ID A0A3B5A5T5_9TELE Unreviewed; 1989 AA.
AC A0A3B5A5T5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Rho GTPase activating protein 21 {ECO:0000313|Ensembl:ENSSPAP00000016110.1};
DE SubName: Full=Rho GTPase-activating protein 21 isoform X3 {ECO:0000313|RefSeq:XP_008292315.1};
GN Name=ARHGAP21 {ECO:0000313|Ensembl:ENSSPAP00000016110.1};
GN Synonyms=arhgap21 {ECO:0000313|RefSeq:XP_008292315.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000016110.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000016110.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008292315.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic
CC vesicle membrane {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00004284}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004395}.
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DR RefSeq; XP_008292315.1; XM_008294093.1.
DR Ensembl; ENSSPAT00000016371.1; ENSSPAP00000016110.1; ENSSPAG00000012148.1.
DR GeneID; 103366386; -.
DR CTD; 57584; -.
DR GeneTree; ENSGT00940000155406; -.
DR OrthoDB; 2997116at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; 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:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01253; PH_ARHGAP21-like; 1.
DR CDD; cd04395; RhoGAP_ARHGAP21; 1.
DR Gene3D; 1.20.5.220; -; 1.
DR Gene3D; 2.30.42.10; -; 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; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23175; PDZ DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23175:SF16; RHO GTPASE-ACTIVATING PROTEIN 21; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000694891}.
FT DOMAIN 58..166
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 959..1073
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1184..1377
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1651..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1828..1855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1907..1977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1773..1787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1907..1932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1989 AA; 216397 MW; B2E80408C7ECCE64 CRC64;
MMAARWSDSP QDNEERKHTA VTPCCEAKQK DGRDQSEASA AASPGAEEEP FSWPGPKTLH
LRRTSQGFGF TLRHFIVYPP ESAVHNSLKD EENGSRGRQR NRLEPMDTIF VKQVKEGGPA
HGAGLCTGDR IVKVNGESII GKTYSQVIAL IQNSDASLEL CVMPKDEDIL QLAYSQDAYL
KGNEAYSGNA QNIPEPPPIC YPRIEVKAAG MAQSSEPAAV SETPRGPVQG PGRRGGATEK
SYRVEIPVPP SPPPQQTSKS QTVVCVCNEN VRTVAMPPDP VDRGSRVARA GPSHRTEENR
YGPSADSGSA RPRPLIPSVP GGAQLQYPSS HPTETPVYSP SSTSRPGAIY SDTLSPAGRA
PNAASPDTFS TAVSPSSNHY SPSPTAPSTS PHQNIDWRTY TTYKDYIDAK RLHTYGCRTI
QERLDSLRAA ANSSSAYAQQ RTTPPPCTSQ RGASQLRRRS ASNDRGVDAS SQGTAVTTPL
RSVSQERLGG GAERTITTRN WPRSVSQDAL PFSTPTGVTK PRARSCDYLG QQPGEPGGVF
SVDRTGFEDR LLLSRGEEAR ASRQGAGLRA LPHLNRSLNG QEEERRGSGL SNSPLAAPVF
TKGTTDSALP SRTDGLIMRP SRLPVKTSIS DPSPALSSTK TTDPLKDQRA NIIGNHLGYS
SPLHLQLRGR ADSLKMESRS EAGLAARSSS CSGPSSKLPM QRQLQSGVVT ASSGSSTTNG
ALSQKPKVRE TSSSTGALVR TNGGLAEGVE GPDATVVVLR RDKNSASAHI RPPSYVLAVN
DNQGGVTHKS PPLVKAGSAD GAMYWMSNDS CREMHLRRLG DTRQKSGSNN LDDSLDSIPF
IDEPSSPSID LDSTHITASA VISATPIITT IPPSPTSPSP LIRRQLSHDQ DSLRLTIIES
DSGTKTERSK SYDEGLDNYR EESRGRSLIP GLKSLRKAVD RSSEDSGSRR DSSSDVFCDA
TKEGLLHFKQ LHTDKGKRVG GGMRPWKQMY AVLRGHYLCL YKDKKEGQAH ANCQAVDEPL
PISIKACLID ISYSDTKRKN VLRLTTSDCE YLFQAEDRED MLAWIRVIQE NSNLDEENAA
FTSHDLISRK IKEYNTLMSP TGSKTEPSPR PSRQSLSIRQ TLLGGKGETK ATSPHSPKPE
QEKKNMHKDD TSPPKDKGTW RKGIPGLMRK PFEKKPSPGV TFGVRLDDCP PAQCNKFVPL
IVEVCCKLVE ERGLEYTGIY RVPGNNAAIS NMQEELNNKG MNDIDIQDDK WRDLNVISSL
LKSFFRKLPE PLFTNDRYTD FIEANRIEDP VERLKVLKRL LHELPDHHYE TLKFLSAHLK
TVAENSEKNK MEPRNLAIVF GPTLVRTTED NMTHMVTHMP DQYKIVETLI QNYDWFFTED
GNGEPVTVSQ EESAVESQPV PNIDHLLTNI GRTGTSQGEV SDSPTSDSAK SKGSWGSGKD
QCSRELLVSS IFAAASRKRK KSKEKPQPSS SDDDLDAVFP KKEIPGQKPN HQTEAQSETR
PSPNAKPNAK QQARAEERKE NGRTVELTPK AKREHRNSLF LKEKTPSRHP SPSPSPNISA
SPNISYQAAP QGKSSLSDPP SQLDENTSDL GTMSSGASVP RSRPKKWTVG ASPDLPACVG
LGAGAGASAG AEVSSITSDY STTSSITFLT GAESSALSPE LQGGEEADDE RSELISEGRP
METDSESDFP VFAPGGGSSQ STPCPEQNQE KTEPRGGGAA EGSTTPKLET RRLFPSHRMI
ECDTLSRRWS LRQKTDSESS VEGAAGSGER GEGRAESSTR LSRVLEVMKK GRSTSSLSSS
SRSESERPEP AWHLKITERL KFRLRTSADD MFAQKNRAPD ARGKKKNIRR RHTMGGQRDF
AELAVINDWR EQGGVDQAAE LSALDRLKPR CSSQDFSIRD WIARERCRGS ESSGEVAPKA
VPEDDHPEAQ DAAHETPPPP ASPGAQPIAG EQLNGSGLQG KNKASLGADA HPHKLSGAQV
VRSRFYQYL
//
