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Database: UniProt
Entry: A0A093SUC3_9PASS
LinkDB: A0A093SUC3_9PASS
Original site: A0A093SUC3_9PASS 
ID   A0A093SUC3_9PASS        Unreviewed;      1975 AA.
AC   A0A093SUC3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Rho GTPase-activating protein 21 {ECO:0000313|EMBL:KFW86119.1};
DE   Flags: Fragment;
GN   ORFNames=N305_13868 {ECO:0000313|EMBL:KFW86119.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW86119.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW86119.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW86119.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL672544; KFW86119.1; -; Genomic_DNA.
DR   STRING; 328815.ENSMVIP00005009241; -.
DR   Proteomes; UP000053258; Unassembled WGS sequence.
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; 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   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:UP000053258}.
FT   DOMAIN          29..125
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          937..1046
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1153..1345
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          346..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          864..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1093..1131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1376..1407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1425..1524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1538..1574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1619..1703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1715..1773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1834..1853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1879..1975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..934
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1382..1406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1433..1521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1627..1650
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1670..1687
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1715..1745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1910..1953
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW86119.1"
FT   NON_TER         1975
FT                   /evidence="ECO:0000313|EMBL:KFW86119.1"
SQ   SEQUENCE   1975 AA;  220524 MW;  79873A1801F22CFA CRC64;
     SKNKDGKEQS EAISPSEEEE TFSWPGPKTV VLRRTSQGFG FTLRHFIVYP PESAVQFSFK
     DEENGNRQGK QRNRLEPMDT IFVKQVKEGG PAFEAGLCTG DRIIKVNGES VIGKTYSQVI
     ALIQNRDSVN FELVFPLLKI DHANTGWRTF LSPSLLNTHL ILSPQAYSQD AYLKGNEAYS
     GNAHNIPEPP PICYPRLTST ASVKAQAADK LSSDFSLGKQ QVSRPVRALT QPERAYRMEI
     QVPPSPTDIA KSNTAVCVCN ETVRTVIVPS EKAVDLPSCR NNHAGPSHRT EEVRYGLKDQ
     TSLKARTTSP SSSVSTAIVL PQTPITRPVD TTGAVSKASN YVVCPEGIPS TRPPAQATDS
     PSVSTNHYSS PTSHQHIDWK TYKTYKEYID NRRMHMYGSR TIQERLDSLR AASQNTTDYN
     QVVPNRTASQ VRRRSTSHDR VPQSVQIRQR SVSQERLEDP VLMKEWPRSA SQDTLTSPSV
     NARNHRARSW DYLSKQGEVL ENFHSDNMIA DTNGDRRKTY KWTGFTEQDD RRGIYERSRQ
     HAFHMSLRGQ NFPIAPSAYI SDNRRTGSRA SLPGSHFQKI SPDFKMLQPS RDLQTPGGVS
     KPAAVSQERL CLTPARSSRS SSLKNSAPYA AKPSIPLNQG LDAIASKDQR TVNHLHQSGL
     LNQQSRIRAE GAQDHKTETG KTIQPSSLSP ASAKLVQPSE CSTTSDNVDG SIRQKIHFER
     EDVRESESLQ TDVQGNDKDT VVMRDKSPSG HQTPQPLRHQ SYILAVNDQE AASDTTCWLP
     NDARREVHIK RIEERKASGS SPPGDSLASI PFIDEPTSPS IDHDIAHIPA SAVISASASQ
     APAITTVPPS PTSPIPLIRR QLSHDHESMR PSVLDSQPAA KTERSKSYDE GLDDYREEGK
     SSIKHVSSLK GIKVPDSQKS SEDSGSRKDS SSEVFGDASK EGWLHFRQLV TDKGKRVGGS
     IRPWKQLYVV LRGHSLYLYK DKKEQVTLSE EEQPISINAC LIDISYCETK RKNVFRLTTS
     DCEYLFQAED RDNMLAWIKA IQDNSNLNDE DTGVTSRDLI SRRIKEYSTM MSKTEPSPKT
     PRQSLSIRQT LLGTKAEQRT QSPHSPKDES ERKLLTKDET SPPKDKGTWR KGIPSIMRKT
     FEKKPSAVGT FGVRLDDCPP AHTNKYIPLI VDICCKLVEE RGLEYTGIYR VPGNNAAISS
     MQEELNKGMT DIDVHDDKWR DLNVISSLLK SFFRKLPEPL FTNDKYADFI DANRKEDPVE
     RLKTLKRLIH DLPEHHYETL KFLSAHLKTV AENSEKNKME PRNLAIVFGP TLVRTSDDNM
     THMVTHMPDQ YKIVETLIQK HDWFFTEDDA EEPLTAVQEE NTVESQPVPN IDHLLTNIGR
     TGVSPGDVSD SATSDSAKSK GSWGSGKDQY SKELLVSSIF AAASRKRKKT KEKPQPSSSE
     DELDNVFFKK ELAEQSRGDT TKEDTAKGEY EREREIGRKQ RMFVLKEKEN SSKKDVNVVK
     DEKKSLKKES ILSEEPSLPY HEKCTKSSNL NCLQTMQKNN PKMPISQSSS QVEETVSDSG
     TMLSTSSQAS QHRYSCKKVA SPEIKHNEFL AADVSSITSD YSTTSSTMYL TGLDASMLSP
     EVQSVTESKG EDADDERSEL ISEGRPMETD SESDFPVFAT SAAAERLSKG KVSEVVKTSR
     RNSEESEVSC TEGSSTPKLE SRRLFSSHKL IECDTLSRRK SARHKTDSEG SGDAKSEKDL
     PTVTKMFDIM KKGRSTSSLA TSARSEADKQ EPTWRLKITD RLKLRLKSSA DDMFGVGNQK
     TNSAETAKRK NIRRRHTLGG QRDFAEISVL NAWKAQEPSQ SRERESELSA VTRLKPKCPA
     QDLSISDWLA RERLRTSTTD LNTGETGKPR LENTSLADVS KVDLPSSADM QADEGSSSSS
     LTLINRTPPS GPFQPLDQVN GENYQNMNKN NFSPAVDAHP HKLSGTQVVR SRFYQ
//
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