FHOD3_MOUSE
ID FHOD3_MOUSE Reviewed; 1578 AA.
AC Q76LL6; B2RQR3; Q5DTV7; Q76HP7; Q76LL5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=FH1/FH2 domain-containing protein 3;
DE AltName: Full=Formin homolog overexpressed in spleen 2;
DE Short=mFHOS2;
GN Name=Fhod3; Synonyms=Fhos2, Kiaa1695;
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 [MRNA] (ISOFORMS 1; 2 AND 4), TISSUE SPECIFICITY, AND
RP FUNCTION.
RX PubMed=15966898; DOI=10.1111/j.1365-2443.2005.00867.x;
RA Kanaya H., Takeya R., Takeuchi K., Watanabe N., Jing N., Sumimoto H.;
RT "Fhos2, a novel formin-related actin-organizing protein, probably
RT associates with the nestin intermediate filament.";
RL Genes Cells 10:665-678(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-1578 (ISOFORM 3).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345; SER-376; THR-413;
RP SER-921 AND THR-933, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, and Kidney;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21149568; DOI=10.1083/jcb.201005060;
RA Iskratsch T., Lange S., Dwyer J., Kho A.L., dos Remedios C., Ehler E.;
RT "Formin follows function: a muscle-specific isoform of FHOD3 is regulated
RT by CK2 phosphorylation and promotes myofibril maintenance.";
RL J. Cell Biol. 191:1159-1172(2010).
CC -!- FUNCTION: May play a role in actin filament polymerization in
CC cardiomyocytes (By similarity). Actin-organizing protein that may cause
CC stress fiber formation together with cell elongation. {ECO:0000250,
CC ECO:0000269|PubMed:15966898}.
CC -!- SUBUNIT: Interacts with nestin/NES-based interfilament (IF). Interacts
CC with SQSTM1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21149568}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:21149568}. Note=Main part of the protein localizes
CC to actin fibers and the remaining part displays filamentous staining.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Named isoforms=3.;
CC Name=1; Synonyms=FHOS2L;
CC IsoId=Q76LL6-1; Sequence=Displayed;
CC Name=2; Synonyms=FHOS2S;
CC IsoId=Q76LL6-2; Sequence=VSP_024400;
CC Name=3;
CC IsoId=Q76LL6-3; Sequence=VSP_024400, VSP_024401;
CC Name=4; Synonyms=FHOS2M;
CC IsoId=Q76LL6-4; Sequence=VSP_024399;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, including left ventricle,
CC kidney, brain and skeletal muscle, including soleus and tibialis
CC anterior (at protein level). {ECO:0000269|PubMed:15966898,
CC ECO:0000269|PubMed:21149568}.
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 -!- MISCELLANEOUS: [Isoform 1]: Major form in heart.
CC -!- MISCELLANEOUS: [Isoform 2]: Major form in kidney and brain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR EMBL; AB078608; BAC98302.1; -; mRNA.
DR EMBL; AB078609; BAC98303.1; -; mRNA.
DR EMBL; AB100088; BAC98348.1; -; mRNA.
DR EMBL; BC138046; AAI38047.1; -; mRNA.
DR EMBL; AK220413; BAD90459.1; -; mRNA.
DR CCDS; CCDS29104.1; -. [Q76LL6-1]
DR CCDS; CCDS89202.1; -. [Q76LL6-4]
DR CCDS; CCDS89203.1; -. [Q76LL6-2]
DR RefSeq; NP_001276583.1; NM_001289654.1. [Q76LL6-2]
DR RefSeq; NP_001276584.1; NM_001289655.1. [Q76LL6-4]
DR RefSeq; NP_780485.2; NM_175276.4. [Q76LL6-1]
DR AlphaFoldDB; Q76LL6; -.
DR SMR; Q76LL6; -.
DR BioGRID; 230379; 2.
DR IntAct; Q76LL6; 1.
DR STRING; 10090.ENSMUSP00000041361; -.
DR iPTMnet; Q76LL6; -.
DR PhosphoSitePlus; Q76LL6; -.
DR jPOST; Q76LL6; -.
DR MaxQB; Q76LL6; -.
DR PaxDb; Q76LL6; -.
DR PRIDE; Q76LL6; -.
DR ProteomicsDB; 267470; -. [Q76LL6-1]
DR ProteomicsDB; 267471; -. [Q76LL6-2]
DR ProteomicsDB; 267472; -. [Q76LL6-3]
DR ProteomicsDB; 267473; -. [Q76LL6-4]
DR Antibodypedia; 8734; 56 antibodies from 13 providers.
DR Ensembl; ENSMUST00000037097; ENSMUSP00000041361; ENSMUSG00000034295. [Q76LL6-1]
DR Ensembl; ENSMUST00000234526; ENSMUSP00000157193; ENSMUSG00000034295. [Q76LL6-4]
DR Ensembl; ENSMUST00000234834; ENSMUSP00000157226; ENSMUSG00000034295. [Q76LL6-2]
DR GeneID; 225288; -.
DR KEGG; mmu:225288; -.
DR UCSC; uc008ehb.2; mouse. [Q76LL6-1]
DR UCSC; uc008ehc.2; mouse. [Q76LL6-2]
DR UCSC; uc012bak.2; mouse. [Q76LL6-4]
DR CTD; 80206; -.
DR MGI; MGI:1925847; Fhod3.
DR VEuPathDB; HostDB:ENSMUSG00000034295; -.
DR eggNOG; KOG1925; Eukaryota.
DR GeneTree; ENSGT00940000154807; -.
DR HOGENOM; CLU_000814_0_1_1; -.
