FOZI1_CAEEL
ID FOZI1_CAEEL Reviewed; 732 AA.
AC P34489;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Formin-homology and zinc finger domains protein 1;
DE Flags: Precursor;
GN Name=fozi-1 {ECO:0000312|WormBase:K01B6.1};
GN ORFNames=K01B6.1 {ECO:0000312|WormBase:K01B6.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21307099; DOI=10.1242/dev.062240;
RA Tian C., Shi H., Colledge C., Stern M., Waterston R., Liu J.;
RT "The C. elegans SoxC protein SEM-2 opposes differentiation factors to
RT promote a proliferative blast cell fate in the postembryonic mesoderm.";
RL Development 138:1033-1043(2011).
CC -!- FUNCTION: Acts redundantly with hlh-1 to promote body wall muscle cell
CC and coelomocyte specification in postembryonic mesoderm progenitors,
CC probably through suppression of sem-2. {ECO:0000269|PubMed:21307099}.
CC -!- TISSUE SPECIFICITY: Transiently expressed in all mesoderm derived
CC progenitor body wall muscle cells before they differentiate.
CC {ECO:0000269|PubMed:21307099}.
CC -!- DEVELOPMENTAL STAGE: Expressed in sex myoblasts at the 16-M cell and
CC 18-M cell stages of mesoderm development in hermaphrodite larvae.
CC {ECO:0000269|PubMed:21307099}.
CC -!- DISRUPTION PHENOTYPE: Double RNAi-mediated knockdown with sem-2 results
CC in no sex myoblast production. {ECO:0000269|PubMed:21307099}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR EMBL; Z22174; CAA80128.1; -; Genomic_DNA.
DR PIR; S40759; S40759.
DR RefSeq; NP_499047.1; NM_066646.3.
DR AlphaFoldDB; P34489; -.
DR SMR; P34489; -.
DR BioGRID; 41506; 30.
DR DIP; DIP-27437N; -.
DR IntAct; P34489; 28.
DR STRING; 6239.K01B6.1; -.
DR EPD; P34489; -.
DR PaxDb; P34489; -.
DR EnsemblMetazoa; K01B6.1.1; K01B6.1.1; WBGene00010453.
DR EnsemblMetazoa; K01B6.1.2; K01B6.1.2; WBGene00010453.
DR EnsemblMetazoa; K01B6.1.3; K01B6.1.3; WBGene00010453.
DR UCSC; K01B6.1; c. elegans.
DR WormBase; K01B6.1; CE00238; WBGene00010453; fozi-1.
DR eggNOG; KOG1923; Eukaryota.
DR HOGENOM; CLU_372662_0_0_1; -.
DR InParanoid; P34489; -.
DR OMA; FAIHRMD; -.
DR OrthoDB; 601132at2759; -.
DR Reactome; R-CEL-5663220; RHO GTPases Activate Formins.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013106; RHOC GTPase cycle.
DR SignaLink; P34489; -.
DR PRO; PR:P34489; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010453; Expressed in larva and 3 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007501; P:mesodermal cell fate specification; IDA:UniProtKB.
DR GO; GO:0048337; P:positive regulation of mesodermal cell fate specification; IGI:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR043592; FMNL_animal.
DR PANTHER; PTHR45857; PTHR45857; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..732
FT /note="Formin-homology and zinc finger domains protein 1"
FT /id="PRO_0000065392"
FT DOMAIN 355..732
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 81848 MW; 1BB4719565E00C2B CRC64;
MMLASSAPTA PSLLPPSSQP SAATTRADDC SSSTSPTNTS ASDASMEMLT SLMNGAVAAA
AAPGNALVKQ ESPPLTTPPL FNPDLALLQF SQLFQAQQAM VQFHNQQKQQ QQIIQQQQQQ
QQQQQQNQNP SQSQSSSSDR KRSYPCTFQY CVICQKDVHS SKLPCHIRQC HVAKPMFQCP
ACDFTSTYSK NNVKSHMVSL HGLAGDPISY MDKYAGQVEE FMKLCFPNVR GRGRPMQGRS
SPKSPTSPTQ PGRRGSQASS LPSRRNTVSQ NDLLATLQQH QQQQAAFHPL RNLRFNPLQS
IFPAVLANNN NNSVLATNKH VNNFLIKQEE SEVPPITMPM QDLKTMLDAN SSPSPISLSS
SIIPIQPIKP GENAQPKYMK SLDWTILNDL QMKGTVFADC RSNMELYAEN IARKIENTKA
FQSFVLSDDM RTVVEEVRSR VSIQLFEVMF AIHRMDIKVL NQNLVDSLLQ IAPTNSDAQL
LRKMENLSDP NEEFLLGLTK IDHIEEKLET MKHMYRFPEQ VELLKENIIK YEIAVKVLSE
SRALRNVMQL VLAILNIGFF DDRQCLSING FSVSDISSIL STNTPSGQSV QSILVTILKD
EINLDLDELF GLIDVLEKIE NDDVNSVAQD LMVLDDKTVR AEKEMEHSGS NIPLSEFVEN
AKTISKERWE HFKSLKTSIE RLTIYLGSPL PRHQNLDAHS PFNNVLQMLR SLKTAIELDD
ASDDHHINVS SP
