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Database: UniProt
Entry: A0A3B4VK88_SERDU
LinkDB: A0A3B4VK88_SERDU
Original site: A0A3B4VK88_SERDU 
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}.
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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
//
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