Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0GNC1 (INF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inverted formin-2
Gene names
Name:Inf2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Enzyme regulation

Phosphate inhibits both the depolymerization and severing activities. Ref.1

Subunit structure

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

Subcellular location

Cytoplasmperinuclear region By similarity.

Domain

The WH2 domain acts as the DAD (diaphanous autoregulatory) domain and binds to actin monomers. Ref.1

Regulated by autoinhibition due to intramolecular GBD-DAD binding. Ref.1

The severing activity is dependent on covalent attachment of the FH2 domain to the C-terminus. Ref.1

Sequence similarities

Belongs to the formin homology family.

Contains 1 FH1 (formin homology 1) domain.

Contains 1 FH2 (formin homology 2) domain.

Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.

Contains 1 WH2 domain.

Sequence caution

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

regulation of cellular component size

Inferred from mutant phenotype PubMed 23349293. Source: MGI

   Cellular_componentperinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q0GNC1-1)

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.
Isoform 2 (identifier: Q0GNC1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1256-1273: EFVPDSDDIKAKRLCVIQ → GLRSRPKAK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 12731272Inverted formin-2
PRO_0000259890

Regions

Domain2 – 330329GBD/FH3
Domain421 – 564144FH1
Domain589 – 979391FH2
Domain1007 – 102216WH2
Coiled coil907 – 98478 Potential
Compositional bias421 – 563143Pro-rich

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue11721Phosphoserine Ref.4
Modified residue11741Phosphoserine Ref.4
Modified residue12031Phosphothreonine By similarity
Modified residue12161Phosphoserine By similarity
Modified residue12301Phosphothreonine By similarity

Natural variations

Alternative sequence1256 – 127318EFVPD…LCVIQ → GLRSRPKAK in isoform 2.
VSP_021560

Experimental info

Mutagenesis10091L → A: Strongly inhibits depolymerization; when associated with A-1010 and A-1019. Ref.1
Mutagenesis10101L → A: Strongly inhibits depolymerization; when associated with A-1009 and A-1019. Ref.1
Mutagenesis10191L → A: Strongly inhibits depolymerization; when associated with A-1009 and A-1010. Ref.1
Sequence conflict10381T → A in AAH60610. Ref.2
Sequence conflict10381T → A in AAI15423. Ref.2
Sequence conflict11671Q → R in AAH60610. Ref.2
Sequence conflict11671Q → R in AAI15423. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: C4438AD8A7041476

FASTA1,273138,560
        10         20         30         40         50         60 
MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESAEPELCIR LLQMPSVVNY SGLRKRLESS 

        70         80         90        100        110        120 
DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT CISCVRAVMN SQQGIEYILS 

       130        140        150        160        170        180 
NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHAL TLDALDHYKM VCSQQYRFSV 

       190        200        210        220        230        240 
IMSELSDSDN VPYVVTLLSV INAIILGPED LRSRAQLRSE FIGLQLLDIL TRLRDLEDAD 

       250        260        270        280        290        300 
LLIQLEAFEE AKAEDEEELQ RISDGINMNS HQEVFASLFH KVSCSPASAQ LLSVLQGLMH 

       310        320        330        340        350        360 
LEPAGRSGQL LWEALENLVN RAVLLASDAQ ACTLEEVVER LLSIKGRPRP SPLDKAHKSV 

       370        380        390        400        410        420 
QTNSVQNQGS SSQNTTTPTT KVEGQQPVVA SPCQHVGSIQ SSSVDIAPQP VALEQCITAL 

       430        440        450        460        470        480 
PLPTPPLSSS TPVLPPTPPP LPGPGATSPL PPPPPPLPPP LPGSGTTSPP PPPPPPPPLP 

       490        500        510        520        530        540 
PPLPGSGTIS PPPPPPPPPL PGTGAVSPPP PPPLPSLPDS HKTQPPPPPP PPLPGMCPVP 

       550        560        570        580        590        600 
PPPPLPRAGQ IPPPPPLPGF SVPSMMGGVE EIIVAQVDHS LGSAWVPSHR RVNPPTLRMK 

       610        620        630        640        650        660 
KLNWQKLPSN VARERNSMWA TLGSPCTAAV EPDFSSIEQL FSFPTAKPKE PSAAPARKEP 

       670        680        690        700        710        720 
KEVTFLDSKK SLNLNIFLKQ FKCSNEEVTS MIQAGDTSKF DVEVLKQLLK LLPEKHEIEN 

       730        740        750        760        770        780 
LRAFTEERAK LSNADQFYVL LLDIPCYPLR VECMMLCEGT AIVLDMVRPK AQLVLTACES 

       790        800        810        820        830        840 
LLTSQRLPVF CQLILKIGNF LNYGSHTGDA DGFKISTLLK LTETKSQQSR VTLLHHVLEE 

       850        860        870        880        890        900 
VEKSHPDLLQ LSRDLEPPSQ AAGINVEIIH SEASANLKKL LEAERKVSAS IPEVQKQYAE 

       910        920        930        940        950        960 
RLQASIEASQ ELDKVFDAIE QKKLELADYL CEDPQQLSLE DTFSTMKTFR DLFTRALKEN 

       970        980        990       1000       1010       1020 
KDRKEQMAKA ERRKQQLAEE EARRPRDEDG KPIRKGPGKQ EEVCVIDALL ADIRKGFQLR 

      1030       1040       1050       1060       1070       1080 
KTARGRGDTE ASGRVAPTDP PKATEPATAS NPTQGTNHPA SEPLDTTAAD EPQGWDLVDA 

      1090       1100       1110       1120       1130       1140 
VTPSPQPSKE EDGPPALERR SSWYVDAIDF LDPEDTPDAQ PSEGVWPVTL GDGQALNPLE 

      1150       1160       1170       1180       1190       1200 
FSSNKPPGVK SSHQDATDPE ALWGVHQTEA DSTSEGPEDE AQRGQSTHLP RTGPGEDEDG 

      1210       1220       1230       1240       1250       1260 
EDTAPESALD TSLDRSFSED AVTDSSGSGT LPRVQGRVSK GTSKRRKKRP SRNQEEFVPD 

      1270 
SDDIKAKRLC VIQ 

« Hide

Isoform 2 [UniParc].

Checksum: CC8EEF55F65801CB
Show »

FASTA1,264137,496

References

« Hide 'large scale' references
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_940803.2. NM_198411.2.
UniGeneMm.250193.

3D structure databases

ProteinModelPortalQ0GNC1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid214049. 1 interaction.

PTM databases

PhosphoSiteQ0GNC1.

Proteomic databases

MaxQBQ0GNC1.
PaxDbQ0GNC1.
PRIDEQ0GNC1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID70435.
KEGGmmu:70435.

Organism-specific databases

CTD64423.
MGIMGI:1917685. Inf2.

Phylogenomic databases

eggNOGNOG149898.
HOGENOMHOG000113072.
HOVERGENHBG081794.
InParanoidQ0GNC1.
PhylomeDBQ0GNC1.

Gene expression databases

GenevestigatorQ0GNC1.

Family and domain databases

InterProIPR016024. 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]
PANTHERPTHR23213:SF5. PTHR23213:SF5. 1 hit.
PfamPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
PF02205. WH2. 1 hit.
[Graphical view]
SMARTSM00498. FH2. 1 hit.
SM00246. WH2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
PS51082. WH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio331621.
PROQ0GNC1.
SOURCESearch...

Entry information

Entry nameINF2_MOUSE
AccessionPrimary (citable) accession number: Q0GNC1
Secondary accession number(s): Q14C56, Q499F7, Q6P9T3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2006
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot