DNMBP_DANRE
ID DNMBP_DANRE Reviewed; 1673 AA.
AC E7F1U2;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Dynamin-binding protein {ECO:0000250|UniProtKB:Q6XZF7};
DE AltName: Full=Scaffold protein Tuba {ECO:0000250|UniProtKB:Q6XZF7};
GN Name=dnmbp;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=26895965; DOI=10.1074/jbc.m115.688663;
RA Baek J.I., Kwon S.H., Zuo X., Choi S.Y., Kim S.H., Lipschutz J.H.;
RT "Dynamin binding protein (Tuba) deficiency inhibits ciliogenesis and
RT nephrogenesis in vitro and in vivo.";
RL J. Biol. Chem. 291:8632-8643(2016).
CC -!- FUNCTION: Plays a critical role as a guanine nucleotide exchange factor
CC (GEF) for CDC42 in several intracellular processes associated with the
CC actin and microtubule cytoskeleton (By similarity) (PubMed:26895965).
CC Plays a central role in renal ciliogenesis and kidney development
CC (PubMed:26895965). {ECO:0000250|UniProtKB:Q6XZF7,
CC ECO:0000269|PubMed:26895965}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6XZF7}. Golgi
CC apparatus, Golgi stack {ECO:0000250|UniProtKB:Q6TXD4}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q6TXD4}. Synapse
CC {ECO:0000250|UniProtKB:M0R4F8}. Cell junction
CC {ECO:0000250|UniProtKB:Q6XZF7}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 1 dpf in the brain and pronephric
CC tubules. At 3 dpf, expression expanded to the eyes and neuromasts,
CC where mechanosensory hair cells exist, along the lateral line.
CC {ECO:0000269|PubMed:26895965}.
CC -!- DISRUPTION PHENOTYPE: The morphants contained multiple phenotypic
CC defects, beginning with a downward-curled tail at 2 dpf. Additional
CC ciliary defects after 3 dpf included small eyes, pericardial edema and
CC hydrocephalus. These defects became more severe, leading to abdominal
CC fluid accumulation, as well as abnormal pronephric kidneys at 5 dpf.
CC {ECO:0000269|PubMed:26895965}.
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DR EMBL; CR352342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001921555.3; XM_001921520.5.
DR AlphaFoldDB; E7F1U2; -.
DR SMR; E7F1U2; -.
DR STRING; 7955.ENSDARP00000127379; -.
DR PaxDb; E7F1U2; -.
DR PeptideAtlas; E7F1U2; -.
DR Ensembl; ENSDART00000153129; ENSDARP00000127379; ENSDARG00000074121.
DR GeneID; 100005174; -.
DR KEGG; dre:100005174; -.
DR CTD; 23268; -.
DR ZFIN; ZDB-GENE-101026-2; dnmbp.
DR eggNOG; KOG3519; Eukaryota.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00950000183088; -.
DR HOGENOM; CLU_252350_0_0_1; -.
DR InParanoid; E7F1U2; -.
DR OMA; YCGNHEA; -.
DR OrthoDB; 207472at2759; -.
DR PhylomeDB; E7F1U2; -.
DR TreeFam; TF330015; -.
DR Reactome; R-DRE-9013148; CDC42 GTPase cycle.
DR PRO; PR:E7F1U2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000074121; Expressed in retina and 28 other tissues.
DR ExpressionAtlas; E7F1U2; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; IMP:ZFIN.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11798; SH3_DNMBP_C1; 1.
DR CDD; cd11794; SH3_DNMBP_N1; 1.
DR CDD; cd11796; SH3_DNMBP_N3; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
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; IPR035469; DNMBP.
DR InterPro; IPR035820; DNMBP_SH3_C1.
DR InterPro; IPR035817; DNMBP_SH3_N1.
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; PTHR22834:SF19; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF07653; SH3_2; 2.
DR Pfam; PF14604; SH3_9; 3.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 6.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 6.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 6.
PE 2: Evidence at transcript level;
KW Cell junction; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Golgi apparatus; Guanine-nucleotide releasing factor;
KW Reference proteome; SH3 domain; Synapse.
