TMOD4_BOVIN
ID TMOD4_BOVIN Reviewed; 345 AA.
AC Q0VC48;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Tropomodulin-4;
DE AltName: Full=Skeletal muscle tropomodulin;
DE Short=Sk-Tmod;
GN Name=TMOD4;
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=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the N-terminus of tropomyosin and to actin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9NZQ9}. Note=In myofibrils with sarcomeric
CC structure, localizes to the pointed end of actin thin filaments.
CC {ECO:0000250|UniProtKB:Q9NZQ9}.
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; BC120356; AAI20357.1; -; mRNA.
DR RefSeq; NP_001068683.1; NM_001075215.1.
DR RefSeq; XP_005203909.1; XM_005203852.3.
DR AlphaFoldDB; Q0VC48; -.
DR SMR; Q0VC48; -.
DR STRING; 9913.ENSBTAP00000043640; -.
DR PaxDb; Q0VC48; -.
DR Ensembl; ENSBTAT00000046331; ENSBTAP00000043640; ENSBTAG00000018071.
DR GeneID; 505645; -.
DR KEGG; bta:505645; -.
DR CTD; 29765; -.
DR VEuPathDB; HostDB:ENSBTAG00000018071; -.
DR VGNC; VGNC:36137; TMOD4.
DR eggNOG; KOG3735; Eukaryota.
DR GeneTree; ENSGT00940000158734; -.
DR HOGENOM; CLU_031052_0_1_1; -.
DR InParanoid; Q0VC48; -.
DR OMA; SIIRFGY; -.
DR OrthoDB; 1025132at2759; -.
DR TreeFam; TF315841; -.
DR Reactome; R-BTA-390522; Striated Muscle Contraction.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000018071; Expressed in longissimus thoracis muscle and 103 other tissues.
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; IBA:GO_Central.
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: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; IPR030129; TMOD4.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR PANTHER; PTHR10901:SF9; PTHR10901:SF9; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..345
FT /note="Tropomodulin-4"
FT /id="PRO_0000281915"
FT REGION 42..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 39184 MW; 9C4BBE388C1B7ED2 CRC64;
MSSYQKELEK YRDIDEDEIL KTLSPEELEQ LDCELQEMDP ENMLLPAGLR QRDQTKKSPT
GPLDREALLQ YLEQQALEVK ERDDLVPFTG EKKGKPYIQP KREIPVEEQV TLEPELEEAL
AHATDAEMCD IAAILGMYTL MSNKQYYDAI CSGEICNTEG ISSVVQPDKY KPVPDEPPNP
TNIEEILKSV RSNDKEVEEV NLNNIQDIPI PMLTELCEAM KTNTHVRSFS LVATRSGDPV
ANAVADMLRE NRSLQSLNIE SNFISSTGLM AVLKAVRENA TLTELRVDNQ RQWPGDAVEM
EMATVLEQCP SIVRFGYHFT QQGPRARAAQ AMTRNNELRR QQKKR