DNMBP_RAT
ID DNMBP_RAT Reviewed; 1577 AA.
AC M0R4F8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Dynamin-binding protein {ECO:0000250|UniProtKB:Q6XZF7};
DE AltName: Full=Scaffold protein Tuba {ECO:0000305|PubMed:14506234};
GN Name=Dnmbp {ECO:0000312|RGD:1583840};
GN Synonyms=Tuba {ECO:0000303|PubMed:14506234};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH DNM1.
RX PubMed=14506234; DOI=10.1074/jbc.m308104200;
RA Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT domains, links dynamin to regulation of the actin cytoskeleton.";
RL J. Biol. Chem. 278:49031-49043(2003).
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 (By similarity). Plays a role in ciliogenesis (By
CC similarity). May play a role in membrane trafficking between the cell
CC surface and the Golgi (PubMed:14506234). {ECO:0000250|UniProtKB:E2RP94,
CC ECO:0000250|UniProtKB:Q6XZF7, ECO:0000269|PubMed:14506234}.
CC -!- SUBUNIT: Binds DNM1 via its N-terminal SH3 domains (PubMed:14506234).
CC The C-terminal SH3 domain binds a complex containing actin, tubulin,
CC Hsp70 and actin-regulatory proteins, such as ENAH, EVL, WIRE, CR16,
CC WAVE1 and NAP1L1 (By similarity). Interacts with FASLG. Interacts (via
CC SH3 domain 6) with WASL. Interacts (via SH3 domain 6) interacts with
CC ENAH. Interacts (via C-terminal domain) with TJP1; required for the
CC apical cell-cell junction localization of DNMBP (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q6TXD4,
CC ECO:0000250|UniProtKB:Q6XZF7, ECO:0000269|PubMed:14506234}.
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:0000269|PubMed:14506234}. Cell junction
CC {ECO:0000250|UniProtKB:Q6XZF7}. Note=Localizes to the apical junction,
CC colocalizes with TJP1. {ECO:0000250|UniProtKB:Q6XZF7}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15057822}.
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DR EMBL; AC096315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006223824.1; XM_006223762.3.
DR RefSeq; XP_006231632.1; XM_006231570.3.
DR AlphaFoldDB; M0R4F8; -.
DR SMR; M0R4F8; -.
DR STRING; 10116.ENSRNOP00000064242; -.
DR PaxDb; M0R4F8; -.
DR GeneID; 309362; -.
DR CTD; 23268; -.
DR RGD; 1583840; Dnmbp.
DR VEuPathDB; HostDB:ENSRNOG00000050742; -.
DR eggNOG; KOG3519; Eukaryota.
DR eggNOG; KOG4225; Eukaryota.
DR HOGENOM; CLU_252350_0_0_1; -.
DR InParanoid; M0R4F8; -.
DR OMA; YCGNHEA; -.
DR OrthoDB; 207472at2759; -.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR PRO; PR:M0R4F8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000050742; Expressed in jejunum and 19 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; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
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; PF07653; SH3_2; 1.
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 1: Evidence at protein level;
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..1577
FT /note="Dynamin-binding protein"
FT /id="PRO_0000446666"
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 784..967
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1008..1217
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 1285..1348
FT /note="SH3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1513..1576
FT /note="SH3 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 209..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 705..755
FT /evidence="ECO:0000255"
FT COMPBIAS 224..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..655
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1467
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 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6XZF7"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6XZF7"
SQ SEQUENCE 1577 AA; 176726 MW; B363A6495244A6C5 CRC64;
MEPGSVVRAI FDFCPSVSEE LPLFVGDVIE VLTVVDEFWL LGKKEDVTGQ FPSSFVEIVT
IPSLKEGERL FVCTCDFISR EPNSLSLHRG DLVIIDGTPT AGWLQGRSSL GARGFFPSSC
IHELCLSSQS RQWHSQNMLL QVPEYSMGQA RALMGLSAQL DEELDFREGD VITIIGVPEP
GWFEGELEGR RGIFPEGFVE LLGPLRTADE SVNAGSGDDS TLNDEVDVSP EEVESEGDED
DQQAGTYGIA LYRFQALESN ELDFEVGDKI RILGTLEDGW LEGRLKGKTG IFPHRFVKLC
PSNRSEETMA LPQGDSFPKN SESSAGEMGD SVVEEARQDP QECEEETPDS GLPEQTSEEP
LDHVAPECVV DKISGQDEDA SGSSPDVDLE GPRAEDPSTP DLSQEVNGIS SLPPQVPLQP
EEEKSQHYLT AGGSRQCPDT FSKLFPLEAK TRNYSSLPPR RTYTQGWSLQ KPAPHLHRAS
SLTASRVNRP GHFSHTAMAS CAQKHQTSAE NAASLCCAPE RPKRRPGLPD KEPATEITPA
SQGDNLDLDS KLTQQLIEFE KSLSGPSTEP KKIVRRFSIM DFYSEKDIVR GSSNSLPSRN
FPERRKALRP PPPRPHTPTS TSPHLLVDQS PKPGPPLVVR PSRPAPLPPP TQQRLNTASP
KPTSCALPGW EAPEKEGSEY TEKSPAQLFP CPSVLARIQD VEHDLDMHTR AQEELNLLLE
EKQDESLRAE TLETLKSYES TIQSLNLELQ QLREMTLLSS QSSSLAAPSG SVSTEKPEQR
MLEKRAKVVA ELLQTEKDYI RDLEMCVERV MVPLQQAQVP NIDFEGLFGN MQTVIKVSKQ
LLAALEITDA VGPVFLDHRD ELEGTYRLYC QNHDEAISLL DIYEKDERIQ KHLQDYLADL
KSLYHEWGCT NYINLGSFLI KPVQRIMRYP LLLMELLNST PESHPDKAPL TSAVLAIKEI
NANINEYKRR KDLVLKYRKA DEDSLMEKIS KLNIHSIIKK SSRVSSHLKH LTGFAPQLKD
EAFEETEKNF RMQERLIKSF IRDLSLYLQH IRESACVKVV AAMSIWDLCM ERGHHDLEQF
EKVHRYISDQ LFTRFKERTE RLVINPLNQL LNMFTGPYKL VQKRFDKLLD FYNCTERAEK
LKDKKTLEDL QSARNNYEAL NSQLLDELPK FQQYAQSLFT NCIHGYAEAH CDFVQKALEQ
LQPLLSLLKA SDREGNLIAI FHEEHSRVLQ QLQVFTFFPE ALPAPRKPFE RKTTDRQSSR
KALLGMPSYM LQSEELRSSL LARYPPEKLF HVQRNFNAAQ DLDVSLLEGD LVGVIKKKDP
MGSQNRWLVD NGVTKGFVYS SFLKPYNPRC SHSDSSVVSH SSTESEHSGS SPSFHRQNSS
SALTFNSNSM TVSFTSGLPQ KQPQDTSPLR ECVPETLGVS SNTGNPETGP SPCPSDPGFS
CQRRPGNPAD GTREISQPAS TLRGCQRRSL HSEVLGYPVP GRSDQGSDSI KGTSRACQTA
GDRDRGLGSS EAEGNQVYFA IYTFKARNPN ELTVLANQRL RILEFKDVTG NTEWWLAEVN
GKKGYVPSNY IRKTEYT
