ID E9QLA5_MOUSE Unreviewed; 1271 AA.
AC E9QLA5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Inverted formin, FH2 and WH2 domain containing {ECO:0000313|Ensembl:ENSMUSP00000098591.3};
GN Name=Inf2 {ECO:0000313|Ensembl:ENSMUSP00000098591.3,
GN ECO:0000313|MGI:MGI:1917685};
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 {ECO:0000313|Ensembl:ENSMUSP00000098591.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [2] {ECO:0007829|PubMed:19144319}
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 [3] {ECO:0000313|Ensembl:ENSMUSP00000098591.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000098591.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [5] {ECO:0000313|Ensembl:ENSMUSP00000098591.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000098591.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; NP_940803.2; NM_198411.2.
DR AlphaFoldDB; E9QLA5; -.
DR SMR; E9QLA5; -.
DR EPD; E9QLA5; -.
DR jPOST; E9QLA5; -.
DR MaxQB; E9QLA5; -.
DR PeptideAtlas; E9QLA5; -.
DR ProteomicsDB; 357501; -.
DR Antibodypedia; 14838; 219 antibodies from 28 providers.
DR DNASU; 70435; -.
DR Ensembl; ENSMUST00000101029.4; ENSMUSP00000098591.3; ENSMUSG00000037679.10.
DR GeneID; 70435; -.
DR KEGG; mmu:70435; -.
DR UCSC; uc007pes.1; mouse.
DR AGR; MGI:1917685; -.
DR CTD; 64423; -.
DR MGI; MGI:1917685; Inf2.
DR VEuPathDB; HostDB:ENSMUSG00000037679; -.
DR GeneTree; ENSGT00940000155691; -.
DR HOGENOM; CLU_005383_1_0_1; -.
DR OMA; MVCSQQY; -.
DR PhylomeDB; E9QLA5; -.
DR TreeFam; TF338399; -.
DR BioGRID-ORCS; 70435; 3 hits in 79 CRISPR screens.
DR ChiTaRS; Inf2; mouse.
DR Proteomes; UP000000589; Chromosome 12.
DR Bgee; ENSMUSG00000037679; Expressed in gastrula and 223 other cell types or tissues.
DR ExpressionAtlas; E9QLA5; baseline and differential.
DR Genevisible; E9QLA5; MM.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0090140; P:regulation of mitochondrial fission; IEA:Ensembl.
DR CDD; cd22061; WH2_INF2; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; INVERTED FORMIN-2; 1.
DR PANTHER; PTHR46345:SF5; INVERTED FORMIN-2; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF02205; WH2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:E9QLA5,
KW ECO:0007829|MaxQB:E9QLA5};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 1..330
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 587..977
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1005..1020
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
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..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 138364 MW; 1705C54B27D54A14 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 LPGMCPVPPP
PPLPRAGQIP PPPPLPGFSV PSMMGGVEEI IVAQVDHSLG SAWVPSHRRV NPPTLRMKKL
NWQKLPSNVA RERNSMWATL GSPCTAAVEP DFSSIEQLFS FPTAKPKEPS AAPARKEPKE
VTFLDSKKSL NLNIFLKQFK CSNEEVTSMI QAGDTSKFDV EVLKQLLKLL PEKHEIENLR
AFTEERAKLS NADQFYVLLL DIPCYPLRVE CMMLCEGTAI VLDMVRPKAQ LVLTACESLL
TSQRLPVFCQ LILKIGNFLN YGSHTGDADG FKISTLLKLT ETKSQQSRVT LLHHVLEEVE
KSHPDLLQLS RDLEPPSQAA GINVEIIHSE ASANLKKLLE AERKVSASIP EVQKQYAERL
QASIEASQEL DKVFDAIEQK KLELADYLCE DPQQLSLEDT FSTMKTFRDL FTRALKENKD
RKEQMAKAER RKQQLAEEEA RRPRDEDGKP IRKGPGKQEE VCVIDALLAD IRKGFQLRKT
ARGRGDTEAS GRVAPADPPK ATEPATASNP TQGTNHPASE PLDTTAADEP QGWDLVDAVT
PSPQPSKEED GPPALERRSS WYVDAIDFLD PEDTPDAQPS EGVWPVTLGD GQALNPLEFS
SNKPPGVKSS HQDATDPEAL WGVHRTEADS TSEGPEDEAQ RGQSTHLPRT GPGEDEDGED
TAPESALDTS LDRSFSEDAV TDSSGSGTLP RVQGRVSKGT SKRRKKRPSR NQEEFVPDSD
DIKAKRLCVI Q
//