DIAP1_RAT
ID DIAP1_RAT Reviewed; 1265 AA.
AC F1M775;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein diaphanous homolog 1;
DE AltName: Full=Diaphanous-related formin-1;
DE Short=DRF1;
DE AltName: Full=mDIA1 {ECO:0000303|PubMed:18651670};
GN Name=Diaph1 {ECO:0000312|RGD:1310707}; Synonyms=Diap1;
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 TISSUE SPECIFICITY.
RX PubMed=18651670; DOI=10.1002/dvdy.21622;
RA Mironova E., Millette C.F.;
RT "Expression of the diaphanous-related formin proteins mDia1 and mDia2 in
RT the rat testis.";
RL Dev. Dyn. 237:2170-2176(2008).
CC -!- FUNCTION: Actin nucleation and elongation factor required for the
CC assembly of F-actin structures, such as actin cables and stress fibers.
CC Binds to the barbed end of the actin filament and slows down actin
CC polymerization and depolymerization. Required for cytokinesis, and
CC transcriptional activation of the serum response factor. DFR proteins
CC couple Rho and Src tyrosine kinase during signaling and the regulation
CC of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC
CC to stabilize microtubules and promote cell migration. Has neurite
CC outgrowth promoting activity. Acts in a Rho-dependent manner to recruit
CC PFY1 to the membrane (By similarity). The MEMO1-RHOA-DIAPH1 signaling
CC pathway plays an important role in ERBB2-dependent stabilization of
CC microtubules at the cell cortex. It controls the localization of APC
CC and CLASP2 to the cell membrane, via the regulation of GSK3B activity.
CC In turn, membrane-bound APC allows the localization of the MACF1 to the
CC cell membrane, which is required for microtubule capture and
CC stabilization. Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the control of cell shape (By
CC similarity). Also acts as an actin nucleation and elongation factor in
CC the nucleus by promoting nuclear actin polymerization inside the
CC nucleus to drive serum-dependent SRF-MRTFA activity (By similarity).
CC {ECO:0000250|UniProtKB:O08808, ECO:0000250|UniProtKB:O60610}.
CC -!- SUBUNIT: Homodimer. Interacts with the GTP-bound form of RHOA.
CC Interacts with RHOC, PFY1, MAPRE1, BAIAP2 and APC. Interacts with SCAI
CC (By similarity). Interacts with DCAF7, via FH2 domain (By similarity).
CC Interacts with NCDN (By similarity). Interacts with OSBPL10, OSBPL2,
CC VIM, TUBB and DYN1 (By similarity). {ECO:0000250|UniProtKB:O08808,
CC ECO:0000250|UniProtKB:O60610}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08808}.
CC Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O08808}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O08808}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:O60610}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:O60610}. Cytoplasm
CC {ECO:0000250|UniProtKB:O08808}. Nucleus {ECO:0000250|UniProtKB:O08808}.
CC Note=Membrane ruffles, especially at the tip of ruffles, of motile
CC cells. {ECO:0000250|UniProtKB:O08808}.
CC -!- TISSUE SPECIFICITY: Expressed in testis (PubMed:18651670). Present in
CC Sertoli cells (at protein level) (PubMed:18651670).
CC {ECO:0000269|PubMed:18651670}.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the GBD/FH3 domain. This autoinhibition is released
CC upon competitive binding of an activated GTPase. The release of DAD
CC allows the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments. {ECO:0000250|UniProtKB:O08808}.
CC -!- PTM: Phosphorylation at Thr-761 is stimulated by cAMP and regulates
CC stability, complex formation and mitochondrial movement (By
CC similarity). {ECO:0000250|UniProtKB:O60610}.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000305}.
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; AABR07031736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07031737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07031738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR IntAct; F1M775; 2.
DR STRING; 10116.ENSRNOP00000057176; -.
DR jPOST; F1M775; -.
DR PaxDb; F1M775; -.
DR PeptideAtlas; F1M775; -.
DR PRIDE; F1M775; -.
