DNMBP_CANLF
ID DNMBP_CANLF Reviewed; 1583 AA.
AC E2RP94;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Dynamin-binding protein {ECO:0000250|UniProtKB:Q6XZF7};
DE AltName: Full=Scaffold protein Tuba {ECO:0000250|UniProtKB:Q6XZF7};
GN Name=DNMBP {ECO:0000250|UniProtKB:Q6XZF7};
GN Synonyms=TUBA {ECO:0000303|PubMed:20479467};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP FUNCTION.
RX PubMed=20479467; DOI=10.1083/jcb.201002097;
RA Qin Y., Meisen W.H., Hao Y., Macara I.G.;
RT "Tuba, a Cdc42 GEF, is required for polarized spindle orientation during
RT epithelial cyst formation.";
RL J. Cell Biol. 189:661-669(2010).
RN [3]
RP FUNCTION.
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. Regulates the structure of apical
CC junctions in epithelial cells (By similarity). Participates in the
CC normal lumenogenesis of epithelial cell cysts by regulating spindle
CC orientation (PubMed:20479467). Plays a key role in ciliogenesis and
CC cyst formation (PubMed:26895965). May play a role in membrane
CC trafficking between the cell surface and the Golgi (By similarity).
CC {ECO:0000250|UniProtKB:Q6TXD4, ECO:0000250|UniProtKB:Q6XZF7,
CC ECO:0000269|PubMed:20479467, ECO:0000269|PubMed:26895965}.
CC -!- SUBUNIT: Binds DNM1 via its N-terminal SH3 domains. The C-terminal SH3
CC domain binds a complex containing actin, tubulin, Hsp70 and actin-
CC regulatory proteins, such as ENAH, EVL, WIRE, CR16, WAVE1 and NAP1L1
CC (By similarity). Interacts with FASLG. Interacts (via SH3 domain 6)
CC with WASL. Interacts (via SH3 domain 6) interacts with ENAH. Interacts
CC (via C-terminal domain) with TJP1; required for the apical cell-cell
CC junction localization of DNMBP (By similarity).
CC {ECO:0000250|UniProtKB:Q6TXD4, ECO:0000250|UniProtKB:Q6XZF7}.
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}. Note=Localizes to the apical junction,
CC colocalizes with TJP1. {ECO:0000250|UniProtKB:Q6XZF7}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAEX03015466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_534988.2; XM_534988.4.
DR AlphaFoldDB; E2RP94; -.
DR SMR; E2RP94; -.
DR STRING; 9615.ENSCAFP00000044264; -.
DR PaxDb; E2RP94; -.
DR GeneID; 477794; -.
DR CTD; 23268; -.
DR eggNOG; KOG3519; Eukaryota.
DR eggNOG; KOG4225; Eukaryota.
DR HOGENOM; CLU_252350_0_0_1; -.
DR InParanoid; E2RP94; -.
DR OMA; YCGNHEA; -.
DR OrthoDB; 207472at2759; -.
DR TreeFam; TF330015; -.
DR Reactome; R-CFA-9013148; CDC42 GTPase cycle.
DR Proteomes; UP000002254; Chromosome 28.
DR Bgee; ENSCAFG00000009561; Expressed in mucosa of urinary bladder and 47 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11798; SH3_DNMBP_C1; 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; -; 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; 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; PTHR22834:SF19; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF14604; SH3_9; 1.
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 3: Inferred from homology;
KW Acetylation; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Guanine-nucleotide releasing factor; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Synapse.
