ID A0A0D9R043_CHLSB Unreviewed; 1576 AA.
AC A0A0D9R043;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:ENSCSAP00000001982.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000001982.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000001982.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000001982.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AQIB01042667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01042668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01042669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007962013.1; XM_007963822.1.
DR STRING; 60711.ENSCSAP00000001982; -.
DR Ensembl; ENSCSAT00000003706.1; ENSCSAP00000001982.1; ENSCSAG00000005674.1.
DR GeneID; 103216378; -.
DR KEGG; csab:103216378; -.
DR CTD; 23268; -.
DR eggNOG; KOG3519; Eukaryota.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00950000183088; -.
DR OMA; YCGNHEA; -.
DR OrthoDB; 25601at2759; -.
DR BioGRID-ORCS; 103216378; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 9.
DR Bgee; ENSCSAG00000005674; Expressed in adrenal cortex and 7 other cell types or tissues.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
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; 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; 2.
DR Pfam; PF07653; SH3_2; 2.
DR Pfam; PF14604; SH3_9; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000029965};
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 243..302
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 783..966
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1007..1216
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 1284..1347
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1512..1575
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 357..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 697..754
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 399..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 176757 MW; EC327F80526B389A CRC64;
MEAGSVVRAI FDFCPSVSEE LPLFVGDVIE VLAVVDEFWL LGKKEDVTGQ FPSSFVEIVT
IPSLKEGERL FVCICEFTSQ ELDSLPLHRG DLVILDGIPT AGWLQGRSCW GARGFFPSSC
VRELCLSSQS RQWHSQSALF QIPEYSMGQA RALMGLSAQL DEELDFREGD VITIIGVPEP
GWFEGELEGR RGIFPEGFVE LLGPLRTVDE SVSSGNPDDC IVNGEVDTPI GEEEIGLDED
EEEPGTYGVA LYRFQALEPN ELDFEVGDKI RILATLEDGW LEGSLKGRTG IFPYRFVKLH
PDTRVEETMA LPQEGSLSRI PETSLDYLEN SLGMEKQRHE TSDHEAEEPD CIISEAPTSP
LGHLTSECEA DRNSYQDEGT AAGPRRSPGV EWEMPLATDS PTSDPTKVVN GISSQPQVPF
HPSLQRSQYY STAGGSHPHS EQHPDLPLEA RKRDYASLPP QRMYSQLKTL QKPVLPLYRG
SSLSASGVVK PSQSSPQLHD IASYAKKHQT SSVYSVSERS EMKPGPQVQG LVMEAATHSQ
GDGSTDLDSK LTQQLIEFEK SLAGPGTEPD KILRHFSITD FNSEKDIVRG SSKLITEQEL
PERRKALRPP PPRPCTPVST SPHLLVDQNL KPAPPLVVRP SRPAPLPPSA QQRTNAVSPK
LLSRHRPTCE TLEKEGHGHM GRSLDQTSPC PLVLVRIEEM EQDLDMYSRA QEELNLMLEE
KQDESSRAET LEDLKFCESN IESLSMELQQ LREMTLLSSQ SSSLVAPSGS VSTENPEQRM
LEKRAKVVEE LLQTERDYIR DLEMCIERIM VPLQQAQVPN IDFEGLFGNM QMVIKVSKQL
LAALEISDAV GPVFLGHRDE LEGTYKIYCQ NHDEAIALLE IYEKDEKIQK HLQDSLTDLK
SLYNEWGCTN YINLGSFLIK PVQRVMRYPL LLMELLNSTP ESHPDKVPLT NAVLAVKEIN
VNINEYKRRK DLVLKYRKGD EDSLMEKISK LNIHSIIKKS NRVSSHLKHL TGFAPQIKDE
VFEETEKNFR MQERLIKSFI RDLSLYLQHI RESACVKVVA AVSMWDVCME RGHRDLEQFE
RVHRYISDQL FTNFKERTER LVISPLNQLL SMFTGPHKLV QKRFDKLLDF YNCTERAEKL
KDKKTLEELQ SARNNYEALN AQLLDELPKF HQYAQGLFTN CVHGYAEAHC DFVHQALEQL
KPLLSLLKVA GREGNLIAIF HEEHSRVLQQ LQVFTFFPES LPATKKPFER KTVDRQSARK
SLVGLPSYML QSEELRASLL ARYPPEKLFQ AERNFNAAQD LDVSLLEGDL VGVIKKKDPM
GSQNRWLIDN GVTKGFVYSS FLKPYNPRRS HSDASVGSHS STESEHGSSS PRFPRQNSGS
TLTFNPSSMA VSFTSGSCQK QPQDVSSPLK EGDQGTLSAS LNPVSSESGP SGCPSDPDST
SQPRSGDAAD VARDVNQPAA TPRSYRNFRH PEMVGYSVPG RNGQGQDLVK GCARTAQAPE
DRSAEPESSE AEGNQVYFAV YTFKARNPNE LSVSANQKLK ILEFKDVTGN TEWWLAEVNG
KKGYVPSNYI RKTEYT
//
