ID   TPM4_HORSE              Reviewed;         248 AA.
AC   P02561;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tropomyosin alpha-4 chain;
DE   AltName: Full=Platelet beta tropomyosin;
DE   AltName: Full=Tropomyosin-4;
GN   Name=TPM4;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-248.
RX   PubMed=6852260; DOI=10.1016/0014-5793(83)80511-0;
RA   Lewis W.G., Cote G.P., Mak A.S., Smillie L.B.;
RT   "Amino acid sequence of equine platelet tropomyosin. Correlation with
RT   interaction properties.";
RL   FEBS Lett. 156:269-273(1983).
CC   -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
CC       Plays a central role, in association with the troponin complex, in the
CC       calcium dependent regulation of vertebrate striated muscle contraction.
CC       Smooth muscle contraction is regulated by interaction with caldesmon.
CC       In non-muscle cells is implicated in stabilizing cytoskeleton actin
CC       filaments. Binds calcium. {ECO:0000250|UniProtKB:P09495,
CC       ECO:0000250|UniProtKB:P67936}.
CC   -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC       beta (TPM2) chain. {ECO:0000250|UniProtKB:P09495}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P09495}. Note=Associates with F-actin stress
CC       fibers. {ECO:0000250|UniProtKB:P09495}.
CC   -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 2
CC       polypeptide chains. The sequence exhibits a prominent seven-residues
CC       periodicity.
CC   -!- MISCELLANEOUS: This protein can span only six actin monomers.
CC   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR   PIR; A02984; TMHOBP.
DR   AlphaFoldDB; P02561; -.
DR   SMR; P02561; -.
DR   STRING; 9796.ENSECAP00000047008; -.
DR   PaxDb; P02561; -.
DR   PeptideAtlas; P02561; -.
DR   PRIDE; P02561; -.
DR   InParanoid; P02561; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   Gene3D; 1.20.5.370; -; 1.
DR   InterPro; IPR000533; Tropomyosin.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Calcium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Metal-binding; Muscle protein; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P67936,
FT                   ECO:0000269|PubMed:6852260"
FT   CHAIN           2..248
FT                   /note="Tropomyosin alpha-4 chain"
FT                   /id="PRO_0000205634"
FT   REGION          16..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2..248
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        26..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P67936"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09495"
FT   MOD_RES         177
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P67936"
FT   MOD_RES         215
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P67936"
FT   MOD_RES         216
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P67936"
SQ   SEQUENCE   248 AA;  28523 MW;  5D5CDF6BF76BB2A8 CRC64;
     MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA ALNRRIQLVE
     EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE
     EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE
     KEDKYEEEIK LLSDKLKEAE TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ
     TLDELNCI