DR UCSC; RGD:1310707; rat.
DR RGD; 1310707; Diaph1.
DR VEuPathDB; HostDB:ENSRNOG00000019688; -.
DR eggNOG; KOG1924; Eukaryota.
DR HOGENOM; CLU_002356_0_0_1; -.
DR InParanoid; F1M775; -.
DR OMA; EKMSIFV; -.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:F1M775; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000019688; Expressed in lung and 19 other tissues.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005522; F:profilin binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0071420; P:cellular response to histamine; ISO:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0035372; P:protein localization to microtubule; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:RGD.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISO:RGD.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR Gene3D; 1.10.20.40; -; 1.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR044933; DIA_GBD_sf.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR027653; Formin_Diaph1.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45691:SF4; PTHR45691:SF4; 2.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Hearing; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1265
FT /note="Protein diaphanous homolog 1"
FT /id="PRO_0000445557"
FT DOMAIN 84..449
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 625..757
FT /note="FH1"
FT /evidence="ECO:0000255"
FT DOMAIN 762..1164
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1187..1215
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 474..568
FT /evidence="ECO:0000255"
FT COILED 1141..1185
FT /evidence="ECO:0000255"
FT COMPBIAS 12..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..746
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 761
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 1050
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 1096
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 1114
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O08808"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
SQ SEQUENCE 1265 AA; 140410 MW; 552D8D90F2FE5E0D CRC64;
MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFT LKRLMADELE RFTSMRIKKE
KEKPNSAHRN SSASYGDDPT AQSLQDISDD QVLVLFEQML VDMNLNEEKQ QPLREKDIVI
KREMVSQYLH TSKAGMNQKE SSRSAMMYIQ ELRSGLRDMH LLSCLESLRV SLNNNPVSWV
QTFGAEGLAS LLDILKRLHD EKEETSGNYD SRNQHEIIRC LKAFMNNKFG IKTMLETEEG
ILLLVRAMDP AVPNMMIDAA KLLSALCILP QPEDMNERVL EAMTERAEME EVERFQPLLD
GLKSGTSIAL KVGCLQLINA LITPAEELDF RVHIRSELMR LGLHQVLQEL REIDNDDMRV
QLNVFDEQGD EDFFDLKGRL DDIRMEMDDF GEVFQIILNT VKDSKAEPHF LSILQHLLLV
RNDYEARPQY YKLIEECVSQ IVLHKNGTDP DFKCRHLQID IEGLVDQMID KTKVEKSEAK
ATELEKKLDS ELTARHELQV EMKKMENDFE QKLQDLQGEK DALDSEKQQI TTQKQDLEAE
VSKLTGEVAK LSKELEDAKK EMASLSAVAV APSVSSSAAV PQAPPLPGTS GTVIPPPPPP
PLPGGAVPPP PPPPLPAGTG IPPPPPLPGG ACISSSPQLF GSTAIPPPPP LPGATAIPPP
PPLPGDTAIP PPPPLPGXTA IPPPPPLPGA TGVPPPPPPL PGSVGVPPPP PLPGGPGLPP
PPPPFPGAPG IPPPPPGMGV PPPPPFGFGI PAAPVLPFGL TPKKVYKPEV QLRRPNWSKF
VAEDLSQDCF WTKVKEDRFE NNELFAKLTL AFSAQTKTSL AKKDQEGGEE KKSVQKKKVK
ELKVLDSKTA QNLSIFLGSF RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML
SELKEEYDDL AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL
RKSENFSSLL ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM TLLHFLAELC
ETDHPDVLKF PDELAHVEKA SRVSAENLQK NLDQMKKQIA DVERDVQNFP AATDEKDKFV
EKMTSFVKDA QEQYNKLRMM HSNMETLYKE LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ
AVKENQKRRE TEEKMRRAKL AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ
SGAAFRRKRG PRQVNRKAGC AVTSLLASEL TKDDAVAASS AKVPKKSEGV TTILEEAKEL
VGRAS
