TPM4_PIG
ID TPM4_PIG Reviewed; 248 AA.
AC P67937; P07226; Q15659; Q9BU85; Q9H8Q3;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tropomyosin alpha-4 chain;
DE AltName: Full=Tropomyosin-4;
GN Name=TPM4;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Smooth muscle;
RX PubMed=14582535; DOI=10.1078/0171-9335-00333;
RA Abouhamed M., Reichenberg S., Robenek H., Plenz G.;
RT "Tropomyosin 4 expression is enhanced in dedifferentiating smooth muscle
RT cells in vitro and during atherogenesis.";
RL Eur. J. Cell Biol. 82:473-482(2003).
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 -!- DEVELOPMENTAL STAGE: Expression is increased in smooth muscle cells
CC during dedifferentiation from the contractile to the synthetic
CC phenotype. {ECO:0000269|PubMed:14582535}.
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 -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; AF087679; AAC61744.1; -; mRNA.
DR RefSeq; NP_999500.1; NM_214335.1.
DR AlphaFoldDB; P67937; -.
DR SMR; P67937; -.
DR STRING; 9823.ENSSSCP00000014722; -.
DR PaxDb; P67937; -.
DR PeptideAtlas; P67937; -.
DR PRIDE; P67937; -.
DR Ensembl; ENSSSCT00000015127; ENSSSCP00000014722; ENSSSCG00000013849.
DR Ensembl; ENSSSCT00015073818; ENSSSCP00015029640; ENSSSCG00015053903.
DR Ensembl; ENSSSCT00025012833; ENSSSCP00025005056; ENSSSCG00025009586.
DR Ensembl; ENSSSCT00035052009; ENSSSCP00035020889; ENSSSCG00035039121.
DR Ensembl; ENSSSCT00040097007; ENSSSCP00040043200; ENSSSCG00040070474.
DR Ensembl; ENSSSCT00045053574; ENSSSCP00045037251; ENSSSCG00045030931.
DR Ensembl; ENSSSCT00050099870; ENSSSCP00050043254; ENSSSCG00050073083.
DR Ensembl; ENSSSCT00055049334; ENSSSCP00055039415; ENSSSCG00055024068.
DR Ensembl; ENSSSCT00060034836; ENSSSCP00060014896; ENSSSCG00060025616.
DR Ensembl; ENSSSCT00065001791; ENSSSCP00065000573; ENSSSCG00065001341.
DR Ensembl; ENSSSCT00070041242; ENSSSCP00070034624; ENSSSCG00070020680.
DR GeneID; 397608; -.
DR KEGG; ssc:397608; -.
DR CTD; 7171; -.
DR VGNC; VGNC:94339; TPM4.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_3_0_1; -.
DR InParanoid; P67937; -.
DR OMA; EDKCKQM; -.
DR OrthoDB; 1576041at2759; -.
DR TreeFam; TF351519; -.
DR Reactome; R-SSC-390522; Striated Muscle Contraction.
DR Reactome; R-SSC-445355; Smooth Muscle Contraction.
DR Reactome; R-SSC-9013424; RHOV GTPase cycle.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Chromosome 2.
DR Bgee; ENSSSCG00000013849; Expressed in lung and 43 other tissues.
DR ExpressionAtlas; P67937; baseline and differential.
DR Genevisible; P67937; SS.
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 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Calcium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Metal-binding; Muscle protein; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P67936"
FT CHAIN 2..248
FT /note="Tropomyosin alpha-4 chain"
FT /id="PRO_0000205637"
FT REGION 15..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; 28522 MW; 5D5CDF6BF76552A8 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
TLNELNCI
