INF2_XENTR
ID INF2_XENTR Reviewed; 1380 AA.
AC Q0IHV1;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Inverted formin-2;
GN Name=inf2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR EMBL; BC122958; AAI22959.1; -; mRNA.
DR RefSeq; NP_001072591.1; NM_001079123.1.
DR RefSeq; XP_012824085.1; XM_012968631.2.
DR RefSeq; XP_012824086.1; XM_012968632.2.
DR RefSeq; XP_012824087.1; XM_012968633.2.
DR RefSeq; XP_017951812.1; XM_018096323.1.
DR AlphaFoldDB; Q0IHV1; -.
DR SMR; Q0IHV1; -.
DR STRING; 8364.ENSXETP00000018819; -.
DR PaxDb; Q0IHV1; -.
DR PRIDE; Q0IHV1; -.
DR GeneID; 780046; -.
DR KEGG; xtr:780046; -.
DR CTD; 64423; -.
DR Xenbase; XB-GENE-5862185; inf2.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_005383_1_0_1; -.
DR InParanoid; Q0IHV1; -.
DR OMA; DHYKMVC; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; Q0IHV1; -.
DR TreeFam; TF326300; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
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: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 2: Evidence at transcript level;
KW Actin-binding; Coiled coil; Reference proteome.
FT CHAIN 1..1380
FT /note="Inverted formin-2"
FT /id="PRO_0000259892"
FT DOMAIN 1..330
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 432..592
FT /note="FH1"
FT DOMAIN 593..981
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1009..1024
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 341..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 879..930
FT /evidence="ECO:0000255"
FT COILED 956..991
FT /evidence="ECO:0000255"
FT COMPBIAS 367..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..541
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 151537 MW; 3314CA4E6848FB6B CRC64;
MSLKEGAHTK WGVLKQKLGP QDPEQIEGNM ENADPELCIR LLQIPSVVNY SGLKKRLESS
DDDWMVQFLE LSGLDLLLEA LDRLSGRGVA RIADALLQLT CINCVRTLMN SHRGIEYIVN
NEGYVRKLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHAL SLDALEHYKA VKNQQYRFSV
IMNELSTSDN VPYMVTLLSA INAIIFGTEE LRKRVQLRNE FIGLQLLDLL TKLRDLEDED
LLIQAIVFEE AKSEDEEELL KIYGGIDMNN HQEVFSTLFN KVSCSPLSVQ LLSVLQGLLH
LDQSHPSSPL LWEALDILVN RAVLLADDCQ NNNVEEVMDR LVTSKKHPSK EKRKPDKCTN
QVNKSIQTDK PKDESCEEKT VKKDPVSSGI PADSLQLSDA LLALPACVSP LHTPLSGDIT
SPSHFPSPPS PVVSNAIDRI STSSSLPPPL PPPLPGTELS LPPPPPPPLP GMGGISLTPP
PPPPLPGMGG MLPPPPPPLP GMGGMLPPPP PPLPGMGGML PPPPPPLPGM GGMLPPPPPP
LPGMGGMPPP PPPLPGMGGM PPPPPPMFGM GTFTDEVVVA RVDYSLGYLP KAYFKVNKPT
LKMKKLNWQK LPPNVINDTH SMWASASSSN DTPEPNYSSI EQLFCLPQAV AKEPAAPVKK
PPKEISFLDS KKNLNLNIFL KQFKCPNEEV IQLIEKGDRS RFDIEILKQF LKLLPEKHEV
ENLKSYQEDK AKLSNADQFY LLLLGIPCYQ LRIECMLICE EVNLMTDVLR PKAKVVSSAC
DDIISSHRLP LFCQLILKVG NFLNYGSHTG NANGFKIGTL LKLTETKANQ NRITLLHHIL
EEIEQNHTDL LQLPSDLENV STAAGINIEN MYSETSGNLK KLRDLQNKIS TAATDVKDQY
EKSIQECMDA LKEVEEQLTD ITQKKVKLAD YLCEDSAKLS LEETFSTMKA FRDLFLKAKK
DNKDRKEQAV KAEKRKKQLA DEEAKRQKGE NGKIIRKGAA KLEEGCIIDA LLADIKKGFQ
LRKTAKTKTE ADSCPKPVSS ETTGTDGTDV KHVDHVGILP QIKLDSSLNL DGTEQHKSKS
KDNCGENFDN KPVVIAPINL DTSACLMNIS EQNAKLPVSA LQEGANLKQN PDTFVKEQSA
IVTTESSTHN NIDGSSVDKC TLGQSQWPSE ISDEVDSKYH EMPMQVEHKE RAVEGKCSLP
KPSVLGTESS SNQNNALNEG SQQHHNNTAN ESLQQAQNSA LSEASQQSCC HTGIKGSPQF
QSSALNADSQ PSHTSVVGSA QAQRNELDDV ALQTRDTTVT EGSQVEEDKC NDEGYPEHKT
MGEHPLNSSS HSTTLQQSSE DGQKVKRGSS KHKKKRRSSK HGEEDGVDSP THKTRGCVVQ
