FHOD1_MOUSE
ID FHOD1_MOUSE Reviewed; 1197 AA.
AC Q6P9Q4; Q8BMK2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=FH1/FH2 domain-containing protein 1;
DE AltName: Full=Formin homolog overexpressed in spleen 1;
DE Short=FHOS;
DE AltName: Full=Formin homology 2 domain-containing protein 1;
GN Name=Fhod1; Synonyms=Fhos1;
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].
RC TISSUE=B-cell, and Spleen;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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].
RC STRAIN=C57BL/6J; 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 SER-370, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-524 AND SER-527, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: Required for the assembly of F-actin structures, such as
CC stress fibers. Depends on the Rho-ROCK cascade for its activity.
CC Contributes to the coordination of microtubules with actin fibers and
CC plays a role in cell elongation. Acts synergistically with ROCK1 to
CC promote SRC-dependent non-apoptotic plasma membrane blebbing (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Self-associates via the FH2 domain. Binds to F-actin via its
CC N-terminus. Binds to the cytoplasmic domain of CD21 via its C-terminus
CC (By similarity). Interacts with ROCK1 in a Src-dependent manner (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection,
CC bleb {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}.
CC -!- DOMAIN: Regulated by intramolecular binding to a C-terminal auto-
CC inhibitory domain. Effector binding abolishes this interaction and
CC activates the protein (By similarity). {ECO:0000250}.
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 -!- PTM: Phosphorylated by ROCK1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR EMBL; AB041045; BAE06182.1; -; mRNA.
DR EMBL; AK030737; BAC27106.1; -; mRNA.
DR EMBL; BC060654; AAH60654.1; -; mRNA.
DR CCDS; CCDS22600.1; -.
DR RefSeq; NP_808367.2; NM_177699.4.
DR AlphaFoldDB; Q6P9Q4; -.
DR SMR; Q6P9Q4; -.
DR BioGRID; 231560; 1.
DR IntAct; Q6P9Q4; 2.
DR MINT; Q6P9Q4; -.
DR STRING; 10090.ENSMUSP00000014922; -.
DR iPTMnet; Q6P9Q4; -.
DR PhosphoSitePlus; Q6P9Q4; -.
DR EPD; Q6P9Q4; -.
DR jPOST; Q6P9Q4; -.
DR MaxQB; Q6P9Q4; -.
DR PaxDb; Q6P9Q4; -.
DR PeptideAtlas; Q6P9Q4; -.
DR PRIDE; Q6P9Q4; -.
DR ProteomicsDB; 267469; -.
DR Antibodypedia; 15694; 163 antibodies from 26 providers.
DR Ensembl; ENSMUST00000014922; ENSMUSP00000014922; ENSMUSG00000014778.
DR GeneID; 234686; -.
DR KEGG; mmu:234686; -.
DR UCSC; uc009nct.2; mouse.
DR CTD; 29109; -.
DR MGI; MGI:2679008; Fhod1.
DR VEuPathDB; HostDB:ENSMUSG00000014778; -.
DR eggNOG; KOG1925; Eukaryota.
DR GeneTree; ENSGT00940000160212; -.
DR HOGENOM; CLU_000814_0_0_1; -.
DR InParanoid; Q6P9Q4; -.
DR OMA; TSPNCSC; -.
DR OrthoDB; 148001at2759; -.
DR PhylomeDB; Q6P9Q4; -.
DR TreeFam; TF316268; -.
DR BioGRID-ORCS; 234686; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Fhod1; mouse.
DR PRO; PR:Q6P9Q4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6P9Q4; protein.
DR Bgee; ENSMUSG00000014778; Expressed in granulocyte and 166 other tissues.
DR Genevisible; Q6P9Q4; MM.
DR GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051660; P:establishment of centrosome localization; IMP:MGI.
DR GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO: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; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR027647; FHOD1.
