TMOD1_BOVIN
ID TMOD1_BOVIN Reviewed; 359 AA.
AC A0JNC0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Tropomodulin-1;
DE AltName: Full=Erythrocyte tropomodulin;
DE Short=E-Tmod;
GN Name=TMOD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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. May play an important role in
CC regulating the organization of actin filaments by preferentially
CC binding to a specific tropomyosin isoform at its N-terminus (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the N-terminus of isoforms 2/3 of TPM3 and to actin.
CC {ECO:0000250}.
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; BC126605; AAI26606.1; -; mRNA.
DR RefSeq; NP_001073108.1; NM_001079640.1.
DR AlphaFoldDB; A0JNC0; -.
DR SMR; A0JNC0; -.
DR STRING; 9913.ENSBTAP00000019585; -.
DR PaxDb; A0JNC0; -.
DR PRIDE; A0JNC0; -.
DR Ensembl; ENSBTAT00000019585; ENSBTAP00000019585; ENSBTAG00000014719.
DR GeneID; 780784; -.
DR KEGG; bta:780784; -.
DR CTD; 7111; -.
DR VEuPathDB; HostDB:ENSBTAG00000014719; -.
DR VGNC; VGNC:36135; TMOD1.
DR eggNOG; KOG3735; Eukaryota.
DR GeneTree; ENSGT00940000158695; -.
DR HOGENOM; CLU_031052_0_0_1; -.
DR InParanoid; A0JNC0; -.
DR OMA; FHAENQR; -.
DR OrthoDB; 1025132at2759; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000014719; Expressed in oocyte and 104 other tissues.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
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_0000282313"
FT REGION 39..138
FT /note="Tropomyosin-binding"
FT /evidence="ECO:0000255"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 40459 MW; B8C637BD6C9D2FE5 CRC64;
MSYRRELEKY RDLDEDEILG GLTEEELRTL ENELDELDPD NALLPAGLRQ KDQTTKAPTG
PFRREELLDH LEKQAKEFKD REDLVPYTGE KRGKVWVPKQ KPMDPVLESV TLEPELEEAL
ANASDAELCD IAAILGMHTL MSNQQYYQAL GSSSIVNKEG LNSVIKPTQY KPVPDEEPNA
TDVEETLERI KNNDPKLEEV NLNNIRNIPI PTLKAYAEAL KENSYVKKFS IVGTRSNDPV
AFALAEMLKV NKVLKTLNVE SNFISGAGIL RLVEALPYNT SLVELKIDNQ SQPLGNKVEM
EIVSMLEKNA TLLKFGYHFT QQGPRLRASN AMMNNNDLVR KRRLADLTGP IIPKCRSGV