ID A0A452SGV1_URSAM Unreviewed; 865 AA.
AC A0A452SGV1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:ENSUAMP00000031780.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000031780.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000031780.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452SGV1; -.
DR Ensembl; ENSUAMT00000035439.1; ENSUAMP00000031780.1; ENSUAMG00000024205.1.
DR GeneTree; ENSGT00950000183088; -.
DR OMA; REGEKWY; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
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 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; 2.
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; 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; PF07653; SH3_2; 1.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 2.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 73..256
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 297..506
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 574..637
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 801..864
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 639..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 98250 MW; 48AC35D07100F472 CRC64;
KCLPYSKDLG VAEHSRALGR FRSACYPGTH TSSPRQRPFG TAEMTLLSSQ SSSPVAPPGS
MYTENPEQRM LEKRAKVVEE LLQTERDYIR DLEMCIEHIM VPLQQAQIPN IDFEGLFGNM
QMVIKVSKQL LADLEISDAV GPVFLDHRDE LEGTYKVYCQ NHDEAISLLE IYEKDEKIQK
HLQDSLADLK SLYTEWGCTN YINLGSFLIK PVQRVMRYPL LLMELLNSTP ESHPDKAPLT
NAVLAVKEIN VNINEYKRRK DLVLKYRKGD EDSLMEKISK LNIHSIIKKS NRVSSHLKHL
TGFAPQIKDE AFEETEKNFR MQERLIKSFI RDLSLYLQHI RESACVKVVA AVGMWDVCME
KGHRDLEQFE KVHRYISDQL FANFKERTER LVISPLNQLL SMFTGPHKLV QKRFDKLLDF
YNCTERAEKL KDKKTLEELQ SARNNYEALN AQLLDELPKF HQFAQGLFAN CVHGYAEAHC
DFVRRALEQL KPLLSLLKVA GREGNLIAIF HEEHSRVLQQ LQVFTFFPES LPAARKPFER
RTVDRQSARK PLLGLPSYML QSEELRASLL ARYPPEKLFQ AERNFNAAQD LDVSLLEGDL
VGVIKKKDPM GSQNRWLIDN GVTKGFVYSS FLKPYNARRS HSDVSVGSHS STESEPSSSS
PRFPRQNSSS ALTFNPGSMA VSFTSGSCQK QPQEATASKE LDQETLGASF NLGCSESSPS
RCPSDPDRSP QPRSWDFPEA ASALHQPAPA GGSYRNARRP ETVGCSLPAR GGQGRDLTKG
CTRTTPSLED KKEEPESREA EGNQVYFAVY TFKARNPNEL SVSANQRLKI LEFKDVTGNT
EWWLAEVNGK KGYVPSNYIR KTEYT
//
