ID   TMOD1_RAT               Reviewed;         359 AA.
AC   P70567;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Tropomodulin-1;
DE   AltName: Full=Erythrocyte tropomodulin;
DE            Short=E-Tmod;
GN   Name=Tmod1; Synonyms=Tmod;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=8886980; DOI=10.1242/jcs.109.9.2299;
RA   Watakabe A., Kobayashi R., Helfman D.M.;
RT   "N-tropomodulin: a novel isoform of tropomodulin identified as the major
RT   binding protein to brain tropomyosin.";
RL   J. Cell Sci. 109:2299-2310(1996).
CC   -!- FUNCTION: Blocks the elongation and depolymerization of the actin
CC       filaments at the pointed end. The Tmod/TM complex contributes to the
CC       formation of the short actin protofilament, which in turn defines the
CC       geometry of the membrane skeleton (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the N-terminus of tropomyosin and to actin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P28289}. Note=In myofibrils with sarcomeric
CC       structure, localizes to the pointed end of actin thin filaments.
CC       {ECO:0000250|UniProtKB:P28289}.
CC   -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR   EMBL; U59241; AAC52855.1; -; mRNA.
DR   AlphaFoldDB; P70567; -.
DR   SMR; P70567; -.
DR   STRING; 10116.ENSRNOP00000013228; -.
DR   PaxDb; P70567; -.
DR   PRIDE; P70567; -.
DR   UCSC; RGD:3874; rat.
DR   RGD; 3874; Tmod1.
DR   eggNOG; KOG3735; Eukaryota.
DR   InParanoid; P70567; -.
DR   PhylomeDB; P70567; -.
DR   Reactome; R-RNO-390522; Striated Muscle Contraction.
DR   PRO; PR:P70567; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR   GO; GO:0005865; C:striated muscle thin filament; ISO:RGD.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005523; F:tropomyosin binding; IDA:RGD.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR   GO; GO:0070307; P:lens fiber cell development; ISO:RGD.
DR   GO; GO:0006936; P:muscle contraction; ISO:RGD.
DR   GO; GO:0030239; P:myofibril assembly; ISO:RGD.
DR   GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR004934; TMOD.
DR   InterPro; IPR030135; TMOD1.
DR   PANTHER; PTHR10901; PTHR10901; 1.
DR   PANTHER; PTHR10901:SF8; PTHR10901:SF8; 1.
DR   Pfam; PF03250; Tropomodulin; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..359
FT                   /note="Tropomodulin-1"
FT                   /id="PRO_0000186130"
FT   REGION          36..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          39..138
FT                   /note="Tropomyosin-binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   359 AA;  40480 MW;  0FAC73649C20591F CRC64;
     MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ KDQTTKAPTG
     PFKREELLDH LEKQAKEFKD REDLVPYTGE KRGKIWVPKQ KPMDPVLESV TLEPELEEAL
     ANASDAELCD IAAILGMHTL MSNQQYYQAL GSSSIVNKEG LNSVIKPTQY KPVPDEEPNP
     TDVEETLERI KNNDPELEEV NLNNIRNIPI PTLKAYAESL KENSYVKKFS IVGTRSNDPV
     AFALAEMLKV NKVLKTLNVE SNFISGAGIL CLVEALPHNT SLVELKIDNQ SQPLGNKVEM
     EIVNMLEKNT TLLKFGYHFT QQGPRLRASN AMMNNNDLVR KRRLADLTGP IIPKCRSGV