ID H0YSE5_TAEGU Unreviewed; 1992 AA.
AC H0YSE5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Rho GTPase activating protein 21 {ECO:0000313|Ensembl:ENSTGUP00000001205.2};
GN Name=ARHGAP21 {ECO:0000313|Ensembl:ENSTGUP00000001205.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000001205.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000001205.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000001205.2}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSTGUT00000001217.2; ENSTGUP00000001205.2; ENSTGUG00000001167.2.
DR GeneTree; ENSGT00940000155406; -.
DR Proteomes; UP000007754; Chromosome 2.
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: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; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
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:SF16; RHO GTPASE-ACTIVATING PROTEIN 21; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00169; PH; 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 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:UP000007754}.
FT DOMAIN 58..167
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 948..1057
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1168..1360
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1992 AA; 222515 MW; 0D36B69C9EC1ECD2 CRC64;
MAQFRILDCV INHNWNFICN LYCAWSDQAS KNKDGKEQSE AISPSEEEET FSWPGPKTVV
LRRTSQGFGF TLRHFIVYPP ESAVQFSFKD EENGNRQGKQ RNRLEPMDTI FVKQVKEGGP
AFEAGLCTGD RIIKVNGESV IGKTYSQVIA LIQNSDSILE LSVMPKDEDI LQLAYSQDAY
LKGNEAYSGN AHNIPEPPPV CYPRLTSTAS VKAQAGDKLP SDFSLGKQQV SRPVRALTQP
ERAYRMEIQV PPSPTDIAKS NTAVCVCNET VRTVIVPSEK AVDLPSCRNN HAGPSHRTEE
VRYGIKDQTS LKAWTTTSPP SLVSTAIVLP QTPITRPVDT TVTVSKASNY VVCPEGIPNT
RPSTQATDSP SVATNHYSSP TSHQHIDWKT YKTYKEYIDN RRMHMYGSRT IQERLDSLRA
ASQNTTEYNQ VVPNRTASQV RRRSTSHDRV PQSVQIRQRS VSQERLEDPV LMKEWPRSAS
QDALTSPSVN ARNHRARSWD YLSKQGEVLE NFHSENMIAD ANGDRRKTYK WTGFTEQDDR
RGIYERSRQH AFHMSLRGQN FPIAPNTYIS DNRRTGSRAS LPGSHFQKVS PDIKVLQPSR
DLQTPGGVSK SAGVSQERLC LTSARSSKSS SLKNSAPYAA KPSIPLNQGL DAIASKDQRT
VNNLHQSSLL NQQSRIRAEG APDHKTETGK TIQPSSLAPA STKLVHPTSE CLTTSDNIDG
SIRQKIHGIE REDVHESESL QMDVQGNDKD TVVMRDKSPS GHQTPQPLRH QSYILAVNDQ
EAASDTTCWL PNDARREVHI KRIEERKASS SSPPGDSLAS IPFIDEPTSP SIDHDIAHIP
ASAVISASAS QAPAITAVPS SPTSPIPLIR RQLSHDHESI RPSVLDSQPA AKTERSKSYD
EGLDDYREEG KSSIKHVSSL KGIKVPDSQK SSEDSGSRKD SSSEVFGDAS KEGWLHFRQL
FTDKGKRVGG SIRPWKQLYV VLRGHSLYLY KDKKEQVTLS EEEQPISINA CLIDISYCET
KRKNVFRLTT SDREYLFQAE DRDNMLAWIK AIQDNSNLND EDTGVTSRDL ISRRIKEYST
MMSSSSSKTE PSPKTPRQSL SIRQTLLGTK AEQRTQSPHS PKDETERKLL TKDETSPPKD
KGTWRKGIPS IMRKTFEKKP SAVGTFGVRL DDCPPAHTNK YIPLIVDICC KLVEERGLEY
TGIYRVPGNN AAISSMQEEL NKGMTDIDVH DDKWRDLNVI SSLLKSFFRK LPEPLFTNDK
YADFIDANRK EDPVERLKTL KRLIHDLPEH HYETLKFLSA HLKTVAENSE KNKMEPRNLA
IVFGPTLVRT SDDNMTHMVT HMPDQYKIVE TLIQKHDWFF TEDDAEEPLT AVQEENTVES
QPVPNIDHLL TNIGRTGVSP GDVSDSATSD SAKSKGSWGS GKDQYSKELL VSSIFAAASR
KRKKTKEKPQ PSSSEDELDN VFFKKELAEQ SRGDTAKENT AKGEYERERE IGRKQRMFVL
KEKENSSKKD VNVVKDEKKS LKKENILTEE PSLPYDEKCT KSSNINCLQT MQKNNPKMPI
SQSSSQVEET VSDSGTVLST SSQASQHRYA CKKVASPEIK HNEFLAADVS SITSDYSTTS
STMYLTGLDA SMLSPEVQSV TESKGEDADD ERSELISEGR PMETDSESDF PVFATSAAAE
RLSKGKVPEV VKTSRRNSEE SEVSCTEGSS TPKLESRRLF SSHKLIECDT LSRKKSARHK
TDSEGSGDAK SEKDLPTVTK MFDIMKKGRS TSSLATSAKS EADKQEPTWR LKITDRLKLR
LKSSADDMFG VGNQKANSAE TAKRKNIRRR HTLGGQRDFA EISVLNAWKA QEPSQNRERE
SELSAVTRLK PKCPAQDLSI SDWLARERLR TSTTDLNTGE TGKPRLENTN LAEVSKVELP
SSAEMQADEG SSSSSLTLIN RTPPSGPFQP PDQVNGENYQ NMNKNNFSPA VDAHPHKLSG
TQVVRSRFYQ YL
//