TPM1_RABIT
ID TPM1_RABIT Reviewed; 284 AA.
AC P58772; P02558; P46902; P99034;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Tropomyosin alpha-1 chain;
DE AltName: Full=Alpha-tropomyosin;
DE AltName: Full=Tropomyosin-1;
GN Name=TPM1; Synonyms=TPMA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Skeletal muscle;
RX PubMed=624724; DOI=10.1016/s0021-9258(17)38122-x;
RA Stone D., Smillie L.B.;
RT "The amino acid sequence of rabbit skeletal alpha-tropomyosin. The NH2-
RT terminal half and complete sequence.";
RL J. Biol. Chem. 253:1137-1148(1978).
RN [2]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Heart muscle;
RX PubMed=6993480; DOI=10.1016/s0021-9258(18)43652-6;
RA Lewis W.G., Smillie L.B.;
RT "The amino acid sequence of rabbit cardiac tropomyosin.";
RL J. Biol. Chem. 255:6854-6859(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT MET-1.
RC STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX PubMed=7622625; DOI=10.1007/bf00122528;
RA Kluwe L., Maeda K., Miegel A., Fujita-Becker S., Maeda Y., Talbo G.,
RA Houthaeve T., Kellner R.;
RT "Rabbit skeletal muscle alpha alpha-tropomyosin expressed in baculovirus-
RT infected insect cells possesses the authentic N-terminus structure and
RT functions.";
RL J. Muscle Res. Cell Motil. 16:103-110(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 103-146.
RX PubMed=6687628; DOI=10.1038/302718a0;
RA Putney S.D., Herlihy W.C., Schimmel P.R.;
RT "A new troponin T and cDNA clones for 13 different muscle proteins, found
RT by shotgun sequencing.";
RL Nature 302:718-721(1983).
RN [5]
RP PHOSPHORYLATION AT SER-283.
RC TISSUE=Skeletal muscle;
RX PubMed=278975; DOI=10.1073/pnas.75.8.3588;
RA Mak A.S., Smillie L.B., Barany M.;
RT "Specific phosphorylation at serine-283 of alpha tropomyosin from frog
RT skeletal and rabbit skeletal and cardiac muscle.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:3588-3592(1978).
RN [6]
RP SUBUNIT.
RX PubMed=23832280; DOI=10.1007/s10974-013-9353-x;
RA Janco M., Suphamungmee W., Li X., Lehman W., Lehrer S.S., Geeves M.A.;
RT "Polymorphism in tropomyosin structure and function.";
RL J. Muscle Res. Cell Motil. 34:177-187(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (15 ANGSTROMS).
RX PubMed=3820300; DOI=10.1016/0022-2836(86)90469-9;
RA Phillips G.N. Jr.;
RT "Construction of an atomic model for tropomyosin and implications for
RT interactions with actin.";
RL J. Mol. Biol. 192:128-131(1986).
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. {ECO:0000250|UniProtKB:P09493}.
CC -!- SUBUNIT: Homodimer (PubMed:23832280). Heterodimer of an alpha (TPM1,
CC TPM3 or TPM4) and a beta (TPM2) chain (By similarity). Interacts with
CC HRG (via the HRR domain); the interaction contributes to the
CC antiangiogenic properties of the histidine/proline-rich region (HRR) of
CC HRG (By similarity). Interacts (via N-terminus) with LMOD2 (via N-
CC terminus) and TMOD1 (via N-terminus) (By similarity).
CC {ECO:0000250|UniProtKB:P04268, ECO:0000250|UniProtKB:P04692,
CC ECO:0000250|UniProtKB:P09493, ECO:0000269|PubMed:23832280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress
CC fibers. {ECO:0000250|UniProtKB:P04692}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms may be produced.;
CC Name=1;
CC IsoId=P58772-1; Sequence=Displayed;
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 -!- PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress
CC and this phosphorylation enhances stress fiber formation in endothelial
CC cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; S78854; AAB34957.1; -; mRNA.
DR EMBL; V00892; CAA24257.1; -; mRNA.
DR PIR; I47056; TMRBA.
DR RefSeq; NP_001099158.1; NM_001105688.1. [P58772-1]
DR PDB; 2D3E; X-ray; 2.60 A; A/B/C/D=176-284.
DR PDB; 2EFR; X-ray; 1.80 A; A/B/C/D=176-273.
DR PDB; 2EFS; X-ray; 2.00 A; A/B/C/D=176-273.
DR PDB; 2TMA; X-ray; 15.00 A; A/B=1-284.
DR PDB; 2W49; EM; 35.00 A; A/B/C/T/U/V/W/X=8-284.
DR PDB; 2W4U; EM; 35.00 A; A/B/C/T/U/V/W/X=8-284.
DR PDB; 2Z5H; X-ray; 2.89 A; A/B/C/D/E/F/G/H=254-284, I=1-24.
DR PDB; 2Z5I; X-ray; 2.10 A; A/B/C/D/E/F/G/H=254-284, I/J=1-24.
DR PDB; 4A7F; EM; 7.70 A; B/H=98-233.
DR PDB; 4A7H; EM; 7.80 A; B/H=98-233.
DR PDB; 4A7L; EM; 8.10 A; B/H=98-233.
DR PDBsum; 2D3E; -.
DR PDBsum; 2EFR; -.
DR PDBsum; 2EFS; -.
DR PDBsum; 2TMA; -.
DR PDBsum; 2W49; -.
DR PDBsum; 2W4U; -.
DR PDBsum; 2Z5H; -.
DR PDBsum; 2Z5I; -.
DR PDBsum; 4A7F; -.
DR PDBsum; 4A7H; -.
DR PDBsum; 4A7L; -.
DR AlphaFoldDB; P58772; -.
DR SMR; P58772; -.
DR BioGRID; 1172720; 1.
DR DIP; DIP-46098N; -.
DR IntAct; P58772; 3.
DR MINT; P58772; -.
DR STRING; 9986.ENSOCUP00000012137; -.
DR iPTMnet; P58772; -.
DR PRIDE; P58772; -.
DR GeneID; 100125989; -.
DR KEGG; ocu:100125989; -.
DR CTD; 7168; -.
DR eggNOG; KOG1003; Eukaryota.
DR InParanoid; P58772; -.
DR EvolutionaryTrace; P58772; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; IMP:CAFA.
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:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0031013; F:troponin I binding; IPI:CAFA.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Muscle protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin alpha-1 chain"
FT /id="PRO_0000205623"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:624724,
FT ECO:0000269|PubMed:6993480, ECO:0000269|PubMed:7622625"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09493"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 283
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000269|PubMed:278975"
FT HELIX 2..24
FT /evidence="ECO:0007829|PDB:2Z5I"
FT HELIX 176..273
FT /evidence="ECO:0007829|PDB:2EFR"
SQ SEQUENCE 284 AA; 32681 MW; E25609F597A72F4D CRC64;
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY
SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
