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Q0GNC1

- INF2_MOUSE

UniProt

Q0GNC1 - INF2_MOUSE

Protein

Inverted formin-2

Gene

Inf2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (03 Oct 2006)
      Previous versions | rss
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    Functioni

    Severs actin filaments and accelerates their polymerization and depolymerization.1 Publication

    Enzyme regulationi

    Phosphate inhibits both the depolymerization and severing activities.1 Publication

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. regulation of cellular component size Source: MGI

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inverted formin-2
    Gene namesi
    Name:Inf2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1917685. Inf2.

    Subcellular locationi

    Cytoplasmperinuclear region By similarity

    GO - Cellular componenti

    1. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1009 – 10091L → A: Strongly inhibits depolymerization; when associated with A-1010 and A-1019. 1 Publication
    Mutagenesisi1010 – 10101L → A: Strongly inhibits depolymerization; when associated with A-1009 and A-1019. 1 Publication
    Mutagenesisi1019 – 10191L → A: Strongly inhibits depolymerization; when associated with A-1009 and A-1010. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 12731272Inverted formin-2PRO_0000259890Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei1172 – 11721Phosphoserine1 Publication
    Modified residuei1174 – 11741Phosphoserine1 Publication
    Modified residuei1203 – 12031PhosphothreonineBy similarity
    Modified residuei1216 – 12161PhosphoserineBy similarity
    Modified residuei1230 – 12301PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ0GNC1.
    PaxDbiQ0GNC1.
    PRIDEiQ0GNC1.

    PTM databases

    PhosphoSiteiQ0GNC1.

    Expressioni

    Gene expression databases

    GenevestigatoriQ0GNC1.

    Interactioni

    Subunit structurei

    Interacts with profilin and actin at the FH1 and FH2 domains respectively.1 Publication

    Protein-protein interaction databases

    BioGridi214049. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0GNC1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 330329GBD/FH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini421 – 564144FH1Add
    BLAST
    Domaini589 – 979391FH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1007 – 102216WH2PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili907 – 98478Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi421 – 563143Pro-richAdd
    BLAST

    Domaini

    The WH2 domain acts as the DAD (diaphanous autoregulatory) domain and binds to actin monomers.1 Publication
    Regulated by autoinhibition due to intramolecular GBD-DAD binding.1 Publication
    The severing activity is dependent on covalent attachment of the FH2 domain to the C-terminus.1 Publication

    Sequence similaritiesi

    Belongs to the formin homology family.Curated
    Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
    Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation
    Contains 1 WH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG149898.
    HOGENOMiHOG000113072.
    HOVERGENiHBG081794.
    InParanoidiQ0GNC1.
    PhylomeDBiQ0GNC1.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR015425. FH2_Formin.
    IPR010472. FH3_dom.
    IPR010473. GTPase-bd.
    IPR014768. GTPase-bd/formin_homology_3.
    IPR027649. Inf2.
    IPR003124. WH2_dom.
    [Graphical view]
    PANTHERiPTHR23213:SF5. PTHR23213:SF5. 1 hit.
    PfamiPF06367. Drf_FH3. 1 hit.
    PF06371. Drf_GBD. 1 hit.
    PF02181. FH2. 1 hit.
    PF02205. WH2. 1 hit.
    [Graphical view]
    SMARTiSM00498. FH2. 1 hit.
    SM00246. WH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    PS51082. WH2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q0GNC1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESAEPELCIR LLQMPSVVNY     50
    SGLRKRLESS DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT 100
    CISCVRAVMN SQQGIEYILS NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL 150
    CIYSPEGHAL TLDALDHYKM VCSQQYRFSV IMSELSDSDN VPYVVTLLSV 200
    INAIILGPED LRSRAQLRSE FIGLQLLDIL TRLRDLEDAD LLIQLEAFEE 250
    AKAEDEEELQ RISDGINMNS HQEVFASLFH KVSCSPASAQ LLSVLQGLMH 300
    LEPAGRSGQL LWEALENLVN RAVLLASDAQ ACTLEEVVER LLSIKGRPRP 350
    SPLDKAHKSV QTNSVQNQGS SSQNTTTPTT KVEGQQPVVA SPCQHVGSIQ 400
    SSSVDIAPQP VALEQCITAL PLPTPPLSSS TPVLPPTPPP LPGPGATSPL 450
    PPPPPPLPPP LPGSGTTSPP PPPPPPPPLP PPLPGSGTIS PPPPPPPPPL 500
    PGTGAVSPPP PPPLPSLPDS HKTQPPPPPP PPLPGMCPVP PPPPLPRAGQ 550
    IPPPPPLPGF SVPSMMGGVE EIIVAQVDHS LGSAWVPSHR RVNPPTLRMK 600
    KLNWQKLPSN VARERNSMWA TLGSPCTAAV EPDFSSIEQL FSFPTAKPKE 650
    PSAAPARKEP KEVTFLDSKK SLNLNIFLKQ FKCSNEEVTS MIQAGDTSKF 700
    DVEVLKQLLK LLPEKHEIEN LRAFTEERAK LSNADQFYVL LLDIPCYPLR 750
    VECMMLCEGT AIVLDMVRPK AQLVLTACES LLTSQRLPVF CQLILKIGNF 800
    LNYGSHTGDA DGFKISTLLK LTETKSQQSR VTLLHHVLEE VEKSHPDLLQ 850
    LSRDLEPPSQ AAGINVEIIH SEASANLKKL LEAERKVSAS IPEVQKQYAE 900
    RLQASIEASQ ELDKVFDAIE QKKLELADYL CEDPQQLSLE DTFSTMKTFR 950
    DLFTRALKEN KDRKEQMAKA ERRKQQLAEE EARRPRDEDG KPIRKGPGKQ 1000
    EEVCVIDALL ADIRKGFQLR KTARGRGDTE ASGRVAPTDP PKATEPATAS 1050
    NPTQGTNHPA SEPLDTTAAD EPQGWDLVDA VTPSPQPSKE EDGPPALERR 1100
    SSWYVDAIDF LDPEDTPDAQ PSEGVWPVTL GDGQALNPLE FSSNKPPGVK 1150
    SSHQDATDPE ALWGVHQTEA DSTSEGPEDE AQRGQSTHLP RTGPGEDEDG 1200
    EDTAPESALD TSLDRSFSED AVTDSSGSGT LPRVQGRVSK GTSKRRKKRP 1250
    SRNQEEFVPD SDDIKAKRLC VIQ 1273
    Length:1,273
    Mass (Da):138,560
    Last modified:October 3, 2006 - v1
    Checksum:iC4438AD8A7041476
    GO
    Isoform 2 (identifier: Q0GNC1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1256-1273: EFVPDSDDIKAKRLCVIQ → GLRSRPKAK

