P58772 (TPM1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tropomyosin alpha-1 chain

Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1

Gene names

Name:	TPM1
Synonyms:	TPMA

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Subunit structure	Heterodimer of an alpha and a beta chain By similarity. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG By similarity.
Subcellular location	Cytoplasm › cytoskeleton.
Domain	The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.
Post-translational modification	Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells By similarity. Ref.5
Sequence similarities	Belongs to the tropomyosin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	Actin-binding
Molecular function	Muscle protein
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms may be produced.

Isoform 1 (identifier: P58772-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 284

284

Tropomyosin alpha-1 chain

PRO_0000205623

Regions

Coiled coil

1 – 284

284

By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.3

Modified residue

283

1

Phosphoserine; by DAPK1 Ref.5

Cross-link

77

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

1

.

.

.

284

Helix Strand Turn

Details...

Helix

176 – 273

98

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: E25609F597A72F4D	FASTA	284	32,681
	10 20 30 40 50 60 MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY 70 80 90 100 110 120 SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 130 140 150 160 170 180 DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE 190 200 210 220 230 240 ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE 250 260 270 280 FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI

References

[1]	"The amino acid sequence of rabbit skeletal alpha-tropomyosin. The NH2-terminal half and complete sequence." Stone D., Smillie L.B. J. Biol. Chem. 253:1137-1148(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Skeletal muscle.
[2]	"The amino acid sequence of rabbit cardiac tropomyosin." Lewis W.G., Smillie L.B. J. Biol. Chem. 255:6854-6859(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Heart muscle.
[3]	"Rabbit skeletal muscle alpha alpha-tropomyosin expressed in baculovirus-infected insect cells possesses the authentic N-terminus structure and functions." Kluwe L., Maeda K., Miegel A., Fujita-Becker S., Maeda Y., Talbo G., Houthaeve T., Kellner R. J. Muscle Res. Cell Motil. 16:103-110(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New Zealand white. Tissue: Skeletal muscle.
[4]	"A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing." Putney S.D., Herlihy W.C., Schimmel P.R. Nature 302:718-721(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-146.
[5]	"Specific phosphorylation at serine-283 of alpha tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle." Mak A.S., Smillie L.B., Barany M. Proc. Natl. Acad. Sci. U.S.A. 75:3588-3592(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-283. Tissue: Skeletal muscle.
[6]	"Construction of an atomic model for tropomyosin and implications for interactions with actin." Phillips G.N. Jr. J. Mol. Biol. 192:128-131(1986) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (15 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S78854 mRNA. Translation: AAB34957.1.
V00892 mRNA. Translation: CAA24257.1.

PIR

TMRBA. I47056.

RefSeq

NP_001099158.1. NM_001105688.1.

UniGene

Ocu.3324.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D3E	X-ray	2.60	A/B/C/D	176-284	[»]
2EFR	X-ray	1.80	A/B/C/D	176-273	[»]
2EFS	X-ray	2.00	A/B/C/D	176-273	[»]
2TMA	X-ray	15.00	A/B	1-284	[»]
2W49	electron microscopy	35.00	A/B/C/T/U/V/W/X	8-284	[»]
2W4U	electron microscopy	35.00	A/B/C/T/U/V/W/X	8-284	[»]
2Z5H	X-ray	2.89	A/B/C/D/E/F/G/H	254-284	[»]
			I	1-24	[»]
2Z5I	X-ray	2.10	A/B/C/D/E/F/G/H	254-284	[»]
			I/J	1-24	[»]
4A7F	electron microscopy	7.70	B/H	98-233	[»]
4A7H	electron microscopy	7.80	B/H	98-233	[»]
4A7L	electron microscopy	8.10	B/H	98-233	[»]

ProteinModelPortal

P58772.

SMR

P58772. Positions 8-284.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46098N.

MINT

MINT-1500045.

Proteomic databases

PRIDE

P58772.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSOCUT00000030296; ENSOCUP00000015511; ENSOCUG00000014122.

GeneID

100125989.

Phylogenomic databases

eggNOG

NOG304012.

GeneTree

ENSGT00550000074494.

HOGENOM

HOG000231521.

HOVERGEN

HBG107404.

OrthoDB

EOG4TXBSM.

Family and domain databases

InterPro

IPR000533. Tropomyosin.
[Graphical view]

Pfam

PF00261. Tropomyosin. 1 hit.
[Graphical view]

PRINTS

PR00194. TROPOMYOSIN.

PROSITE

PS00326. TROPOMYOSIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P58772.

PMAP-CutDB

P58772.

Entry information

Entry name

TPM1_RABIT

Accession

Primary (citable) accession number: P58772
Secondary accession number(s): P02558, P46902, P99034

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program