TPM3_BOVIN
ID TPM3_BOVIN Reviewed; 284 AA.
AC Q5KR47; Q32PI2;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Tropomyosin alpha-3 chain;
DE AltName: Full=Gamma-tropomyosin;
DE AltName: Full=Tropomyosin-3;
GN Name=TPM3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RA Oe M., Nakajima I., Muroya S., Chikuni K.;
RT "Bovine tropomyosin isoforms.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC beta (TPM2) chain. Interacts with TMOD1. {ECO:0000250|UniProtKB:P04692,
CC ECO:0000250|UniProtKB:P06753}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Skeletal muscle;
CC IsoId=Q5KR47-1; Sequence=Displayed;
CC Name=2; Synonyms=Cytoskeletal;
CC IsoId=Q5KR47-2; Sequence=VSP_026081, VSP_026082, VSP_026083;
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 -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; AB198072; BAD86592.1; -; mRNA.
DR EMBL; BC108106; AAI08107.1; -; mRNA.
DR RefSeq; NP_001011674.1; NM_001011674.1. [Q5KR47-1]
DR RefSeq; XP_005203687.1; XM_005203630.3. [Q5KR47-1]
DR RefSeq; XP_005203696.1; XM_005203639.3. [Q5KR47-2]
DR AlphaFoldDB; Q5KR47; -.
DR SMR; Q5KR47; -.
DR STRING; 9913.ENSBTAP00000013077; -.
DR PaxDb; Q5KR47; -.
DR PeptideAtlas; Q5KR47; -.
DR PRIDE; Q5KR47; -.
DR Ensembl; ENSBTAT00000013077; ENSBTAP00000013077; ENSBTAG00000033217. [Q5KR47-1]
DR Ensembl; ENSBTAT00000047197; ENSBTAP00000044420; ENSBTAG00000033217. [Q5KR47-2]
DR GeneID; 497019; -.
DR KEGG; bta:497019; -.
DR CTD; 7170; -.
DR VEuPathDB; HostDB:ENSBTAG00000033217; -.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_0_0_1; -.
DR InParanoid; Q5KR47; -.
DR OMA; XKCSELE; -.
DR OrthoDB; 1576041at2759; -.
DR TreeFam; TF351519; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000033217; Expressed in gluteus medius and 104 other tissues.
DR ExpressionAtlas; Q5KR47; baseline and differential.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; Muscle protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin alpha-3 chain"
FT /id="PRO_0000289991"
FT REGION 1..43
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:0000250|UniProtKB:P58776"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58774"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06753"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21107"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21107"
FT VAR_SEQ 1..80
FT /note="MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKG
FT TEDELDKYSEALKDAQEKLELAEKKAAD -> MAGITTIEAVKRKIQVLQQQADDAEER
FT AERLQREVEGERRAREQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026081"
FT VAR_SEQ 189..211
FT /note="KCSELEEELKNVTNNLKSLEAQA -> RCREMDEQIRLMDQNLKCLSAAE
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026082"
FT VAR_SEQ 259..284
FT /note="ELYAQKLKYKAISEELDHALNDMTSI -> KLKCTKEEHLCTQRMLDQTLLD
FT LNEM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026083"
FT INIT_MET Q5KR47-2:1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT MOD_RES Q5KR47-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
FT MOD_RES Q5KR47-2:228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 284 AA; 32819 MW; A3BCE715565DABBD CRC64;
MEAIKKKMQM LKLDKENALD RAEQAEAEQK QAEERSKQLE DELAAMQKKL KGTEDELDKY
SEALKDAQEK LELAEKKAAD AEAEVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ENRALKDEEK MELQEIQLKE AKHIAEEADR KYEEVARKLV IIEGDLERTE
ERAELAESKC SELEEELKNV TNNLKSLEAQ AEKYSQKEDK YEEEIKILTD KLKEAETRAE
FAERSVAKLE KTIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
