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FH1/FH2 domain-containing protein 1 (Formin homolog overexpressed in spleen 1) (FHOS) (Formin homology 2 domain-containing protein 1)

 FHOD1_MOUSE             Reviewed;        1197 AA.
Q6P9Q4; Q8BMK2;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 126.
RecName: Full=FH1/FH2 domain-containing protein 1;
AltName: Full=Formin homolog overexpressed in spleen 1;
Short=FHOS;
AltName: Full=Formin homology 2 domain-containing protein 1;
Name=Fhod1; Synonyms=Fhos1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell, and Spleen;
PubMed=15966898; DOI=10.1111/j.1365-2443.2005.00867.x;
Kanaya H., Takeya R., Takeuchi K., Watanabe N., Jing N., Sumimoto H.;
"Fhos2, a novel formin-related actin-organizing protein, probably
associates with the nestin intermediate filament.";
Genes Cells 10:665-678(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-524 AND
SER-527, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Required for the assembly of F-actin structures, such as
stress fibers. Depends on the Rho-ROCK cascade for its activity.
Contributes to the coordination of microtubules with actin fibers
and plays a role in cell elongation. Acts synergistically with
ROCK1 to promote SRC-dependent non-apoptotic plasma membrane
blebbing (By similarity). {ECO:0000250}.
-!- SUBUNIT: Self-associates via the FH2 domain. Binds to F-actin via
its N-terminus. Binds to the cytoplasmic domain of CD21 via its C-
terminus (By similarity). Interacts with ROCK1 in a Src-dependent
manner (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol
{ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell
projection, bleb {ECO:0000250}. Note=Predominantly cytoplasmic.
{ECO:0000250}.
-!- DOMAIN: Regulated by intramolecular binding to a C-terminal auto-
inhibitory domain. Effector binding abolishes this interaction and
activates the protein (By similarity). {ECO:0000250}.
-!- DOMAIN: The DAD domain regulates activation via by an
autoinhibitory interaction with the GBD/FH3 domain. This
autoinhibition is released upon competitive binding of an
activated GTPase. The release of DAD allows the FH2 domain to then
nucleate and elongate nonbranched actin filaments (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated by ROCK1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB041045; BAE06182.1; -; mRNA.
EMBL; AK030737; BAC27106.1; -; mRNA.
EMBL; BC060654; AAH60654.1; -; mRNA.
CCDS; CCDS22600.1; -.
RefSeq; NP_808367.2; NM_177699.4.
UniGene; Mm.87724; -.
ProteinModelPortal; Q6P9Q4; -.
SMR; Q6P9Q4; -.
BioGrid; 231560; 1.
IntAct; Q6P9Q4; 3.
MINT; Q6P9Q4; -.
STRING; 10090.ENSMUSP00000014922; -.
iPTMnet; Q6P9Q4; -.
PhosphoSitePlus; Q6P9Q4; -.
EPD; Q6P9Q4; -.
MaxQB; Q6P9Q4; -.
PaxDb; Q6P9Q4; -.
PeptideAtlas; Q6P9Q4; -.
PRIDE; Q6P9Q4; -.
Ensembl; ENSMUST00000014922; ENSMUSP00000014922; ENSMUSG00000014778.
GeneID; 234686; -.
KEGG; mmu:234686; -.
UCSC; uc009nct.2; mouse.
CTD; 29109; -.
MGI; MGI:2679008; Fhod1.
eggNOG; KOG1925; Eukaryota.
eggNOG; ENOG410XRBZ; LUCA.
GeneTree; ENSGT00870000136417; -.
HOGENOM; HOG000015130; -.
HOVERGEN; HBG051615; -.
InParanoid; Q6P9Q4; -.
OMA; PKLCIGD; -.
OrthoDB; EOG091G0147; -.
PhylomeDB; Q6P9Q4; -.
TreeFam; TF316268; -.
ChiTaRS; Fhod1; mouse.
PRO; PR:Q6P9Q4; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000014778; -.
CleanEx; MM_FHOD1; -.
Genevisible; Q6P9Q4; MM.
GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0014704; C:intercalated disc; IDA:MGI.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; IEA:Ensembl.
GO; GO:0051660; P:establishment of centrosome localization; IMP:MGI.
GO; GO:0007097; P:nuclear migration; IMP:MGI.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR015425; FH2_Formin.
InterPro; IPR027647; FHOD1.
InterPro; IPR014768; GBD/FH3_dom.
PANTHER; PTHR23213:SF189; PTHR23213:SF189; 3.
Pfam; PF02181; FH2; 1.
SMART; SM00498; FH2; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS51444; FH2; 1.
PROSITE; PS51232; GBD_FH3; 1.
1: Evidence at protein level;
Actin-binding; Cell projection; Complete proteome; Cytoplasm;
Cytoskeleton; Phosphoprotein; Reference proteome.
CHAIN 1 1197 FH1/FH2 domain-containing protein 1.
/FTId=PRO_0000194906.
DOMAIN 53 462 GBD/FH3. {ECO:0000255|PROSITE-
ProRule:PRU00579}.
DOMAIN 491 647 FH1.
DOMAIN 648 1045 FH2. {ECO:0000255|PROSITE-
ProRule:PRU00774}.
DOMAIN 1085 1166 DAD.
REGION 644 839 Interaction with ROCK1. {ECO:0000250}.
COMPBIAS 491 641 Pro-rich.
COMPBIAS 1028 1031 Poly-Gln.
MOD_RES 370 370 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y613}.
MOD_RES 499 499 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Y613}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y613}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 722 722 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Y613}.
CONFLICT 323 323 L -> Q (in Ref. 2; BAC27106).
{ECO:0000305}.
CONFLICT 929 929 E -> K (in Ref. 2; BAC27106).
{ECO:0000305}.
CONFLICT 1196 1196 E -> G (in Ref. 2; BAC27106).
{ECO:0000305}.
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


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