INF2_MOUSE
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 03-AUG-2022, entry version 103.
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; 4.
DR DIP; DIP-61548N; -.
DR IntAct; Q0GNC1; 3.
DR STRING; 10090.ENSMUSP00000098591; -.
DR iPTMnet; Q0GNC1; -.
DR PhosphoSitePlus; Q0GNC1; -.
DR EPD; Q0GNC1; -.
DR jPOST; Q0GNC1; -.
DR MaxQB; Q0GNC1; -.
DR PaxDb; Q0GNC1; -.
DR PeptideAtlas; Q0GNC1; -.
DR PRIDE; Q0GNC1; -.
DR ProteomicsDB; 269405; -. [Q0GNC1-1]
DR ProteomicsDB; 269406; -. [Q0GNC1-3]
DR DNASU; 70435; -.
DR GeneID; 70435; -.
DR KEGG; mmu:70435; -.
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 74 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:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0032535; P:regulation of cellular component size; IMP:MGI.
DR GO; GO:0090140; P:regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IBA:GO_Central.
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; 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; PTHR46345; 2.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 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
