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O97162

- TPM_RHIMP

UniProt

O97162 - TPM_RHIMP

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Protein

Tropomyosin

Gene
N/A
Organism
Rhipicephalus microplus (Cattle tick) (Boophilus microplus)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli

Functioni

Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin
OrganismiRhipicephalus microplus (Cattle tick) (Boophilus microplus)
Taxonomic identifieri6941 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariParasitiformesIxodidaIxodoideaIxodidaeRhipicephalinaeRhipicephalusBoophilus

Pathology & Biotechi

Protein family/group databases

Allergomei7728. Boo m 7.
7729. Boo m 7.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284TropomyosinPRO_0000205677Add
BLAST

Proteomic databases

PRIDEiO97162.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO97162.
SMRiO97162. Positions 1-283.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 284284By similarityAdd
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.Curated

Keywords - Domaini

Coiled coil, Repeat

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

O97162-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAIKKKMQA MKLEKDNAVD RAETAEQQSR EAALRAEKAE EEVRSLQKKI
60 70 80 90 100
QQIENELDQV QEQLSQANSK LEEKDKALQA AEAEVAAHNR RIQLLEEDLE
110 120 130 140 150
RSEERLKIAT QKLEEASQAA DESERMRKML EHRSITDEER MDGLEGQLKE
160 170 180 190 200
ARTMAEDADR KYDEVARKLA MVEADLERAE ERAETGETKI VELEEELRVV
210 220 230 240 250
GNNLKSLEVS EEKALQKEET YEMQIRQMTN RLQEAEARAE FAERSVQKLQ
260 270 280
KEVDRLEDEL VQEKEKYKAI SDELDQTFSE LTGY
Length:284
Mass (Da):33,002
Last modified:May 1, 1999 - v1
Checksum:iDFFEA6828BCD73E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124514 mRNA. Translation: AAD17324.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124514 mRNA. Translation: AAD17324.1 .

3D structure databases

ProteinModelPortali O97162.
SMRi O97162. Positions 1-283.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 7728. Boo m 7.
7729. Boo m 7.0101.

Proteomic databases

PRIDEi O97162.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

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

Publicationsi

  1. Johnson C.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiTPM_RHIMP
AccessioniPrimary (citable) accession number: O97162
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 1999
Last modified: October 1, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3