TPM_PSOOV
ID TPM_PSOOV Reviewed; 284 AA.
AC Q3BJY7;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Tropomyosin {ECO:0000303|PubMed:15679630, ECO:0000303|PubMed:16817997};
DE AltName: Full=PoTRO {ECO:0000303|PubMed:16817997};
DE AltName: Allergen=Pso o 10.0101 {ECO:0000305};
OS Psoroptes ovis (Sheep scab mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Psoroptidae; Psoroptes.
OX NCBI_TaxID=83912 {ECO:0000312|EMBL:CAJ38272.1};
RN [1] {ECO:0000312|EMBL:CAJ38272.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=16817997; DOI=10.1017/s0031182006000631;
RA Nisbet A.J., MacKellar A., Wright H.W., Brennan G.P., Chua K.Y., Cheong N.,
RA Thomas J.E., Huntley J.F.;
RT "Molecular characterization, expression and localization of tropomyosin and
RT paramyosin immunodominant allergens from sheep scab mites (Psoroptes
RT ovis).";
RL Parasitology 133:515-523(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX PubMed=15679630; DOI=10.1111/j.0141-9838.2004.00717.x;
RA Huntley J.F., Machell J., Nisbet A.J., Van den Broek A., Chua K.Y.,
RA Cheong N., Hales B.J., Thomas W.R.;
RT "Identification of tropomyosin, paramyosin and apolipophorin/vitellogenin
RT as three major allergens of the sheep scab mite, Psoroptes ovis.";
RL Parasite Immunol. 26:335-342(2004).
CC -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC a central role in the calcium dependent regulation of muscle
CC contraction. {ECO:0000250|UniProtKB:Q22866}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A2V735}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, but especially prevalent in the
CC anterior muscle bundles associated with legs. Expression in the mid and
CC posterior regions is probably related to the numerous, small muscle
CC bundles associated with the digestive and reproductive systems (at
CC protein level). {ECO:0000269|PubMed:16817997}.
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. {ECO:0000305}.
CC -!- ALLERGEN: Causes an allergic reaction in sheep (PubMed:16817997,
CC PubMed:15679630). Binds to IgE of sheep allergic to scab mites
CC (PubMed:15679630). {ECO:0000269|PubMed:15679630,
CC ECO:0000269|PubMed:16817997}.
CC -!- SIMILARITY: Belongs to the tropomyosin family.
CC {ECO:0000255|RuleBase:RU004515, ECO:0000305}.
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DR EMBL; AM114276; CAJ38272.1; -; mRNA.
DR AlphaFoldDB; Q3BJY7; -.
DR SMR; Q3BJY7; -.
DR Allergome; 2488; Pso o 10.
DR Allergome; 4108; Pso o 10.0101.
DR GO; GO:0043292; C:contractile fiber; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006937; P:regulation of muscle contraction; ISS:UniProtKB.
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 Allergen; Coiled coil; Muscle protein; Repeat.
FT CHAIN 1..284
FT /note="Tropomyosin"
FT /id="PRO_0000447465"
FT COILED 1..273
FT /evidence="ECO:0000255"
SQ SEQUENCE 284 AA; 32914 MW; CE78E8EB8F348782 CRC64;
MEAIKKKMQA MKLEKDNAID RAEIAEQKAR DANLRAEKSE EEVRGLQKKI QQIENELDQV
QEQLSAANTK LEEKKKALQT AEGDVAALNR RIQLIEEDLE RSEERLKIAT AKLEEASQSA
DESERMRKML EHRSITDEER MDGLENQLKE ARMMAEDADR KYDEVARKLA MVEADLERAE
ERAETGESKI VELEEELRVV GNNLKSLEVS EEKAQQREEA HEQQIRIMTA KLKEAEARAE
FAERSVQKLQ KEVDRLEDEL VHEKEKYKSI SDELDQTFAE LTGY
