ID A0A091HVR9_CALAN Unreviewed; 1954 AA.
AC A0A091HVR9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Rho GTPase-activating protein 21 {ECO:0000313|EMBL:KFP00047.1};
DE Flags: Fragment;
GN ORFNames=N300_06442 {ECO:0000313|EMBL:KFP00047.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP00047.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP00047.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP00047.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL217900; KFP00047.1; -; Genomic_DNA.
DR STRING; 9244.A0A091HVR9; -.
DR Proteomes; UP000054308; 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:UP000054308}.
FT DOMAIN 29..138
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 918..1027
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1134..1326
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 331..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1515..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1695..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1890..1906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1917..1932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP00047.1"
FT NON_TER 1954
FT /evidence="ECO:0000313|EMBL:KFP00047.1"
SQ SEQUENCE 1954 AA; 218354 MW; 411C35D0EBB63BCB CRC64;
SKNKDGKEQS EALSPSEEEE TFSWPGPKTV VLRRTSQGFG FTLRHFIVYP PESAVQFSFK
DEENGNRQGK QRNRLEPMDT IFVKQVKEGG PAFEAGLCTG DRIIKVNGES VIGKTYSQVI
ALIQNSDSIL ELSVMPKDED ILQLAYSQDA YLKGNEAYSG NAHNIPEPPP ICYPRLTSTA
SVMAQAGDKL SSDFSLGKQQ VSRPVRALTQ PERAYRMEIQ VPPSPTDIAK SNTAVCVCNE
TVRTVIVPSE KAVDLPSCRN NHAGPSHRTE EVRYGLKDQT SLKARTTSPS SSVSTAIVLP
QTPITRPVDP TGTLSKPSNY VVCPEGIPNT RSPAQVTESP SVSTNHYSSP TSHQHIDWKT
YKTYKEYIDN RRMHMYGSRT IQERLDSLRA ASQNTTDYNQ VVPNRTAPQV RRRSTSHDRV
PQSVQIRQRS VSQERLEDPV LMKEWPRSAS QDTLTSSSVN AKNHRARSWD YLSKQGEVLE
NFHSDNLIAD TNGDRRKTYK WTGFTEQDDR RGIYERSRQH AFHMSLRGQN FSMAPSAYIS
DNRRTGSRAS LPGSHFQKVP PDIKMLQSSR DLQTPGGVLK PTAVSQERLS LTPARSSKSS
SLKNSAPYAA KPSFPLNQGL DAVASKDQRT VNHLHQCGLL NQQSSIRAEG ALDHKTVTGK
TIQPSSLSPA STKLVHPMSE SLTTSDNVDG SIRQKIHDFE REDVHEPEIL QMDGQENDKD
RVVMRDKSPS GHQTPQPLRH HSYILAVNDQ EAASDTTCWL PNDARREVHI KRIEERKASG
SSPPGDSLAS IPFIDEPTSP SIDHDIAHIP ASAVISASAS QTPAVTTVPP SPTSPIPLIR
RQLSHDHESI RPSVLDSQPA AKTERSKSYD EGLDDYREDV KPSIKHVSSL KGIKVPDSQK
SSEDSGSRKD SSSEVFGDAS KEGWLHFRQL VTDKGKRVGG SIRPWKQLYV VLRGHSLYLY
KDKKEQVTPS EEEQPISINA CLIDISYCET KRKNVFRLTT SECEYLFQAE DRDNMLAWIK
AIQDNSNLND EDTGVTSRDL ISRRIKEYNT MMSKTEPSPK TPRQSLSIRQ TLLGTKAEQR
TQSPHSPKDE SERKLFTKDE TSPPKDKGTW RKGIPSIMRK TFEKKPSAVG TFGVRLDDCP
PAHTNKYIPL IVDICCKLVE ERGLEYTGIY RVPGNNAAIS SMQEELNKGM TDIDVHDDKW
RDLNVISSLL KSFFRKLPEP LFTNDKYADF IDANRKEDPV ERLKTLKRLI HDLPEHHYET
LKFLSAHLKT VAENSEKNKM EPRNLAIVFG PTLVRTSDDN MTHMVTHMPD QYKIVETLIQ
KHDWFFTEDD AEEPLTAVQE ENTVESQPVP NIDHLLTNIG RTGVSPGDVS DSATSDSAKS
KGSWGSGKDQ YSKELLVSSI FAAASRKRKK TKEKPQPSSS EDELDNVFFK KELAEQSRDT
TKEDIAKGEY ERERDLGRKH RMFVLKEKEN SSKKDVNVVK DEKKTLKKEN ILSQEPSLPY
HEKCTKSPNL SCLQTTQKNN PKIPISQSSS QVDETVSDSG TMLSTSSQAS QHRYSCKKVA
SPEIKHSEFL AADVSSITSD YSTTSSTMYL TGLDASMLSP EVQSVTESKG EDADDERSEL
ISEGRPMETD SESDFPVFAT SAAAERLPKG KVSEVVKTSR RNSEESEVSC TEGSSTPKLE
SRRLFSSHKL IECDTLSRRK SARHKTDSEG SGDAKSEKDL PTVTKMFDIM KKGRSTSSLA
TSAKSEADKE PTWRLKITDR LKLRLKSSAD DMFGVGNQKA NSAETAKRKN IRRRHTLGGQ
RDFAEISVLN AWKAQEPSQS REREAELSAV NRLKPKCPAQ DLSISDWLAR ERLRTSTTDL
NTGETGKPRP ENMSLADVSQ AELPLSEELQ ADEGSSSSSL TLINRTPPLG PFQPPDQVNG
ENYQNMNKTN FSPAVDAHPH KLSGTQVVRS RFYQ
//
