FHDC1_MOUSE
ID FHDC1_MOUSE Reviewed; 1149 AA.
AC Q3ULZ2; B9EHC4; Q69ZC2; Q8C0A0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=FH2 domain-containing protein 1;
DE AltName: Full=Inverted formin-1 {ECO:0000303|PubMed:18815276};
GN Name=Fhdc1; Synonyms=Inf1 {ECO:0000303|PubMed:18815276}, Kiaa1727;
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].
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Medulla oblongata;
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 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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18815276; DOI=10.1091/mbc.e08-05-0469;
RA Young K.G., Thurston S.F., Copeland S., Smallwood C., Copeland J.W.;
RT "INF1 is a novel microtubule-associated formin.";
RL Mol. Biol. Cell 19:5168-5180(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-655, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26564798; DOI=10.1091/mbc.e15-02-0070;
RA Copeland S.J., Thurston S.F., Copeland J.W.;
RT "Actin- and microtubule-dependent regulation of Golgi morphology by
RT FHDC1.";
RL Mol. Biol. Cell 27:260-276(2016).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP170.
RX PubMed=29742020; DOI=10.1091/mbc.e18-02-0088;
RA Copeland S.J., McRae A., Guarguaglini G., Trinkle-Mulcahy L.,
RA Copeland J.W.;
RT "Actin-dependent regulation of cilia length by the inverted formin FHDC1.";
RL Mol. Biol. Cell 29:1611-1627(2018).
CC -!- FUNCTION: Microtubule-associated formin which regulates both actin and
CC microtubule dynamics. Induces microtubule acetylation and stabilization
CC and actin stress fiber formation (PubMed:18815276). Regulates Golgi
CC ribbon formation (PubMed:26564798). Required for normal cilia assembly.
CC Early in cilia assembly, may assist in the maturation and positioning
CC of the centrosome/basal body, and once cilia assembly has initiated,
CC may also promote cilia elongation by inhibiting disassembly
CC (PubMed:29742020). {ECO:0000269|PubMed:18815276,
CC ECO:0000269|PubMed:26564798, ECO:0000269|PubMed:29742020}.
CC -!- SUBUNIT: Interacts with CEP170. {ECO:0000269|PubMed:29742020}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:26564798}.
CC Cell projection, cilium {ECO:0000250|UniProtKB:Q9C0D6}. Note=Associates
CC with microtubules. {ECO:0000269|PubMed:18815276,
CC ECO:0000269|PubMed:26564798, ECO:0000269|PubMed:29742020}.
CC -!- TISSUE SPECIFICITY: Brain, heart and lung (at protein level).
CC {ECO:0000269|PubMed:18815276}.
CC -!- DOMAIN: The FH2 and MBD domains are essential for its function in
CC regulating Golgi ribbon formation. {ECO:0000250|UniProtKB:Q9C0D6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32522.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173244; BAD32522.1; ALT_INIT; mRNA.
DR EMBL; AK031946; BAC27616.1; -; mRNA.
DR EMBL; AK145217; BAE26306.1; -; mRNA.
DR EMBL; BC137632; AAI37633.1; -; mRNA.
DR CCDS; CCDS17438.1; -.
DR RefSeq; NP_001028473.2; NM_001033301.4.
DR RefSeq; NP_001192284.1; NM_001205355.1.
DR RefSeq; XP_006501391.1; XM_006501328.3.
DR AlphaFoldDB; Q3ULZ2; -.
DR SMR; Q3ULZ2; -.
DR BioGRID; 230846; 11.
DR IntAct; Q3ULZ2; 1.
DR STRING; 10090.ENSMUSP00000088525; -.
DR iPTMnet; Q3ULZ2; -.
DR PhosphoSitePlus; Q3ULZ2; -.
DR jPOST; Q3ULZ2; -.
DR MaxQB; Q3ULZ2; -.
DR PaxDb; Q3ULZ2; -.
DR PRIDE; Q3ULZ2; -.
DR ProteomicsDB; 270986; -.
DR Antibodypedia; 16653; 13 antibodies from 8 providers.
DR DNASU; 229474; -.
DR Ensembl; ENSMUST00000091002; ENSMUSP00000088525; ENSMUSG00000041842.
DR Ensembl; ENSMUST00000107689; ENSMUSP00000103317; ENSMUSG00000041842.
DR GeneID; 229474; -.
