ID A0A455AP73_PHYMC Unreviewed; 1411 AA.
AC A0A455AP73;
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|RefSeq:XP_028337844.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028337844.1};
RN [1] {ECO:0000313|RefSeq:XP_028337844.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028337844.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Golgi apparatus, Golgi stack {ECO:0000256|ARBA:ARBA00004348}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
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DR RefSeq; XP_028337844.1; XM_028482043.2.
DR Proteomes; UP000248484; Chromosome 20.
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; 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; 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; 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; 4.
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; 4.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
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 787..970
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1011..1220
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT REGION 219..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1411 AA; 159826 MW; 72899839D5A7B610 CRC64;
MEAGSVVRAI FDFCPSVSEE LPLFVGDVIE VLAVVDEFWL LGKKEDVTGQ FPSSFVEVVT
IPSLKEGERL FVCICEFTSL ELNSLSLHRG DLVVLDGTPT AGWLQGRSCW GARGFFPSSC
VRELCLSSQS RQWHSQSALL HIPEYSMGQA RALMGLSAQL DEELDFREGD VITIIGVPEP
GWFEGELEGR RGIFPEGFVE LLGPLRTVAE SVSSGNCDDC ITNGEVDTNT GEERQPEEES
EQPGTYGIAL YRFQALEPNE LDFEVGDKIQ ILGTLEDGWL EGSLKGRTGI FPYRFVKLCP
QTRVEETMDL PPESSLTNIP DTSLDCSENL EVEGKRHESH ECKAEKSSSV ISETSTSALE
HLTSEYEEDK NSHWDAGTSE GPPRSTGSGH EQLLARYSST KDPSEVVNGV ASQTPVPFHP
ELQKNQYYSI GGGSNPRPDQ YSDPLPLEAR TRDYSSLPPR RTYSQPKTLQ NPVPPLHSTF
SHLASRAVRP SQLSPQLQGV ARCVKKHLTP KENASSFCSA SERSEMKPGL QDKAPAVEAM
ALSQGDGNTD LDSKLTQQLI EFEKSLSGPG TEPDKILRHF SIMDFNSEKD IFRDSSKLII
QQELPERRKA LRPPPPRPCT PASTPPHLPV DQSLRPEPPL AMRPSRPAPL PPLAQQRTNA
VPPKLLTCNR PGWETLEKEG PENMEKTLDQ TSQCPLVLVR IQEMEQDLDM CCRAQEELNL
LLEEKQEESL RAETPENLEF YESNIESLNM ELQQLREMTL LSSQSSALVA PSASVSTESP
EQRMLEKRAK VIEELLQTER DYIRDLEMCI ERIMVPLQQA QIPNIDFEGL FGNMQMVIKV
SKQLLADLEV SDAVGPVFLD HRDELEGTYK VYCQNHDEAI SLLEIYEKDE KIQKHLQDSL
ADLKSLYNEW GCTNYINLGS FLIKPVQRVM RYPLLLMELL NSTPESHPDK VPLTNAVLAV
KEINVNINEY KRRKDLVLKY RKGDEDSLME KISKLNIHSI IKKSNRVSSH LKHLTGFAPQ
IKDEVFEETE KNFRMQERLI KSFIRDLSLY LQHIRESACV KVVAAVSMWD VCMEKGHRDL
EQFEKVHRYI SDQLFTNFKE RTERLVISPL NQLLNMFTGP HKLVQKRFDK LLDFYNCTER
AEKLKDKKTL EELQSARNNY EALNAQLLDE LPKFHQYAQG LFSNCVHGYA EAHCDFVRQA
LEQLKPLLSL LKVTGREGNL IAVFHEEHSR VLQQLQVFTF FPESLPATKR SFERKTMDRQ
STRKPLLGLP SYMLQSEELR ASLLARYPPE KLFQAERNFN AAQDLDVSLL EGDLVGVIKK
KDPMGSQNRW LIDNGGYKAA RMTELRLSAS TRNPCGILNK IDLYCIYSYT IYLPPGSVGL
HSNRLLLRHP FGFQLLTLLK LTDLQSLLRE F
//