    Note: No experimental confirmation available.

    Show »
    Length:1,264
    Mass (Da):137,496
    Checksum:iCC8EEF55F65801CB
    GO

    Sequence cautioni

    The sequence AAH60610.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH99931.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1038 – 10381T → A in AAH60610. (PubMed:15489334)Curated
    Sequence conflicti1038 – 10381T → A in AAI15423. (PubMed:15489334)Curated
    Sequence conflicti1167 – 11671Q → R in AAH60610. (PubMed:15489334)Curated
    Sequence conflicti1167 – 11671Q → R in AAI15423. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1256 – 127318EFVPD…LCVIQ → GLRSRPKAK in isoform 2. 1 PublicationVSP_021560Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ834374 mRNA. Translation: ABI20145.1.
    BC060610 mRNA. Translation: AAH60610.1. Different initiation.
    BC099931 mRNA. Translation: AAH99931.1. Different initiation.
    BC115422 mRNA. Translation: AAI15423.2.
    BC115423 mRNA. Translation: AAI15424.2.
    RefSeqiNP_940803.2. NM_198411.2.
    UniGeneiMm.250193.

    Genome annotation databases

    GeneIDi70435.
    KEGGimmu:70435.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ834374 mRNA. Translation: ABI20145.1 .
    BC060610 mRNA. Translation: AAH60610.1 . Different initiation.
    BC099931 mRNA. Translation: AAH99931.1 . Different initiation.
    BC115422 mRNA. Translation: AAI15423.2 .
    BC115423 mRNA. Translation: AAI15424.2 .
    RefSeqi NP_940803.2. NM_198411.2.
    UniGenei Mm.250193.

    3D structure databases

    ProteinModelPortali Q0GNC1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 214049. 1 interaction.

    PTM databases

    PhosphoSitei Q0GNC1.

    Proteomic databases

    MaxQBi Q0GNC1.
    PaxDbi Q0GNC1.
    PRIDEi Q0GNC1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 70435.
    KEGGi mmu:70435.

    Organism-specific databases

    CTDi 64423.
    MGIi MGI:1917685. Inf2.

    Phylogenomic databases

    eggNOGi NOG149898.
    HOGENOMi HOG000113072.
    HOVERGENi HBG081794.
    InParanoidi Q0GNC1.
    PhylomeDBi Q0GNC1.

    Miscellaneous databases

    NextBioi 331621.
    PROi Q0GNC1.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q0GNC1.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR015425. FH2_Formin.
    IPR010472. FH3_dom.
    IPR010473. GTPase-bd.
    IPR014768. GTPase-bd/formin_homology_3.
    IPR027649. Inf2.
    IPR003124. WH2_dom.
    [Graphical view ]
    PANTHERi PTHR23213:SF5. PTHR23213:SF5. 1 hit.
    Pfami PF06367. Drf_FH3. 1 hit.
    PF06371. Drf_GBD. 1 hit.
    PF02181. FH2. 1 hit.
    PF02205. WH2. 1 hit.
    [Graphical view ]
    SMARTi SM00498. FH2. 1 hit.
    SM00246. WH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    PS51082. WH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "INF2 is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization."
      Chhabra E.S., Higgs H.N.
      J. Biol. Chem. 281:26754-26767(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, DOMAIN, ENZYME REGULATION, MUTAGENESIS OF LEU-1009; LEU-1010 AND LEU-1019.
      Strain: BALB/c.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 546-1273 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 556-1273 (ISOFORM 1).
      Strain: C3H/He and C57BL/6.
      Tissue: Mesenchymal stem cell.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    4. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1172 AND SER-1174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiINF2_MOUSE
    AccessioniPrimary (citable) accession number: Q0GNC1
    Secondary accession number(s): Q14C56, Q499F7, Q6P9T3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 14, 2006
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 65 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3