ID A0A493TZV0_ANAPP Unreviewed; 1432 AA.
AC A0A493TZV0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Dynamin-binding protein {ECO:0000256|ARBA:ARBA00018186};
DE AltName: Full=Scaffold protein Tuba {ECO:0000256|ARBA:ARBA00032587};
GN Name=DNMBP {ECO:0000313|Ensembl:ENSAPLP00000031105.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000031105.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000031105.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000031105.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi apparatus, Golgi stack
CC {ECO:0000256|ARBA:ARBA00004348}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
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DR Ensembl; ENSAPLT00000033714.1; ENSAPLP00000031105.1; ENSAPLG00000010732.2.
DR GeneTree; ENSGT00950000183088; -.
DR Proteomes; UP000016666; Chromosome 6.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07589; BAR_DNMBP; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11798; SH3_DNMBP_C1; 1.
DR CDD; cd11794; SH3_DNMBP_N1; 1.
DR CDD; cd11795; SH3_DNMBP_N2; 1.
DR CDD; cd11796; SH3_DNMBP_N3; 1.
DR CDD; cd11797; SH3_DNMBP_N4; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 5.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR035820; DNMBP_SH3_C1.
DR InterPro; IPR035817; DNMBP_SH3_N1.
DR InterPro; IPR035818; DNMBP_SH3_N2.
DR InterPro; IPR035819; DNMBP_SH3_N3.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22834:SF19; DYNAMIN-BINDING PROTEIN; 1.
DR PANTHER; PTHR22834; NUCLEAR FUSION PROTEIN FUS2; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00499; P67PHOX.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 5.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 5.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 5.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 21..80
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 85..145
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 163..222
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 262..321
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 779..962
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1003..1212
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 1281..1344
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 226..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 702..752
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 416..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1432 AA; 158334 MW; 43F890A973221128 CRC64;
MGSGDGRTLR YRSACRPHAM EAGSVVRAVF DFCPSVSEEL PLFVGDVIEV LAVVDEFWLL
GKKEGVTGQF PSSFVEPVDI PPMKQGEKLF VCTSDFTSQE PGSLSLQRGD LVILGGSLAS
SWLQGRSSWG SKGFFPSSCV RELCLSTRSR QLSQSALLEV PAYSLGQARA LMDLSAQLEE
ELDFREGDVI NIVGIPEPGW FEGELRGQRG IFPEGFVELL TPLRAAGTSE DPEPRGTCDT
NGTVEVPTKQ EEDSREDGGQ EPGSTYGVAL YQFQALESQE LDFEVGDRIR IVGILEDGWL
EGELRGKRGI FPHRFVRLEA SDPCREKVGA GDPQAGVSCE VNIQQDPESA CSKALPLPGK
DGRDVEDGSI AHPVADTITS HMAERSEGPL GSDLRHQAFP DTGLQGPHPK ATADSLPSDC
TKTVNGLHPS AQLPPQQSSK PGQAGMLEPQ ALPEHDGDSP AMPQQAPCSP PDTCRSQVIS
PPNSWTAPEP QENQSSTQDL DGWVDSQQEK SKSCSSSLGG AHVGSDTWSG TWGECSLLTA
QGDGCTDLDS KLTEQLAQFE KSLSSTGAEQ DKVSRHFSIL DYSSEKDIVR GSPEPASHAK
PPERRKALRP PPPRPSTLTT APMPSQPSRL PKGRSLSFSV KPSRPAPRPP SSSQRRSLAP
LQLQPSAQEQ RAEEGRDDTM QTGAASPCSI LLTRIGEVER DLEAYGKTRA ELSLMLEEQQ
DELVRAETLE NLDFCDSNIE SLSVELQELR EMTLLSSQTP SLETSSAATE SPEHRMLEKR
SKVIEELLQT ERDYIRDLEM CVERIMVPLQ QAQVQNVDFE GLFGNIQVVI SFSKQLLSTL
EASDAIGPVF LAQRAELESV YRVYCQNHDE AIALLETYEK DEKIQKLLVD LLDSLRSLYS
EWGCTNYINL GSFLIKPVQR VMRYPLLLME LLSATPESHP DKAPLTAALL AVKEINVNIN
EYKRRKDLVL KYRKGDEDSL MEKISKLNFH SIIKKSNRVS SHLKHLTGFA PQLKDEAFEE
TEKNFRMQER LIKSFIRDLS LYLQHVRESA CMKALAAVSM WDLCTEKGSG DLDQFQKVNR
LISDQLFSNF KERTERLVSS PLNQLLSMFA GPHKLVQKRF DKLLDFHNCT ERAEKLKDKR
TLEELQSARN NYEALNAQLL DELPKFLCFA KELFASCVRG YAEAHCDFVR LALEELRPLL
SLLKVSGREG NLIAVFQEEH SRVLQQLQAF TFFPESQAAP KKPFERKSME RQSARRQPLG
ALPSYLLQSD DIRAALLARY SPDSLFQAER NFNAAQDLDV SLLEGDIVGV IKKKDPMGSQ
NRWLIDNGVT KGFVYSSFLK PYNPRRSQSD VSVGSHSSNE SEHSSSSPHS STTLTFSPSG
AAVAFTQKPL QDSASPGDPY QSPQTPSQTD SPSVPQLSSG DRTERLEAGV VT
//