FT CHAIN 1..1583
FT /note="Dynamin-binding protein"
FT /id="PRO_0000446665"
FT DOMAIN 2..61
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 66..126
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 145..204
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 243..302
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 791..974
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1015..1224
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 1292..1355
FT /note="SH3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1519..1582
FT /note="SH3 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 217..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 742..762
FT /evidence="ECO:0000255"
FT COMPBIAS 405..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6XZF7"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6XZF7"
SQ SEQUENCE 1583 AA; 178015 MW; 6F6BF8CC9DA9CE7C CRC64;
MEAGSVVRAI FDFCPSVSEE LPLFVGDIIE VLAVVDEFWL LGKKEDVTGQ FPSSFVEIVT
IPSLKEGERL FVCISEFTSQ ELNSLPLHRG DLVILDDAPT ASWLQGRSCW GARGFFPSSC
VRELCLSSQS RRWHSQSALL QIPEYSMGQA RALMGLSAQL DEELDFREGD VITIIGVPEP
GWFEGELEGR RGIFPEGFVE LLGPLRTVDE LVSSGNHNDC IINGEEETPT GEEERGPEED
EEQPGTYGIA LYRFQALEPN ELDFEVGDKI RILGTLEDGW LEGSLKGRTG IFPYRFVKLF
SKTRAEETMD LPKESSPTEI PDTSLDCREN PLVVEGRHKS PEYKAEKSNC VISETSASPL
EHLTSECEVH KSSHQDEGTS RGPPRSPGWG HEQPLARHSP AEDPSETING VSSQSQVPFR
PRWQQNQYYS TTGRGHLSTE QYSDPLPLEA KAKDYSSRPP RGMYSPPKTF QKPVPSPHGS
SCPLAPRVVR PSLLSSQLQS MVRGAKKYHT PKENASSFCS ASERSEVKAG LQDRAFTADL
IALGQGGGHT DLDSKLTQQL VEFEKSLSGP GAEPEAILRH FSIMNFNSEK DIVRGSSKSI
TPQELPERRR ALRPPPPRPS TPASTSPHVL LDQNLKPEPP LAMRPSRPAP LPPSAQHRVT
AVTPGLLTPG LFTHESCESP EKEGPENLDQ TLDQTSQCPL VLVRIQEMEQ DLDMCSPAPE
EPNLTLEEKQ DESLRAETPE DLEFYESNIE SLNMELQQLR EMTLLSSQSS SPVAPPGSMY
TENPEQRMLE KRAKVIEELL QTERDYVRDL EMCIEHIMAP LQQTQIPNID FEGLFGNMQM
VIKVSKQLLA DLEISDAVGP VFLDHRDELE GTYKVYCQNH DEAISLLEIY EKDEKIQKHL
QDSLADLKSL YTEWGCTNYI NLGSFLIKPV QRVMRYPLLL MELLNSTPES HPDKAPLTSA
VLAVKEINVN INEYKRRKDL VLKYRKGDED SLMEKISKLN IHSIIKKSNR VSSHLKHLTG
FAPQIKDEAF EETEKNFRMQ ERLIKSFIRD LSLYLQHIRE SACVKVVAAV SMWDVCMEKG
HRDLEQFEKV HRYISDQLFT NFKERTERLV ISPLNQLLSM FTGPHKLVQK RFDKLLDFYN
CTERAEKLKD KKTLEELQSA RNNYEALNAQ LLDELPKFHQ YAQGLFTNCI HGYAEAHCDF
VRQALEQLKP LLSLLKVAGR EGNLIAIFHE EHSRVLQQLQ VFTFFPESLP AARKPFERKT
LDRQSARKPL LGLPSYMLQS EELRASLLTR YPPEKLFQAE RNFNAAQDLD VSLLEGDLVG
VIKKKDPMGS QNRWLIDNGV SQGFVYSSFL KPYNTRRSHS DVSVGSHSST ESEQSSSSPR
FPRQNSSGTL TFNPGSMAVS FTSGSCQKQP QDATSPKELG QEILSASSNL GCSESSPSRC
PSDPDSSPQP RSWDSPEAAR DISQPAPALR GYRNSRHPEI GGYSLPGRNG QGKDLTKGCA
RTTQALEDKN EEPESREAEG NQVYFAVYTF KARNPNELSV SANQRLKILE FKDVTGNTEW
WLAEVNGKKG YVPSNYIRKA EYT