DR KEGG; mmu:229474; -.
DR UCSC; uc008pqc.3; mouse.
DR CTD; 85462; -.
DR MGI; MGI:2684972; Fhdc1.
DR VEuPathDB; HostDB:ENSMUSG00000041842; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000155128; -.
DR HOGENOM; CLU_009023_0_0_1; -.
DR InParanoid; Q3ULZ2; -.
DR OMA; LECWKQE; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; Q3ULZ2; -.
DR TreeFam; TF324020; -.
DR BioGRID-ORCS; 229474; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Fhdc1; mouse.
DR PRO; PR:Q3ULZ2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3ULZ2; protein.
DR Bgee; ENSMUSG00000041842; Expressed in femorotibial joint and 185 other tissues.
DR ExpressionAtlas; Q3ULZ2; baseline and differential.
DR Genevisible; Q3ULZ2; MM.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0090161; P:Golgi ribbon formation; IMP:UniProtKB.
DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Cilium biogenesis/degradation;
KW Golgi apparatus; Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1149
FT /note="FH2 domain-containing protein 1"
FT /id="PRO_0000317281"
FT DOMAIN 88..483
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 18..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1086
FT /note="MTBD; microtubule-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D6"
FT COMPBIAS 31..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D6"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 55
FT /note="S -> P (in Ref. 2; BAE26306)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="Missing (in Ref. 2; BAC27616)"
FT /evidence="ECO:0000305"
FT CONFLICT 878
FT /note="S -> R (in Ref. 2; BAE26306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1149 AA; 125367 MW; C69D98C60C6B0782 CRC64;
MHVMNCVSLA SDKENGTLAT AAAFMTGQTS PSASPPPPPP PPPPPPCPHS GEGFSPSPPP
PLPPPLPGGP PIPPPPPPGL PSVSYLNGYS SLGKKKRMRS FFWKTIPEEQ VRGKTNIWTL
AAKQQHQYQI DKKTIEELFG QQEDTSKASL PKRGGALNSS FRDAREEVTV LDAKRSMNIG
IFLKQFKKSP QSIVEDIYQG KSEHYGSETL REILKLLPES EEVKKLKAFN GDVSKLSLAD
SFLHCLIQVP NYSLRIEAMV LKKEFLPSCS SLFKDIRTLR AATKELMLCE ELHSILHLVL
QAGNIMNAGG YAGNAVGFKL SSLLKLADTK ANKPGMNLLH FVAQEAQKQD AILLNFSEKL
QHVQETSRLS LDITEAELHS LFVRTKSLQE NIQLDQELCQ QMEDFLQFAV EKLAELELWK
RELQGEAHTL IDFFCEDKET MKLDECFQIF RDFCTRFNKA VKDNHDREEQ ERKQLQRQKE
MEQKRYSWST GELGSFGRSS SENDVQMLAK TGTEDLPSFL KPRPNSPSYR PPNTRRSRLS
LGISADRELL TFLESATSSP EDPNKFNSLP RSSPRQARPT IAWMEPREQQ SHGPNFTHEP
QASKIQEKAP PPAWQNQLPT TWREEPASPL PLAGRSRPSL RKRNSEPVGL GPTQSPPLLP
LDLGVREHEL VTGLTQFDLQ SPKSLEEGSQ LTLNDFCPTK LPSPGDRSSQ PFAAGGDSLP
PKDTDTQEVL SPAGEDDRTI SDEPSSEALV SVVVTDTEDK DAGPLLYVSD TTDCSLTLDC
SEGMDSRAGG DKQEEEKEGD GSVSSGAGEA GSSQVSSNSV SSPPGEVPAP KSSKSELSCQ
GGLPKDRPSR GKDAIAPKRN SFKEASVGAS KPVSARRSQG VTTKPVRTLN SSENEHMRKV
VPISKSSRGA GPWKRPEPTP KATPRETPSS TDTPLSRRSS VRGTSDTSPR RPQVSGSGAE
EPRLPRSSGS ISGRPGKDAP LQPRASFRKP SAKPLRNIPR QKPEENKVSS PNSPDPESPK
EEPKAPQATG VSRALPPIPS FARNTVASSS RSLRTDAPPA ARTTGLTRTV SQRQLRVKGG
SEDSASKDIG TLKRASSARA SKKCPESAGG SSANVETSLK GRGTTERSSL RLKDSGQATL
GRILRPLQK
