FMNL3_MOUSE
ID FMNL3_MOUSE Reviewed; 1028 AA.
AC Q6ZPF4; Q3TCF9; Q3U2E4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Formin-like protein 3;
GN Name=Fmnl3; Synonyms=Frl2, Kiaa2014;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95; SER-174 AND SER-1014, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH SRGAP2.
RX PubMed=21148482; DOI=10.1074/jbc.m110.190397;
RA Mason F.M., Heimsath E.G., Higgs H.N., Soderling S.H.;
RT "Bi-modal regulation of a formin by srGAP2.";
RL J. Biol. Chem. 286:6577-6586(2011).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the control of cell shape and
CC migration. Required for developmental angiogenesis. In this process,
CC required for microtubule reorganization and for efficient endothelial
CC cell elongation. In quiescent endothelial cells, triggers rearrangement
CC of the actin cytoskeleton, but does not alter microtubule alignement.
CC {ECO:0000250|UniProtKB:Q6NXC0, ECO:0000250|UniProtKB:Q8IVF7}.
CC -!- SUBUNIT: Interacts with SRGAP2 (via SH3 domain).
CC {ECO:0000269|PubMed:21148482}.
CC -!- INTERACTION:
CC Q6ZPF4-1; P68135: ACTA1; Xeno; NbExp=3; IntAct=EBI-16027300, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IVF7}. Cell
CC membrane {ECO:0000250|UniProtKB:Q8IVF7}; Lipid-anchor {ECO:0000255}.
CC Note=Enriched in lamellipodia. {ECO:0000250|UniProtKB:Q8IVF7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZPF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZPF4-2; Sequence=VSP_025894, VSP_025895;
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98283.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129473; BAC98283.1; ALT_INIT; mRNA.
DR EMBL; AK155331; BAE33197.1; -; mRNA.
DR EMBL; AK170744; BAE41997.1; -; mRNA.
DR EMBL; BC131961; AAI31962.1; -; mRNA.
DR CCDS; CCDS27819.1; -. [Q6ZPF4-1]
DR CCDS; CCDS79408.1; -. [Q6ZPF4-2]
DR RefSeq; NP_001297551.1; NM_001310622.1.
DR RefSeq; NP_001297552.1; NM_001310623.1. [Q6ZPF4-2]
DR RefSeq; NP_035841.1; NM_011711.2. [Q6ZPF4-1]
DR PDB; 4EAH; X-ray; 3.40 A; A/B/C/E=555-954.
DR PDBsum; 4EAH; -.
DR AlphaFoldDB; Q6ZPF4; -.
DR SMR; Q6ZPF4; -.
DR BioGRID; 204547; 14.
DR DIP; DIP-32010N; -.
DR IntAct; Q6ZPF4; 3.
DR STRING; 10090.ENSMUSP00000085566; -.
DR iPTMnet; Q6ZPF4; -.
DR PhosphoSitePlus; Q6ZPF4; -.
DR MaxQB; Q6ZPF4; -.
DR PaxDb; Q6ZPF4; -.
DR PeptideAtlas; Q6ZPF4; -.
DR PRIDE; Q6ZPF4; -.
DR ProteomicsDB; 267486; -. [Q6ZPF4-1]
DR ProteomicsDB; 267487; -. [Q6ZPF4-2]
DR Antibodypedia; 1106; 77 antibodies from 14 providers.
DR DNASU; 22379; -.
DR Ensembl; ENSMUST00000081224; ENSMUSP00000079984; ENSMUSG00000023008. [Q6ZPF4-2]
DR Ensembl; ENSMUST00000088233; ENSMUSP00000085566; ENSMUSG00000023008. [Q6ZPF4-1]
DR GeneID; 22379; -.
DR KEGG; mmu:22379; -.
DR UCSC; uc007xpj.1; mouse. [Q6ZPF4-1]
DR UCSC; uc007xpl.1; mouse. [Q6ZPF4-2]
DR CTD; 91010; -.
DR MGI; MGI:109569; Fmnl3.
DR VEuPathDB; HostDB:ENSMUSG00000023008; -.
DR eggNOG; KOG1923; Eukaryota.
DR GeneTree; ENSGT00940000159962; -.
DR HOGENOM; CLU_003597_0_0_1; -.
DR InParanoid; Q6ZPF4; -.
DR OMA; ELANFWH; -.
DR OrthoDB; 288325at2759; -.
DR PhylomeDB; Q6ZPF4; -.
DR TreeFam; TF325155; -.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR BioGRID-ORCS; 22379; 2 hits in 57 CRISPR screens.
DR ChiTaRS; Fmnl3; mouse.
