ID   INF2_MOUSE              Reviewed;        1273 AA.
AC   Q0GNC1; Q14C56; Q499F7; Q6P9T3;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Inverted formin-2;
GN   Name=Inf2;
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] (ISOFORM 1), FUNCTION, SUBUNIT, DOMAIN, ACTIVITY
RP   REGULATION, AND MUTAGENESIS OF LEU-1009; LEU-1010 AND LEU-1019.
RC   STRAIN=BALB/cJ;
RX   PubMed=16818491; DOI=10.1074/jbc.m604666200;
RA   Chhabra E.S., Higgs H.N.;
RT   "INF2 is a WASP homology 2 motif-containing formin that severs actin
RT   filaments and accelerates both polymerization and depolymerization.";
RL   J. Biol. Chem. 281:26754-26767(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 546-1273 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 556-1273 (ISOFORM 1).
RC   STRAIN=C3H/He, and C57BL/6J; TISSUE=Mesenchymal stem cell;
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   IDENTIFICATION BY 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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1172 AND SER-1174, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1203; THR-1223 AND THR-1230,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, 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).
CC   -!- FUNCTION: Severs actin filaments and accelerates their polymerization
CC       and depolymerization. {ECO:0000269|PubMed:16818491}.
CC   -!- ACTIVITY REGULATION: Phosphate inhibits both the depolymerization and
CC       severing activities. {ECO:0000269|PubMed:16818491}.
CC   -!- SUBUNIT: Interacts with profilin and actin at the FH1 and FH2 domains
CC       respectively. Interacts with DAAM2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q27J81, ECO:0000269|PubMed:16818491}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0GNC1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0GNC1-3; Sequence=VSP_021560;
CC   -!- DOMAIN: The WH2 domain acts as the DAD (diaphanous autoregulatory)
CC       domain and binds to actin monomers. {ECO:0000269|PubMed:16818491}.
CC   -!- DOMAIN: Regulated by autoinhibition due to intramolecular GBD-DAD
CC       binding. {ECO:0000269|PubMed:16818491}.
CC   -!- DOMAIN: The severing activity is dependent on covalent attachment of
CC       the FH2 domain to the C-terminus. {ECO:0000269|PubMed:16818491}.
CC   -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60610.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH99931.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DQ834374; ABI20145.1; -; mRNA.
DR   EMBL; BC060610; AAH60610.1; ALT_INIT; mRNA.
DR   EMBL; BC099931; AAH99931.1; ALT_INIT; mRNA.
DR   EMBL; BC115422; AAI15423.2; -; mRNA.
DR   EMBL; BC115423; AAI15424.2; -; mRNA.
DR   RefSeq; NP_940803.2; NM_198411.2.
DR   AlphaFoldDB; Q0GNC1; -.
DR   SMR; Q0GNC1; -.
DR   BioGRID; 214049; 6.
DR   DIP; DIP-61548N; -.
DR   IntAct; Q0GNC1; 3.
DR   STRING; 10090.ENSMUSP00000098591; -.
DR   GlyGen; Q0GNC1; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q0GNC1; -.
DR   PhosphoSitePlus; Q0GNC1; -.
DR   EPD; Q0GNC1; -.
DR   jPOST; Q0GNC1; -.
DR   MaxQB; Q0GNC1; -.
DR   PaxDb; 10090-ENSMUSP00000098591; -.
DR   PeptideAtlas; Q0GNC1; -.
DR   ProteomicsDB; 269405; -. [Q0GNC1-1]
DR   ProteomicsDB; 269406; -. [Q0GNC1-3]
DR   Pumba; Q0GNC1; -.
DR   DNASU; 70435; -.
DR   GeneID; 70435; -.
DR   KEGG; mmu:70435; -.
DR   AGR; MGI:1917685; -.
DR   CTD; 64423; -.
DR   MGI; MGI:1917685; Inf2.
DR   eggNOG; KOG1922; Eukaryota.
DR   InParanoid; Q0GNC1; -.
DR   PhylomeDB; Q0GNC1; -.
DR   BioGRID-ORCS; 70435; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Inf2; mouse.
DR   PRO; PR:Q0GNC1; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q0GNC1; Protein.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0045010; P:actin nucleation; IDA:MGI.
DR   GO; GO:0010467; P:gene expression; IDA:MGI.
DR   GO; GO:0032535; P:regulation of cellular component size; IMP:MGI.
DR   GO; GO:0090140; P:regulation of mitochondrial fission; ISO:MGI.
DR   CDD; cd22061; WH2_INF2; 1.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR010472; FH3_dom.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   InterPro; IPR027649; Inf2.
DR   InterPro; IPR003124; WH2_dom.
DR   PANTHER; PTHR46345; INVERTED FORMIN-2; 1.