FT CHAIN 1..1673
FT /note="Dynamin-binding protein"
FT /id="PRO_0000446667"
FT DOMAIN 2..61
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 66..127
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 146..205
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 244..303
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 783..970
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1011..1220
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 1288..1351
FT /note="SH3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1516..1579
FT /note="SH3 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 209..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 743..797
FT /evidence="ECO:0000255"
FT COMPBIAS 234..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1673 AA; 191172 MW; 1CB6475A9FF732EA CRC64;
MEAGSVVRAV FEFLPSVSEE LPLFTGDVIE VLSVVDEFWL LGNKDGVTGQ FPTTFVESVT
IPGTKAGENL YVCINDFNSA EAGNLPLKRG DVVAAESSMD SVWMRGHNAW GSRGLFPVSC
IKELELSGRS RQLSERSAAV QASELPPHAL GQARALMNLH AQLDEELDFR EGDVITIIGL
PEPGWFQGEL DNRTGLFPEG FVELLGPLRS PLEEPEPQTL EQYPDYSNED EERRAEEEKD
EEPPEMEIQQ CQEDEEEEEG AIYGIALYEF RALEPGELDF DVGDRIRILA SMDDGWLEGQ
IHSRRGVFPH RFVKIEGQLQ TVPQTETLIN EISVPKREEE CYTPDYTSAE EDHTVPEYGQ
ELSIQQDHTV WDLDYFERRE EEQKENNGHN VHSDQSSQER RMTQNQSQVQ PQERRRDRPP
PPQTQPNRGS SSAHRSVQIN RRSSPNMGRP QLPPRPSLHA LSNRKYSTGS HASLRQPPPA
PITMNQSLNP PNKTSPNSTW TRNNGKYASY NSRNPLSSKS SGEKNRQKKL TRHASVNDAD
IISGGSSEQQ AWPQVQGSNG FPTSQTMGTL ALSAKDLEAK LSQQLIEFEK SLPSHSNEAT
EQSRWEEVSG RLGNKVSRHF SIMDYSDEND IIRGSSHSSI ERLLPSTSSP SGSASSSLER
RKNLRPPPPR PRVLRPPAPT NTHWSQTNGR ITPQPYRPAR PAPRPPPPCP HTNAVTPPTT
SNPFYNSPDE EEIVEEMEEP EDVLEAEKEM EREQEQYRLL LRLEEVEREI DMYSNTAQEL
QAMLDEEQDE TSRQQALENL EFCSYTMETL TLEQQQLQEM TLLASQPKSL ESSPASAANS
EDPELRMLEK RTKVIEELLQ TEHDYIKDLQ MCVKEIIQPL QKKQVQGIDF DGLFGNISSV
IDLSRRLNKT LQDTDSIGQV FLSYKDQLED VYKIYCQNHD DAISLLETYE KDENIQKHVL
ECLEKLRGIY REWGKTNYIN LGSFLIKPVQ RVMRYPLLLM ELLNTTPESH HDRQQLSEAV
MSIKEINVNI NEYKRRKDLV VKYRKGDEDR LIDKISKLSM HSIIKKSNRV SSHLKHLTGI
SPQIKDEAFD DAEKRFRLQE RLIKSFIRNI SLYLQHIRES ASVKVLAAIS FCDIYTERQQ
QMDPERFQRA HRCISDKQFT EFKERTEALV ITPLTQLLNM FTGPHKLIQK RRDKLLDYDN
CKERAERLKD KRVQEELQTA RNNYEALNAQ LLDELPKFHR AAEDLFTSCV RGFVQAQRDF
ISLTLGELTP LLQLSGLGGT EGNLVSLFQE EHTRVLDLLQ SFSFFPENLP TTVRKTFEKK
TLEKQYTKKP QAPPNYVLQT DEHRAGLLVR YGPENLYQAE RNFNAAQDLD VSVLEGDIVG
VIKQQDPMGS QNRWLIDNGV TKGFVYSSFL KPYNPRRSQS DVSIESQSSN ESGYGGSSPM
FSRQNSNSTL TFNQETSTVS FTTATTQNQS NTRPNNESTP RKIRETSSNQ RDSLEPGFRN
SPNHKEVSET AIRNSREYSE PSHRSSTNHR DSVDSDQNTP TNSRDRLDLS ETDSSSSRNS
RYEPSSRYQD SKASYGSHQR QNGDYSGQQR RPQYTPEEYI EPEPEPEIDG HQIYYALYSF
SARCANELSI SANQRVRILE FQDMNGNQEW WLGEAGGRRG YVPSNYIRKS EYT
