DIAP3_RAT
ID DIAP3_RAT Reviewed; 1172 AA.
AC F1LVW7; A0A0G2K8Y4;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 4.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein diaphanous homolog 3;
DE AltName: Full=Diaphanous-related formin-3;
DE Short=DRF3;
DE AltName: Full=mDIA2 {ECO:0000303|PubMed:18651670};
GN Name=Diaph3 {ECO:0000312|RGD:1593287};
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, AND 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 Required for cytokinesis, stress fiber formation and transcriptional
CC activation of the serum response factor. Binds to GTP-bound form of Rho
CC and to profilin: acts in a Rho-dependent manner to recruit profilin to
CC the membrane, where it promotes actin polymerization. DFR proteins
CC couple Rho and Src tyrosine kinase during signaling and the regulation
CC of actin dynamics. Also acts as an actin nucleation and elongation
CC factor in the nucleus by promoting nuclear actin polymerization inside
CC the nucleus to drive serum-dependent SRF-MRTFA activity.
CC {ECO:0000250|UniProtKB:Q9Z207}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18651670}. Nucleus
CC {ECO:0000269|PubMed:18651670}. Note=During mitosis, co-localizes with
CC the actin-rich cleavage furrow and with the microtubule-rich central
CC spindle during cytokinesis (By similarity). Shuttles between the
CC cytoplasm and the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:Q9NSV4, ECO:0000250|UniProtKB:Q9Z207}.
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:Q9Z207}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9Z207}.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000305}.
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DR EMBL; AABR07018707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07018708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07018709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07018710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07018711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07018712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07018713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001292101.1; NM_001305172.1.
DR AlphaFoldDB; F1LVW7; -.
DR SMR; F1LVW7; -.
DR STRING; 10116.ENSRNOP00000012167; -.
DR jPOST; F1LVW7; -.
DR PaxDb; F1LVW7; -.
DR PeptideAtlas; F1LVW7; -.
DR PRIDE; F1LVW7; -.
DR GeneID; 290396; -.
DR KEGG; rno:290396; -.
DR CTD; 81624; -.
DR RGD; 1593287; Diaph3.
DR eggNOG; KOG1924; Eukaryota.
DR HOGENOM; CLU_002356_0_0_1; -.
DR InParanoid; F1LVW7; -.
DR OrthoDB; 1204639at2759; -.
DR TreeFam; TF315383; -.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
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-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:F1LVW7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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; IPR027654; Formin_DIAPH3.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45691:SF9; PTHR45691:SF9; 1.
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 Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..1172
FT /note="Protein diaphanous homolog 3"
FT /id="PRO_0000445558"
FT DOMAIN 94..456
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 541..611
FT /note="FH1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z207"
FT DOMAIN 616..1014
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1037..1067
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 493..530
FT /evidence="ECO:0000255"
FT MOTIF 16..39
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9Z207"
FT MOTIF 1163..1172
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9Z207"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..586
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSV4"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSV4"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSV4"
FT MOD_RES 1073
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSV4"
FT MOD_RES 1158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSV4"
SQ SEQUENCE 1172 AA; 133833 MW; E672A885D920DE5D CRC64;
MEKHRARALG RDSKASRRKG LPSAPPAGPY ELGEKRPKLH LNIRTLTDDM LDKFASIRIP
KGSKKERPPL PQLKTVSGSS DYSSVSSETM ENNPKSLSEN EVLKLFEKMM EDMNLNEDKK
APLREKDFSI KKEMVMQYIN TASKTGSLRS SRQISPQEFI HELKMGYTGE RLFTYLESLR
VSLTSNPVSW VQNFGHEGLG LLLDILEKLI NGQIQEKVVK KTQHKVIQCL RALMNTQYGL
ERIMSDERSL SLLAKAMDPK QPSMMADVVK LLSAVCIVGE ESILEEVLEA LTSAGEERKI
DRFFSIVEGL RHNSVQLQVA CMQLINALVT SPDDLDFRLH LRNEFMRCGL KEILPNLKGI
KNDGLDIQLK VFDEHKEEDL SEFSHRFEDI RAEFDEASDV YSVVWDTVKE TRAEGHFVSI
LQHLLLIRND RFIRQQYFKL IDECVSQIVL HRDGIDPDFT YRKRLDLDLS QFVDVCIDQA
KLEEWEEKAS EHCKKFEKEC TDHQETQAQL QKKEAKINEL QAELQAFKSQ FGALPPGTKI
PLQTSAKGEP GPSAFPPAPP ALGAGVPPPP PPPPPPPPPL PGMAMPFGGP VPPPPPLGFL
GGQNFIPLNL PFGLKPKKEF KPEISMRRLN WLKIGPNEMS ENCFWIKVNE NKYENKDLLC
KLENTFCCLE KEKRDTNDFD EKKVIKKRMK ELKFLDPKIA QNLSIFLSSF RVPYEKIRTM
ILEVDEAQLS ESMIQNLMKH LPDEEQLKSL SQFRSDYNSL CEPEQFAVVM SNVKRLRPRL
TAILFKLQFE EQVNNINPDI MAVSTACEEI KKSKSFSKLL ELVLLMGNYM NAGSRNAQTF
GFDLSSLCKL KDTKSADQKT TLLHFLVDVC EEKHPDILPF VDDLAHLDKA SRVSVEMLEK
SLKQMGRQLL QLEKNLETFP PPEDLHDKFV IKMSSFIITA KEHYGKLSTL LDNMTQLYQS
VMSYYAVDTK KVSVEEFFND LNNFRTSFMQ ALKENIRKRE AAEKEKRARI AKERAEKERL
ERQQEKKRLL EMKTEGDETG VMDSLLEALQ SGAAFRDRRK RTPKLKDIRQ SLSPMSQRPV
LKVCNHENQK MQLSEGSRPH HSINCTSTRT PVAKELNCNL DTHTSTGRIK AVEKEACNAE
SNRKKEMELL GSVSKSESVP EVEALLARLR AL
