ID A0A2U4BQ64_TURTR Unreviewed; 1535 AA.
AC A0A2U4BQ64;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 27.
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|RefSeq:XP_019795363.2};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019795363.2};
RN [1] {ECO:0000313|RefSeq:XP_019795363.2}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019795363.2};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_019795363.2; XM_019939804.2.
DR Proteomes; UP000245320; Chromosome 16.
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 CDD; cd11797; SH3_DNMBP_N4; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
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; 2.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
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..126
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 145..204
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 242..301
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 788..971
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 964..1178
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 1246..1309
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1471..1534
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 219..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1535 AA; 172571 MW; AE0400206D21D242 CRC64;
MEAGSVVRAI FDFCPSVSEE LPLFVGDVIE VLAVVDEFWL LGKKEDVTGQ FPSSFVEVVT
IPSLKEGERL FVCICEFTSL ELNSLSLHRG DLVVLDGTPT AGWLQGRSCW GARGFFPSSC
VRELCLSSQS RQWHSQSALL QIPEYSMGQA RALMGLSAQL DEELDFREGD VITIIGVPEP
GWFEGELEGR RGIFPEGFVE LLGPLRTVDE SVSSGNCDDC ITNGEVDTNT GEERQPEEEG
EQPGTYGIAL YRFQALEPNE LDFEVGDKIR ILGTLEDGWL EGSLKGRTGI FPYRFVKLCP
QTGVEETVDL PQESSLTNIP DTSLDCSEDF LEVEGKRHES HEYKAEKSNS VISETSTSPL
EHLTSEYEED KNSHWDVGSS EGPPRSTGSG HEQLLTKYSS TKDPSEVVNG VTSQTPVPFH
PELQKNQYYS TGGGSNPRPH QYSDPLPLEA RTRDYSSLPP RRTYSQPKTL QKPVTPLHST
FSRLASRAVR PSQLSPQLQG MARCVKKHLT PKENASSFCS ASEKSEMKPG LQDETPAVEA
VALSQGDGNT DLDSKLTQQL IEFEKSLSGP GTEPDKILRH FSIMDFNSEK DIFRGSSKLI
IQQELPERRK ALRPPPPRPC TPASTPPHLP VDQSLRPEPP LAMRPSRPAP LPPSAQQRTN
AVPPKLLTCN RPGWESLEKE GPENMEKTLD QTSQCPLVLV RIQEMEQDLD VCCRAQEELN
LPLEEKQEES LRADTPENLE FYESNIESLD MELQQLREMT LLSSQSSALV APSGSVSTES
PEQRMLEKRA KVIEELLQTE RDYIRDLEMC LERIMVPLQQ AQIPNIDFEG LFGNMQMVIK
VSKQLLADLE ISDAVGPVFL DHRDELEGTY KVYCQNHDEA ISLLEIYEKD EKIQKHLQDS
LADLKSLYNE WGCTNYINLG SFLIKPVQRV MRYPLLLMEL LNSTPESHPD KVPLTSAVLA
VKEINVNINE YKRRKDLVLK YRKGDEDSLM EKISKLNIHS IIKKSNRVSS HLKHLTGFAP
QIKDEVFEET EKNFRMQERL IKSFIRDLSL YLQHIRKERT ERLVISPLNQ LLNMFTGPHK
LVQKRFDKLL DFYNCTERAE KLKDKKTLEE LQSARNNYEA LNAQLLDELP KFHQYAQGLF
SNCVHGYAEA HCDFVRQALE QLKPLLSLLK VTGREGNLIA VFHEEHSRVL QQLQVFTFFP
ESLPATKRSF DRKTMDRQST RKPLLGLPSY MLQSEELRAS LLVRYPPEKL FQAERNFNAA
QDLDVSLLEG DLVGVIKKKD PMGSQNRWLI DNGVTKGFVY SSFLKPYNAR RSHSDASVGS
HSSTESEHGS SSPRFPRRQN SGGTLTFNPS SVAVSFSSGP TQKQPPDTSS LTEFDQGTLS
ASLNSESSPS RCPSDPDSPS QHGPWDSVDA ARDLQQPAPT LRSSRNPRHP EMAGHSVPGR
NGQGRDLVKG CARTALSLDD RNGQLENSEA EGNQVYFAVY TFKARNPNEL SVSANQRLKI
LEFKDVTGNT EWWLAEVNGK KGYVPSNYIC KTEYT
//
