ID   RH21B_XENLA             Reviewed;        1902 AA.
AC   Q71M21;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Rho GTPase-activating protein 21-B;
DE   AltName: Full=Rho-type GTPase-activating protein 21-B;
DE   AltName: Full=XrGAP;
GN   Name=arhgap21-b; Synonyms=xrgap;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=12711552; DOI=10.1016/s1567-133x(02)00073-x;
RA   Kim J., Shim S., Choi S.-C., Han J.-K.;
RT   "A putative Xenopus Rho-GTPase activating protein (XrGAP) gene is expressed
RT   in the notochord and brain during the early embryogenesis.";
RL   Gene Expr. Patterns 3:219-223(2003).
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}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the differentiating tissues during
CC       early embryogenesis. {ECO:0000269|PubMed:12711552}.
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DR   EMBL; AF462392; AAQ04821.1; -; mRNA.
DR   RefSeq; NP_001083524.1; NM_001090055.1.
DR   AlphaFoldDB; Q71M21; -.
DR   SMR; Q71M21; -.
DR   GeneID; 398972; -.
DR   KEGG; xla:398972; -.
DR   CTD; 398972; -.
DR   Xenbase; XB-GENE-1011033; arhgap21.L.
DR   OrthoDB; 142586at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 398972; Expressed in egg cell 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..1902
FT                   /note="Rho GTPase-activating protein 21-B"
FT                   /id="PRO_0000305248"
FT   DOMAIN          77..162
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          903..1016
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          1103..1295
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1039..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1306..1357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1375..1394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1494..1520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1559..1704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1729..1748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1803..1890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..901
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1064
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1066..1092
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1334..1356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1494..1513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1564..1587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1612..1630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1632..1680
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1823..1878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1902 AA;  211463 MW;  C61B9567A556E01E CRC64;
     MATRRAIVPE QQQEPSSPAS EISKNKDWQE QSEMVSPTEE EGFCWPGPKS VALRRASEGF
     GFTLRHFIVY PPESAVHTSV KDEENGNRGV NAGRPRNRLE PMDTIFVKQV KEGGPAHEAG
     LCTGDRIIKV NGESVIGKTY SQVIALIQNS DSTLELSVMP KDEDILQLAY SQDAYLKGND
     SYSGNAQNIP EPPPLCYPRV QPEASVMAQP VEVLPSGTSL ATQQSSCPLR TATTQPERSY
     RVEIQVPPSP TDIVKSNTAV CVCNEAVRTV IVPSEKVVDL SSNRTNRAGP LHRTGLADPS
     ILKRTTSPSS STPNVPMVPS TRHFDSAGVI GKPPSYGGLA ENMFSTRPAA HAEESPSPTN
     HYASPGSHQH IDWRDYKTYK EYIDNRRMLM YGCRTIQERL DSLRAASQNT TDYNQMLPNR
     SSGQVRRRST SHDRVPQSAQ MRKRSVSQER LEDPVLMKEW PRSASQDTLT SPAVASRNHR
     SELWDYLTRK GDFDQFIVET HSNGERNTNY QWSGFTEQDD RRGINERPRQ HAFHMSLRSP
     NFTMAPVPFT SSDNRRGGAR VLASAHPLQM VHPDMKTIQP TRNFQNSSRA PHPRPALSDR
     SGFAISKSNS VKIPTPYAAK PHSPSVRSDD GIVRDQKPVN YLHVGGPQNC QRKTQTESAL
     GFHLDSIKTS MSASSSSPST SQKVDVKITQ SPEANAGDSN AVLSPVDQVV LRERPSPGQQ
     TSPPIRQQSY IFAVNEQEGA SDTTCWLPND ARREVHIKRI EQRKASGSNS PGDSLASIPF
     IDEPTSPSID HEIGNIPASA VISISAQPLP TITTVPPSPT SPVPLMRRHF SHDHDSIRPI
     VLEVNSKTER SKSCDEGLDD YKEDGKLCLK QGSSLKGIKA RENVQSSEDS ESRKDSSSDV
     FSDSNKEGFL YFRQLTTEKG KRVSGSIRPW KQMYVVLRGS ALYLQKDKKE QTGHSSAQSD
     EEQLIGINGC LIDISYSETK RKNVFRLTTS DREFLFQAED RDDMLAWIKA IQENGNLNDE
     QTDQASRVLI SKRIKEYNTM MSSSSNKTEP SPKAQRQTLS IRQQFRAGKP DDDISPPKDK
     GSWRRIMKKP FEKKPTTGGT FGVRLDDCPP AHNNKYVPLI VDVCCKLVED RGLETTGIYR
     VPGNNAAISS MQEELNKGNT DIDIQDDKWR DLNVISSLLK SFFRKLPDPL FTNEKYNDFI
     EANRKEDPVE RLKTLKRLIL DLPDHHYETL KYLSAHLKTV ADSSEKNKME PRNLAIVFGP
     TLVRTSEDNM THMVTHMPDQ YKIVETLIQK HDWFFSEESA DEPITTVHEE STVESQPVPN
     IDHLLPNIGR TGLSPGDVSD SATSDSAKSK GSWGSGKDQY SRELLVSSLF AAASRKRKKQ
     KDKPQPSSSE DELDNVFYQK ELSQVEFQKP DKQNVDKDMD LKAKANALSL KDADNVKGTN
     IIKEDKLEKD IMYSEPTSPC PPKLLEPPIA NHGLQAPSND KNIPQINFQM EESMSDSGTM
     LSTSSQASVQ GSKPKVVSPE FKGSDFLTAD VSSITSDYST TSSTIYMTGL DSILISPEVQ
     SVAESKGEEA DDERSELVSE GRPMETDSEN DFPIFASSLA FDRRHQSKAE EPSRNVQVNS
     EGSPSCTEGS ITPKMDRRRF SSHKLIECDT LSRKKSVQQK TDSDCSAESK TEETLSDAQE
     AVKKGRSLSI VDPTGNNEPE EPAWRIKITE RLKLRLKASA DDMFGIGSQK ANAAETRKKK
     NIRRRHTLGG HRDFAEISVL NAWKINEPSS KEAELSAVDR LKPKCPSQDL SISEWLVRER
     LRTSTSELST VEPEEKHISE TTGQKESASA SPPPSSPSQV STAVLPAGSD SPSHETAPQP
     DDQMNGDSFQ SKNKNNFSPA VDAHPHKLSG TQVVRSRFYQ YL