DR   PANTHER; PTHR46345:SF5; INVERTED FORMIN-2; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   Pfam; PF02205; WH2; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q27J81"
FT   CHAIN           2..1273
FT                   /note="Inverted formin-2"
FT                   /id="PRO_0000259890"
FT   DOMAIN          2..330
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT   DOMAIN          421..564
FT                   /note="FH1"
FT   DOMAIN          589..979
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   DOMAIN          1007..1022
FT                   /note="WH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          907..984
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1063
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1136..1151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1209..1237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1249..1267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q27J81"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q27J81"
FT   MOD_RES         1172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         1174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         1203
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q27J81"
FT   MOD_RES         1218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q27J81"
FT   MOD_RES         1223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1230
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1256..1273
FT                   /note="EFVPDSDDIKAKRLCVIQ -> GLRSRPKAK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021560"
FT   MUTAGEN         1009
FT                   /note="L->A: Strongly inhibits depolymerization; when
FT                   associated with A-1010 and A-1019."
FT                   /evidence="ECO:0000269|PubMed:16818491"
FT   MUTAGEN         1010
FT                   /note="L->A: Strongly inhibits depolymerization; when
FT                   associated with A-1009 and A-1019."
FT                   /evidence="ECO:0000269|PubMed:16818491"
FT   MUTAGEN         1019
FT                   /note="L->A: Strongly inhibits depolymerization; when
FT                   associated with A-1009 and A-1010."
FT                   /evidence="ECO:0000269|PubMed:16818491"
FT   CONFLICT        1038
FT                   /note="T -> A (in Ref. 2; AAH60610/AAI15423)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1167
FT                   /note="Q -> R (in Ref. 2; AAH60610/AAI15423)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1273 AA;  138560 MW;  C4438AD8A7041476 CRC64;
     MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESAEPELCIR LLQMPSVVNY SGLRKRLESS
     DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT CISCVRAVMN SQQGIEYILS
     NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHAL TLDALDHYKM VCSQQYRFSV
     IMSELSDSDN VPYVVTLLSV INAIILGPED LRSRAQLRSE FIGLQLLDIL TRLRDLEDAD
     LLIQLEAFEE AKAEDEEELQ RISDGINMNS HQEVFASLFH KVSCSPASAQ LLSVLQGLMH
     LEPAGRSGQL LWEALENLVN RAVLLASDAQ ACTLEEVVER LLSIKGRPRP SPLDKAHKSV
     QTNSVQNQGS SSQNTTTPTT KVEGQQPVVA SPCQHVGSIQ SSSVDIAPQP VALEQCITAL
     PLPTPPLSSS TPVLPPTPPP LPGPGATSPL PPPPPPLPPP LPGSGTTSPP PPPPPPPPLP
     PPLPGSGTIS PPPPPPPPPL PGTGAVSPPP PPPLPSLPDS HKTQPPPPPP PPLPGMCPVP
     PPPPLPRAGQ IPPPPPLPGF SVPSMMGGVE EIIVAQVDHS LGSAWVPSHR RVNPPTLRMK
     KLNWQKLPSN VARERNSMWA TLGSPCTAAV EPDFSSIEQL FSFPTAKPKE PSAAPARKEP
     KEVTFLDSKK SLNLNIFLKQ FKCSNEEVTS MIQAGDTSKF DVEVLKQLLK LLPEKHEIEN
     LRAFTEERAK LSNADQFYVL LLDIPCYPLR VECMMLCEGT AIVLDMVRPK AQLVLTACES
     LLTSQRLPVF CQLILKIGNF LNYGSHTGDA DGFKISTLLK LTETKSQQSR VTLLHHVLEE
     VEKSHPDLLQ LSRDLEPPSQ AAGINVEIIH SEASANLKKL LEAERKVSAS IPEVQKQYAE
     RLQASIEASQ ELDKVFDAIE QKKLELADYL CEDPQQLSLE DTFSTMKTFR DLFTRALKEN
     KDRKEQMAKA ERRKQQLAEE EARRPRDEDG KPIRKGPGKQ EEVCVIDALL ADIRKGFQLR
     KTARGRGDTE ASGRVAPTDP PKATEPATAS NPTQGTNHPA SEPLDTTAAD EPQGWDLVDA
     VTPSPQPSKE EDGPPALERR SSWYVDAIDF LDPEDTPDAQ PSEGVWPVTL GDGQALNPLE
     FSSNKPPGVK SSHQDATDPE ALWGVHQTEA DSTSEGPEDE AQRGQSTHLP RTGPGEDEDG
     EDTAPESALD TSLDRSFSED AVTDSSGSGT LPRVQGRVSK GTSKRRKKRP SRNQEEFVPD
     SDDIKAKRLC VIQ
//