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P58772

- TPM1_RABIT

UniProt

P58772 - TPM1_RABIT

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Protein
Tropomyosin alpha-1 chain
Gene
TPM1, TPMA
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene namesi
Name:TPM1
Synonyms:TPMA
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Tropomyosin alpha-1 chain
PRO_0000205623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei283 – 2831Phosphoserine; by DAPK11 Publication

Post-translational modificationi

Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells By similarity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP58772.

Miscellaneous databases

PMAP-CutDBP58772.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi1172720. 1 interaction.
DIPiDIP-46098N.
IntActiP58772. 2 interactions.
MINTiMINT-1500045.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2423
Helixi176 – 27398

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D3EX-ray2.60A/B/C/D176-284[»]
2EFRX-ray1.80A/B/C/D176-273[»]
2EFSX-ray2.00A/B/C/D176-273[»]
2TMAX-ray15.00A/B1-284[»]
2W49electron microscopy35.00A/B/C/T/U/V/W/X8-284[»]
2W4Uelectron microscopy35.00A/B/C/T/U/V/W/X8-284[»]
2Z5HX-ray2.89A/B/C/D/E/F/G/H254-284[»]
I1-24[»]
2Z5IX-ray2.10A/B/C/D/E/F/G/H254-284[»]
I/J1-24[»]
4A7Felectron microscopy7.70B/H98-233[»]
4A7Helectron microscopy7.80B/H98-233[»]
4A7Lelectron microscopy8.10B/H98-233[»]
ProteinModelPortaliP58772.
SMRiP58772. Positions 8-284.

Miscellaneous databases

EvolutionaryTraceiP58772.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 284284 By similarity
Add
BLAST

Domaini

The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.

Sequence similaritiesi

Belongs to the tropomyosin family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG304012.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
OrthoDBiEOG7673C8.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms may be produced.

Isoform 1 (identifier: P58772-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL    50
KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD 100
RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE 150
AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV 200
TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE FAERSVTKLE 250
KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 284
Length:284
Mass (Da):32,681
Last modified:July 21, 1986 - v1
Checksum:iE25609F597A72F4D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S78854 mRNA. Translation: AAB34957.1.
V00892 mRNA. Translation: CAA24257.1.
PIRiI47056. TMRBA.
RefSeqiNP_001099158.1. NM_001105688.1. [P58772-1]
UniGeneiOcu.3324.

Genome annotation databases

GeneIDi100125989.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S78854 mRNA. Translation: AAB34957.1 .
V00892 mRNA. Translation: CAA24257.1 .
PIRi I47056. TMRBA.
RefSeqi NP_001099158.1. NM_001105688.1. [P58772-1 ]
UniGenei Ocu.3324.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P58772.
SMRi P58772. Positions 8-284.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1172720. 1 interaction.
DIPi DIP-46098N.
IntActi P58772. 2 interactions.
MINTi MINT-1500045.

Proteomic databases

PRIDEi P58772.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100125989.

Phylogenomic databases

eggNOGi NOG304012.
HOGENOMi HOG000231521.
HOVERGENi HBG107404.
OrthoDBi EOG7673C8.

Miscellaneous databases

EvolutionaryTracei P58772.
PMAP-CutDB P58772.

Family and domain databases

InterProi IPR000533. Tropomyosin.
[Graphical view ]
Pfami PF00261. Tropomyosin. 1 hit.
[Graphical view ]
PRINTSi PR00194. TROPOMYOSIN.
PROSITEi PS00326. TROPOMYOSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiTPM1_RABIT
AccessioniPrimary (citable) accession number: P58772
Secondary accession number(s): P02558, P46902, P99034
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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