIFAVNEQ EGVSDTTCWL PNDARREVHI KRIEQRKASG SNSPGNSLAS
     IPFIDEPTSP SIDHEIGNIP ASAVISISEQ PLPTITTVPP SPTSPVPLMR RHFSHDHDSI
     RPSILEVNSK TERSKSCDEG LDDYKEEGKL GLKQGSSLKG VQARENVPSS EDSESRKDSS
     SDVFSDSNKE GFLYFRQVTT EKGKRVSGSI RPWKQMYVVL RGSALYLQKD KKEQTGHSSA
     QSDEEQLIGI NGCLIDISYS ETKRKHVFRL TTSDREFLFQ AEDRDDMLAW IKAIQENGNL
     NDEQTDQASR VLISKRIKEY NTMMSSASNK SEQSPKAPRQ TLSIRQPFRA TRPDGKLQSP
     HSPKQESERR LFSKDDISPP KDKGSWRRIM KNPFEKKPIT GGTFGVRLDD CPPAHNNKYV
     PLIVDVCCKL VEERGLEATG IYRVPGNNAA ISSMQEDLNK ANTDIDIQDD KWRDLNVISS
     LLKSFFRKLP DPLFTNEKYN DFIEANRTED PVERLKTLKR LILDLPDHHY ETLKYLSAHL
     KTVADNAELN KMEPRNLAIV FGPTLVRTSE DNMTHMVTHM PDQYKIVETL IQKHDWFFSD
     ESADEPITTV HEESTVESQP VPNIDHLLPN IGRTGLSPGD VSDSATSDSA KPKGSWGSGK
     DQYSRELLVS SLFAAASRKR KKPKDKPQPS SSEDELDNVF YQKELSQVEF QIPDKQNVDK
     DADLKAKANA LSFKDADNIK GTNIITEDKL ESDIMHSEST SPCLPKLLEP PKENHRLQVP
     SDDKTIPQIS FQMEESMSDS GTMLSNSSQA SAQRSKPKVV SPEFKGHDFL TADVSSITSD
     YSTTSSTIYM TGLDPNPISP EVQSVAESKG EEADDERSEL ISEGRPVETD SENDFHIFAS
     SLAFNRQHRS KEEDPPRNVQ ANAEGSPSCT EGSITPRLDT RRFSSHKLIE CDTLSRKKSV
     RLKTDSECSA ESKNEETLSD AHEVMKKSRS PINVDTTANN EPEEPAWRIK ITDRLKLRLK
     ASADDMFGIG SQKAHAAETR KKKNIRRRHT LGGQRDFAEI SVLNAWKINE PSSKEVELSA
     VDRLKPKCPS QDLSISDWLA RERLRTSTSE LSTVEPEEKH ISETTGQKES VSPSPPPSSS
     PSQVSTADIP TGSESPSLGT APQSDDQMNG DSFQSKNKNN FSPAVDAHPH KLSGTQVVRS
     RFYQYL