ID   INF2_XENLA              Reviewed;        1099 AA.
AC   Q6NTV6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Inverted formin-2;
GN   Name=inf2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR   EMBL; BC068848; AAH68848.1; -; mRNA.
DR   RefSeq; NP_001084562.1; NM_001091093.1.
DR   AlphaFoldDB; Q6NTV6; -.
DR   SMR; Q6NTV6; -.
DR   IntAct; Q6NTV6; 1.
DR   MINT; Q6NTV6; -.
DR   DNASU; 414513; -.
DR   GeneID; 414513; -.
DR   KEGG; xla:414513; -.
DR   CTD; 414513; -.
DR   Xenbase; XB-GENE-5862221; inf2.S.
DR   OrthoDB; 1204639at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 414513; Expressed in stomach and 17 other tissues.
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   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   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   2: Evidence at transcript level;
KW   Actin-binding; Coiled coil; Reference proteome.
FT   CHAIN           1..1099
FT                   /note="Inverted formin-2"
FT                   /id="PRO_0000259891"
FT   DOMAIN          1..330
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT   DOMAIN          426..569
FT                   /note="FH1"
FT   DOMAIN          621..1009
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   DOMAIN          1037..1052
FT                   /note="WH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT   REGION          348..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1000..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1064..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          907..1019
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        366..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..509
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1099 AA;  121481 MW;  7CF57CE48928CE85 CRC64;
     MSLTEGAHTK WGVLKQKLGP QDPDQIEGNL ENADPELCIR LLQIPSVVNY SGLKKRLESS
     DDEWMCQFLE LSGLDLLLEA LDRLSGRGVA RIADALLQLT CINCVRTLMN SHKGIEYIVN
     NEGYVRKLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHAL CLDALEHYKV VKNQQYRFSV
     ITNELSSSDN VPYMVTLLSV INAIIFGTEE LRNRVQLRNE FIGLQLLDLL TKLRDLEDED
     LLIQALVFEE AKSEDEEELL KIYGGINMNN HQEVFSTLFN KVSCSPLSVQ LLSILQGLLQ
     LDQSHPTSPL LWEALEVLVN RAVLLADDCQ NNNVEEVMDR LVTSKKLSSK EKRKTDKCTN
     KVNKSIQTDK PKEESCEGKT VKKDPVSSGI PADSLQLLDA LLAPPTKEDS PACITPLHTH
     LSGELTCSSV LPSPPSPLVP NADERISSSS SPLPPPPPPL PGTELSPPPP GMVALSLPPP
     PPPLPGMGGM LPPPPPPLPG MGGMLPTPPP PPLPGMGGML PPPPPPLPGM GGMLPPPPPP
     LPGMGGMLPP PPPPLPGMGG MLPPPPPLPG MGGMLPPPPP PLPGMGGMPP PPPPMPGMGT
     FTDEVVVARV DYSLGYLPKA FLKVNKPTLK MKKLNWQKIP PNVIKDSHSM WASASSIEDT
     VEPNYSSIEQ LFCLPQAAVK ESAVPVKKPP KEITFLDSKK NLNLNIFLKQ FKCPNKEVIE
     LIEKGDRSRF DIEILKQFLK LLPEKHEVEN LKSYQEDKAK LSNADQFYLL LLGVPCYQLR
     IECMLICEEI NLMIDMIRPR AKVVSSACDD IISSHRLPLF CQLILKVGNF LNYGSHTGNA
     NGFKISTLLK LTETRANQTR ITLLHHILEE IEHNHTDLLQ LPTDLENVST VAGINIENMY
     TETSGNLKKL RDLQNKISTA ATDVKEQYEK SIQDCMDTLK ELEEQLTDIS QKKVKLADYL
     CEDPTKLSLE ETFSTMKAFR ELFLKAKKDN KDRKEQAVKA EKRKQQIADE ETKRQKGENG
     KIIRKGAAKL EEGCIIDDLL ADIKKGFQLR KTAKTKTKAD ACPKTLSSET NRTDIQHVGK
     RPEVPPVHPQ RKIIILKRQ