DR InParanoid; Q76LL6; -.
DR OMA; EDDAQCQ; -.
DR OrthoDB; 148001at2759; -.
DR PhylomeDB; Q76LL6; -.
DR TreeFam; TF316268; -.
DR BioGRID-ORCS; 225288; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Fhod3; mouse.
DR PRO; PR:Q76LL6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q76LL6; protein.
DR Bgee; ENSMUSG00000034295; Expressed in myocardium of ventricle and 257 other tissues.
DR Genevisible; Q76LL6; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005865; C:striated muscle thin filament; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:MGI.
DR GO; GO:0045214; P:sarcomere organization; IGI:MGI.
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; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR041387; FHOD1_GBD_N.
DR InterPro; IPR014768; GBD/FH3_dom.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF18382; Formin_GBD_N; 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 Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1578
FT /note="FH1/FH2 domain-containing protein 3"
FT /id="PRO_0000283792"
FT DOMAIN 18..405
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 985..1016
FT /note="FH1"
FT DOMAIN 1039..1435
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1515..1547
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 324..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 597..645
FT /evidence="ECO:0000255"
FT COMPBIAS 324..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..421
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1013
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 933
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 400..432
FT /note="KDEEEEEEEEQPITEPNSEEEREDDAQCQGKDS -> N (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15966898"
FT /id="VSP_024399"
FT VAR_SEQ 401..551
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15966898, ECO:0000303|Ref.3"
FT /id="VSP_024400"
FT VAR_SEQ 992..1005
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_024401"
FT CONFLICT 575
FT /note="Y -> S (in Ref. 3; BAD90459)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="S -> P (in Ref. 3; BAD90459)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="G -> S (in Ref. 3; BAD90459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1578 AA; 175655 MW; F9EE9B7354D51A70 CRC64;
MATLACRVQF LDDTDPFNST NFPEPSRPPL FTFREDLALG TQLAGVHRLL RAPHKLDDCT
LQLSHNGAYL DLEATLAEQR DELEGFQDDT GRGKKNSIIL RTQLSVRVHA CIEKLYNSSG
RDLRRALFSL KQIFQDDKDL VHEFVIAEGL TCLIKVGAEA DQNYQNYILR ALGQIMLYVD
GMNGVINHSE TIQWLYTLVG SKFRLVVKTA LKLLLVFVEY SESNAPLLIQ AVSAVDTKRG
VKPWSNIMEI LEEKDGVDTE LLVYAMTLVN KTLAGLPDQD TFYDVVDCLE ELGIAAVSQR
HLNKKGTDLD LLEQFNIYEV ALRHEDGDET AEPPPSGHRD RRRASMCSGG TVGEQQGLDR
RRSRRHSIQN IKSPLSAPTS PCSPSVPAFK PSQVRDLCEK DEEEEEEEEQ PITEPNSEEE
REDDAQCQGK DSKASSASGQ SSPGKDAAPE SSALHTTSSP TSQGRWLSAS TAARSPVLGG
TSGPEASRPA ARLLPPSPGL ATRPSTAPKV SPTIDKLPYV PHSPFHLFSY DFEDSPLLTK
DKGGDSQTEN RYSNFSSNSF QSSRPSPGPS GSPSYASSFS SPQDTRSSPS GLLTSSFRQH
QESLAAERER RRQEREERLQ RIEREERNKF NREYLDKREE QRQARGERYK YLEQLAAETQ
EKEPRSQSVS RGRADLSLDL SLPAAPAPPS PSSQSPSADS QEALPVPSSP PTLQCPQVSG
KDHEPELEAE AGQGADEASQ DIASAHRGAE SQEEPVLELE PEERASLSEK ERQNEEVNER
DNCSASSISS SSSTLEREEK EDKLSEDRAT GLWSTSLQDV GVNGQCGDIL TSKRFMLDML
YAHNRKSTED EEKDDGEPGR SAQEVEAVAS LATRISTLQA NSQAPEESIK RVDIGCLDNR
GSVKAFAEKF NSGEVGRGAI SPDVESQDKV PDTPPAQLKT ESDYIWDQLM ANPRELRIQD
MDFTDLGEED DIDVLDVDLG HREAPGPPPP PPPTFLGLPP PPPPPLLDSV PPPPVPGNLL
ASPVFNTPQG LGWSQVPRGQ PAFTKKKKTI RLFWNEVRPF EWPSKNNRRC REFLWSKLEP
IKVDTSRLEH LFESKSKELS VTKKTAADGK RQEIIVLDSK RSNAINIGLT VLPPPRTIKI
AILNFDEYAL NKEGIEKILT MIPTEEEKQK IQEAQLANPE VPLGSAEQFL LTLSSISELS
ARLHLWAFKM DYETTEKEVA EPLLDLKEGI DQLENNKTLG FILSTLLAIG NFLNGTNAKA
FELSYLEKVP EVKDTVHKQS LLHHVCTMVV ENFPDSSDLY SEIGAITRSA KVDFDQLQDN
LCQMERRCKA SWDHLKAIAK HEMKPVLKQR MSEFLKDCAE RIIILKIVHR RIINRFHSFL
LFMGHPPYAI REVNINKFCR IISEFALEYR TTRERVLQQK QKRANHRERN KTRGKMITDS
GKFSGSSPAA PSQPQGLSYA EDAAEHENMK AVLKTSSPAL EDATPVLGVR TRSRASRGST
SSWTMGTEES PSVTDDAADE IMDRIVKSAT QVPSQRVVPR ERKRSRANRK SLRRTLKSGL
TPEEARALGL VGTSELQL
