ID A0A3B4ZL84_9TELE Unreviewed; 1811 AA.
AC A0A3B4ZL84;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Rho GTPase-activating protein 21-like {ECO:0000313|Ensembl:ENSSPAP00000002422.1, ECO:0000313|RefSeq:XP_008290407.1};
GN Name=ARHGAP21 {ECO:0000313|Ensembl:ENSSPAP00000002422.1};
GN Synonyms=LOC103364897 {ECO:0000313|RefSeq:XP_008290407.1};
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:ENSSPAP00000002422.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000002422.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008290407.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_008290407.1; XM_008292185.1.
DR STRING; 144197.ENSSPAP00000002422; -.
DR Ensembl; ENSSPAT00000002460.1; ENSSPAP00000002422.1; ENSSPAG00000001861.1.
DR GeneID; 103364897; -.
DR CTD; 326745; -.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
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; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
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:SF24; RHO GTPASE-ACTIVATING PROTEIN 21 ISOFORM X1; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00683; SPECTRINPH.
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 GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000694891}.
FT DOMAIN 56..163
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 815..929
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1039..1232
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1741..1766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1811 AA; 200562 MW; 7BAEBDFCCDC02AB6 CRC64;
MMAASRWVPS CEDDDRQRAR SSFCESDSQE WRNLADSPAA QYPTEDEVFS WPRPKTVRLC
RTSQGFGFTL RHFIVYPPES TLHCFLEEDH GRRGRQRNRL EQMDTIFVKQ VKEGGPAHGA
GLCTGDRIVK VNGASIIGKA YCEVISLIQD SGDFLELCVM PKDEDILQLA YSQDAYLRGH
STYSGNACHI PDPPPVCYPR VDCKPTGMAQ ATDSAGQVCR GPAAPPDHGY RKEIPVPPSP
PPPQSYPKSQ TAVCMRNDSV RTVVVPPNTT HMGRMGPAHR IDFMDPVFAR GRPGSLAQYP
HPRKADVYPG GPGMVGYGGQ APHFPGNHQN IDWRTYQTYR EYIDNKGIHS HGSRTIQERL
DNLRSTSHAT FGASHHIPRG DWGPKGIRRR STSHERSYQG PPPHFQIAPR SASQDRMSSA
EKMSHARNWP PRSVSQDGLV HKARARSTDY VDPAELARPS ERRAGYGRAD QGTRPSRQSI
PRHAMLYRPS VGHSGMRGPP NPSLYSKGPD SLQTRSSPML SDRPRHFGKS TSAEHSFADQ
RLSVKGNHAA YSTQGQNRMR AETMQPVEAG RDAALAAHRS SSCSTPKEMP QRPSILKPPP
LELQCQVNGR SPTESGVVLR EKPPSGKNPS PLRHPSYILA VNDDGPDSTT DVSACWLPND
ARREIHIRRL GEQCHTSCSS NLDESLDSIP FIDEPVSPSV DREAAPIPPS AVISVAPSIT
TGPSSQGSPC PPIRRQLSHD QESLRSALLD SDSASKTERS KSYDEGLDNY QEESRGRSSS
KHMPSLRGLR KALDGHKSSG DSGSRRDSSS DIFADSSKEG LLNFRQLSTD KNKRVGGGMR
SWKQMYAVLQ GHTLTLYKDR KEALSHATTQ SDEDPLRISI KACLIDISYS DTRRKNVLRL
TTSDCEYLFQ AEGRDDMLTW IRVIQENSNP DEENATVTSQ DLISRKIKEY NMMSAPSSRS
EPSPKTSRQS LSIKQAFMGS KADVKSHSPH SPRPGEERRA LKDDSSPPRD RGAWKLGGIA
GIMKKPFEKK TPAGITFGVR LDDCPSAQCN RYVPLIVEVC CKVVEERGLE YTGIYRVPGN
NAAISSMQEE LNTKGMTDID IQEDKWRDLN VISSLLKSFF RKLPEPLFTN EKYADFIEAN
RTEESVERLK ELKRLIYELP HHHYETLKFL CAHLKKVSDN CEKNKMEPRN LAIVFGPTLV
RTSEDNMTNM VNHMPDQCKI VENLIQQFDW FFTDDSDEDP VTTAEQESTV QSQPVPNIDH
LLSNIGRTAA SPGEVSDSAC SDSSKSKGLW GSGKDQCSKE MLRSSFFANR KRKKPKDKAH
PSSSDDDLDH VFTKKELPEE SQQQSLWSPG SRTEEEEQTD ETSEKENLRT SSEEQLDKSN
RKESLSSSPM SQPSPSLPPE HISSTLPTGS PYTSPSHSPN LSYRMPMAHQ SSLSDPPSNY
DDTVSDLGTM NSTSSQASVP RVRRGRMAAL GTDACPSGLG AEVCSITSDY STTSSMTFLT
GAELSTLSPE VQSVSESRGG EDADDERSEL ISEGRPMETD SESDLSVFTV GKADQRELQE
APRPLPSHRL IECDTLSRKK AAQQKTDSES SLEGARSDKD SNRLSRVLGS VKGRSTGSLS
SSSRSELDKT EPAWKLKITD RLKVRLRMSV DDMFGVGSQR SRSPEGRSKK KNIRRRHTMG
GQRDFAELSV LGDWPQSVAI GSGSRSELSA VDRLKPKCSS QDFSIGDWIA RERHRTSNPE
VSLDFSEQQG GLCGANSQNL GASSSSELPH RPGEALNGDV PQSKNLSLSA TAHPHKLTSS
QVVHSRFYQY L
//
