ID A0A3B4VK88_SERDU Unreviewed; 1735 AA.
AC A0A3B4VK88;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Dynamin-binding protein {ECO:0000256|ARBA:ARBA00018186};
DE AltName: Full=Scaffold protein Tuba {ECO:0000256|ARBA:ARBA00032587};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000030200.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000030200.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Golgi
CC apparatus, Golgi stack {ECO:0000256|ARBA:ARBA00004348}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
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; ENSSDUT00000030719.1; ENSSDUP00000030200.1; ENSSDUG00000021757.1.
DR GeneTree; ENSGT00950000183088; -.
DR OMA; YCGNHEA; -.
DR Proteomes; UP000261420; Unplaced.
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; cd12141; SH3_DNMBP_C2; 1.
DR CDD; cd11794; SH3_DNMBP_N1; 1.
DR CDD; cd11795; SH3_DNMBP_N2; 1.
DR CDD; cd11796; SH3_DNMBP_N3; 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; 6.
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; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 3.
DR PRINTS; PR00499; P67PHOX.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 6.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 6.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 6.
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 SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 2..61
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 66..130
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 152..211
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 273..332
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 876..1053
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1094..1303
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 1374..1437
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1671..1734
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 332..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1479..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 742..820
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 332..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1665
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1735 AA; 196535 MW; 505232AB19DB40A9 CRC64;
MEAGKVVRAV FEFLPSVSEE LPLFTGDVIE VLSVVDEFWL LGNKDGVTGQ FPSTFVEEVT
IPSTKPGDQL YVCINDFSSA EPGNLSLKRG DVVVREAGGS MDLGETWQRG CNAWGVRGLF
PTSCVKELNL SGRSRQLSER SAQAQASELP PYALGQARAL MNLHAQLNEE LDFREGDLII
ITGLPEPGWF QGELEGRRGI FPEGFVELLA PLRSPQEPVD CQYLNDDPQQ FSYEDPYDAG
EGTEEEGVEE GEVFLREEEE QKEDVVEEEE EEEGGVYGVA LYEFRAMEPG ELDFDVGDRI
RVISTLEDGW LEGEVRGQRG IFPHRFVKID DGGQKTAEET NVVEPEEDKE NSCSSEYSPD
HSCPNGAEDD PDWRTYEDHT VWDLDYFERT EEQRWQSENK SAGAQTNNRA QREGGSRPDS
QPRRPVAPAQ RGPERPKSTP PARPRLPPRP SLPAHSHRQH GSSSGTNRSN HTNGNTRPLQ
SKLTHSLTLP STRSGLSKDS RHYKRPPADG AATNIRGASL GQALINLVEA HKQKKLTRHA
SVSDADMMMG GAETRTHSQQ SVRGYNGMMP TSITLDALAT SAGDLEAKLT QQLFEFEKSL
TTSYIDSNMS SGASRDMSSV VDLSQQSPIS RHFSILEYSD ESDIIRGSSH SPVSHLLQSK
SASSSLERRR TLRPPPPRPR VLRPQAPAAY KPARPAPRPP PRCPRQNAAP PTGSPIFYTP
DEPAVNLLDD ITEGQAEFGD LAAAQEHEIQ CQLEEEKELE REMELESQRQ REEEERYQLL
LRLQEVEHDM EAYAHTAEEL RAMLEEEDDE TARMQAMENL EFCNYTLETL ALEQQQLQEM
TLLSSQPKSL DSTPTSDSTP TSGTGTEDPE QRMLEKRSKV IEELLQTEKD YIKDLQMCVK
EIIEPLQKKQ VKNVDFDGLF GNISSVIDLS QRLLDTLQET DSIGKVFVDF KAELEEVYKI
YCQNHDDAIS LLESYEKDEN IQRHVLECLD RLRGKTNYIN LGSFLIKPVQ RVMRYPLLLM
ELLGATPESH HDRPQLHQAL QAVKEINVNI NEYKRRKDLV VKYRKGDEDT FIDKISKLSM
HSIIKKSNRV SSHLKHLTGI SPQIKDEAFD EAEKKFRLQE RLIKSFIRDI SLYLQHIRES
ASVKVLAAIS FCDIYTERSV LDPERFQRAH RCISDKQFTQ FKERTEALVI NPLTQLLLMF
AGPHKLIQKR FDKLLDYDNC KERADRLKDR RVQEDLQVAR NNYEALNAQL LDELPKFHSA
AEDLFTGCVR AFAQSQKDFM KTTLGELKPL LQFSNKVGME GNLIAQFQEE YGRVLQLLQS
FSFCPENLPP AASTKKPFEK KTLEKQTSKK QLQGPPNYIM QTEEHRAGLL VRYGPEKLFQ
AERNFNAAQD LDVSILEGDL VGVIKQQDPM GSHNRWLIDN GVTKGFVYSS FLKPYNPRRS
QSDVSIESQS SNESGYGGSS PVFSRQNSNS TLTFNQETAT VSFSTSQHQS HSSPHPSLDS
ASYRRSHHRD ALNPDSASQS NSINSSPRNP SNRREFLDQT HRNSPSHRDT EPSYRHSGNH
RDSYDTSYAS SSSHKETSDL SETDSSSSHR NNHSQRYGHT DKSYSSYQWR NGDNGGQKKS
VYSRDEYIEP EPEPEPEPEP EPEPEPEPEL EPELDPEPEP EPEPEHDSEL DGHQIYYALY
SFNARCANEL SISANQRLRI LEFQDMNGNS EWWLGEAGGR RGYVPSNYIR KSEYT
//