DR PRO; PR:Q6ZPF4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6ZPF4; protein.
DR Bgee; ENSMUSG00000023008; Expressed in primary oocyte and 157 other tissues.
DR ExpressionAtlas; Q6ZPF4; baseline and differential.
DR Genevisible; Q6ZPF4; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0032794; F:GTPase activating protein binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR DisProt; DP02638; -.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR027655; Fmnl3.
DR InterPro; IPR043592; FMNL_animal.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45857; PTHR45857; 1.
DR PANTHER; PTHR45857:SF3; PTHR45857:SF3; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 2.
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; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Cell membrane; Cytoplasm;
KW Developmental protein; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IVF7"
FT CHAIN 2..1028
FT /note="Formin-like protein 3"
FT /id="PRO_0000289096"
FT DOMAIN 26..472
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 561..951
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 986..1018
FT /note="DAD"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..541
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 152..202
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025894"
FT VAR_SEQ 999..1028
FT /note="VLKSVPFTARTAKRGSRFFCDAAHHDESNC -> GFNHQRMVVHSQVRSAVP
FT PSGPPRAPGPH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025895"
FT HELIX 581..584
FT /evidence="ECO:0007829|PDB:4EAH"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 603..609
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 641..654
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 658..666
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 675..683
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 688..699
FT /evidence="ECO:0007829|PDB:4EAH"
FT TURN 704..706
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 709..719
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 723..758
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 761..778
FT /evidence="ECO:0007829|PDB:4EAH"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 790..794
FT /evidence="ECO:0007829|PDB:4EAH"
FT STRAND 795..800
FT /evidence="ECO:0007829|PDB:4EAH"
FT STRAND 804..807
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 808..819
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 821..824
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 833..837
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 841..863
FT /evidence="ECO:0007829|PDB:4EAH"
FT TURN 868..870
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 871..901
FT /evidence="ECO:0007829|PDB:4EAH"
FT TURN 906..908
FT /evidence="ECO:0007829|PDB:4EAH"
FT HELIX 911..937
FT /evidence="ECO:0007829|PDB:4EAH"
SQ SEQUENCE 1028 AA; 117169 MW; BBA0436746934A3B CRC64;
MGNLESTDGG PGEPPSVPLL LPPGKTPMPE PCELEERFAL VLSSMNLPPD KARLLRQYDN
EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPNVTRKKFR RRVQESTKVL RELEISLRTN
HIGWVREFLN DENKGLDVLV DYLSFAQCSV MFDFEGLESG DDGAFDKLRS WSRSIEDLQP
PNALSAPFTN SLARSARQSV LRYSTLPGRR ALKNSRLVSQ KDDVHVCILC LRAIMNYQYG
FNLVMSHPHA VNEIALSLNN KNPRTKALVL ELLAAVCLVR GGHEIILAAF DNFKEVCKEL
HRFEKLMEYF RNEDSNIDFM VACMQFINIV VHSVEDMNFR VHLQYEFTKL GLEEFLQKSR
HTESEKLQVQ IQAYLDNVFD VGGLLEDAET KNVALEKVEE LEEHVSHLTE KLLDLENENM
MRVAELEKQL LQREKELESI KETYENTSNQ VHTLRRLIKE KEEAFQRRCH LEPSARGLES
MGGEALARVG PTELTEGIPP SDLDLLAPAP PTEETLPLPP PPAPPLPPPP PPLPDKCPPA
PPLPGAAPSV VLTVGLSAIR IKKPIKTKFR LPVFNWTALK PNQINGTVFS ELDDEKILED
LDLDRFEELF KTKAQGPALD LICSKNKTAQ KAASKVTLLE ANRAKNLAIT LRKAGRSAEE
ICRAIHTFDL QTLPVDFVEC LMRFLPTEAE VKLLRQYERE RQPLEELAAE DRFMLLFSKV
ERLTQRMAGM AFLGNFQDNL QMLTPQLNAI IAASASVKSS QKLKQMLEII LALGNYMNSS
KRGAVYGFKL QSLDLLLDTK STDRKMTLLH FIALTVKEKY PELANFWQEL HFVEKAAAVS
LENVLLDVKE LGRGMELIRR ECSIHDNSVL RNFLSTNEGK LDKLQRDAKT AEEAYNAVVR
YFGESPKTTP PSVFFPVFVR FIRSYKEAEQ ENEARKKQEE VMREKQLAQE AKKLDAKTPS
QRNKWQQQEL IAELRRRQAK EHRPVYEGKD GTIEDIITVL KSVPFTARTA KRGSRFFCDA
AHHDESNC