DR InterPro; IPR041387; FHOD1_GBD_N.
DR InterPro; IPR014768; GBD/FH3_dom.
DR PANTHER; PTHR45920:SF2; PTHR45920:SF2; 3.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF18382; Formin_GBD_N; 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 Actin-binding; Cell projection; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1197
FT /note="FH1/FH2 domain-containing protein 1"
FT /id="PRO_0000194906"
FT DOMAIN 53..462
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 491..647
FT /note="FH1"
FT DOMAIN 648..1045
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1085..1166
FT /note="DAD"
FT REGION 344..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..839
FT /note="Interaction with ROCK1"
FT /evidence="ECO:0000250"
FT REGION 1055..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..641
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y613"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y613"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y613"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 722
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y613"
FT CONFLICT 323
FT /note="L -> Q (in Ref. 2; BAC27106)"
FT /evidence="ECO:0000305"
FT CONFLICT 929
FT /note="E -> K (in Ref. 2; BAC27106)"
FT /evidence="ECO:0000305"
FT CONFLICT 1196
FT /note="E -> G (in Ref. 2; BAC27106)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1197 AA; 129600 MW; 162634FAB9715F01 CRC64;
MAGEEERGDG DPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP LSAQIPALHR
LLGAPLKLED CALQVSPSGY YLDPELSLEE QREMLEGFYE EISKGRKPTL ILRTQLSVRV
NAILEKLYGS SGPELRRSLF SLKQIFQEDK DLVPEFVHSE GLSCLIRVGA AADHNYQSYI
LRALGQLMLF VDGMLGVVAH SETVQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF
IQAVNAVASA TGTLPWANLV SILEEKNGAD AELLVYTVTL INKTLAALPD QDSFYDVTDA
LEQQGMEALV QRFLGTAGTD VDLRTQLTLY ESALRLEDGD MEEAAAAAAA GGRRERRKPS
SEEGKRSRRS LEGGGCPVRA PEPGSTGSAS PVGSTPSTGS APPTNPAFSS TGPASGLLRT
SVNLFPTISV GPSVDSSCER SVYKARFLEN VAAAETEKQA ALAQGRAETL AGATVDDTDG
SSGTRELWDS PEPASAPRTP QSPVSRILLR TQRSLEPEPK KPVSPPSPKA EPIQEPPTCV
PKLCIGDLDF SDLGEDEDQD TLNVESVEAG KASPFLSSLS PSLSGGPPPP PPPPPPITGS
CPPPPPPPLP PPATGSCPPP PPPPPPPIIG SCPPPPPLAA PFTHSALDGP RHPTKRKTVK
LFWRELKLTG GPGCSRSRFG PCPTLWASLE PVSVDTARLE HLFESRAKDV LPTKKAGEGR
RTMTVVLDPK RSNAINIGLT TLPPVHVIKA ALLNFDEFAV SKDGIEKLLT MMPTEEERQK
IEEAQLANPD VPLGPAENFL MTLASIGGLA ARLQLWAFKL DYESMEREIA EPLFDLKVGM
EQLVHNATFR CILATLLAVG NFLNGSQSSG FELSYLEKVS EVKDTVRRQS LLYHLCSLVL
QTRPDSSDLY SEIPALTRCA KVDFEQLTEN LGQLECRSQA AEDSLRSLAK HELSPALRAR
LTHFLAQCTR RVAMLRVVHR RVCNRFHAFL LYLGYTPQAA RDVRIMQFCH TLREFALEYR
TCRERVLQQQ QKRATYRERN KTRGRMITET EKFSGVAGEA PNNLSVPVAV GSGPGQGDTD
NHASMKSLLT SRPEDATHSR RSRGMVQSSS PVSHTAVGPS AASPEETAAS GLPTDTSDEI
MDLLVQSVTK SGPRALAARE RKRSRGNRKS LRRTLKSGLG DDLVQALGLS KAPGLEV
