TMOD_CAEEL
ID TMOD_CAEEL Reviewed; 392 AA.
AC O01479; Q95Q88;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Tropomodulin;
DE AltName: Full=Tmod-like protein;
DE Short=cTmd1;
DE AltName: Full=Uncoordinated protein 94;
GN Name=unc-94; Synonyms=tmd-1; ORFNames=C06A5.7;
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], AND ALTERNATIVE SPLICING.
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 [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 199-392.
RX PubMed=15211521; DOI=10.1002/prot.10597;
RA Lu S., Symersky J., Li S., Carson M., Chen L., Meehan E., Luo M.;
RT "Structural genomics of Caenorhabditis elegans: crystal structure of the
RT tropomodulin C-terminal domain.";
RL Proteins 56:384-386(2004).
CC -!- FUNCTION: Acts as the pointed end capping protein which maintains the
CC length and dynamics of the actin filament. Blocks the elongation and
CC depolymerization of the actin filaments at the pointed end (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the N-terminus of actin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O01479-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O01479-2; Sequence=VSP_016398, VSP_016399;
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; FO080102; CCD61217.1; -; Genomic_DNA.
DR EMBL; FO080102; CCD61218.1; -; Genomic_DNA.
DR PIR; T25521; T25521.
DR RefSeq; NP_491734.1; NM_059333.3.
DR RefSeq; NP_491735.1; NM_059334.3. [O01479-2]
DR PDB; 1PGV; X-ray; 1.80 A; A=199-392.
DR PDBsum; 1PGV; -.
DR AlphaFoldDB; O01479; -.
DR SMR; O01479; -.
DR BioGRID; 37729; 9.
DR STRING; 6239.C06A5.7b; -.
DR EPD; O01479; -.
DR PaxDb; O01479; -.
DR PeptideAtlas; O01479; -.
DR EnsemblMetazoa; C06A5.7a.1; C06A5.7a.1; WBGene00006823. [O01479-1]
DR EnsemblMetazoa; C06A5.7a.2; C06A5.7a.2; WBGene00006823. [O01479-1]
DR EnsemblMetazoa; C06A5.7b.1; C06A5.7b.1; WBGene00006823. [O01479-2]
DR GeneID; 172275; -.
DR CTD; 172275; -.
DR WormBase; C06A5.7a; CE29023; WBGene00006823; unc-94. [O01479-1]
DR WormBase; C06A5.7b; CE29024; WBGene00006823; unc-94. [O01479-2]
DR eggNOG; KOG3735; Eukaryota.
DR GeneTree; ENSGT00940000169280; -.
DR InParanoid; O01479; -.
DR OMA; FHAENQR; -.
DR OrthoDB; 1025132at2759; -.
DR PhylomeDB; O01479; -.
DR EvolutionaryTrace; O01479; -.
DR PRO; PR:O01479; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006823; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0005865; C:striated muscle thin filament; IDA:WormBase.
DR GO; GO:1990357; C:terminal web; IDA:WormBase.
DR GO; GO:0051015; F:actin filament binding; IC:WormBase.
DR GO; GO:0005523; F:tropomyosin binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0071689; P:muscle thin filament assembly; IMP:WormBase.
DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0051694; P:pointed-end actin filament capping; IDA:WormBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:WormBase.
DR DisProt; DP02982; -.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR004934; TMOD.
DR InterPro; IPR030137; TMOD_invertebrate.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR PANTHER; PTHR10901:SF6; PTHR10901:SF6; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..392
FT /note="Tropomodulin"
FT /id="PRO_0000186138"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..7
FT /note="MSQAKTD -> MSNMEPPPPMFPRSRIYHS (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_016398"
FT VAR_SEQ 39..41
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_016399"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:1PGV"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1PGV"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:1PGV"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1PGV"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:1PGV"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:1PGV"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1PGV"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1PGV"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:1PGV"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:1PGV"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1PGV"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:1PGV"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1PGV"
FT HELIX 364..385
FT /evidence="ECO:0007829|PDB:1PGV"
SQ SEQUENCE 392 AA; 44398 MW; E6C363F21FBF1D53 CRC64;
MSQAKTDYYS EEKTFSAPSA NSQQGTQLPS KVYNKGLKDL EDNDIEGLLS SLSIDELEDL
NNDFDPDNSM LPPSQRCRDQ TDKEPTGPYK RDNLLKFLED KAKTEKDWED VCPYTPGQKR
GKVYDSDSGR NSEEPENGKM EMPIEIDLDD DEEELECALV TAPEKDLVDL AGILGMHNVL
NQPQYYNALK GKTQDESTGT TFNGIMQSYV PRIVPDEPDN DTDVESCINR LREDDTDLKE
VNINNMKRVS KERIRSLIEA ACNSKHIEKF SLANTAISDS EARGLIELIE TSPSLRVLNV
ESNFLTPELL ARLLRSTLVT QSIVEFKADN QRQSVLGNQV EMDMMMAIEE NESLLRVGIS
FASMEARHRV SEALERNYER VRLRRLGKDP NV
