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Database: UniProt
Entry: A0A3Q3RWK6_9TELE
LinkDB: A0A3Q3RWK6_9TELE
Original site: A0A3Q3RWK6_9TELE 
ID   A0A3Q3RWK6_9TELE        Unreviewed;       288 AA.
AC   A0A3Q3RWK6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Tropomyosin alpha-1 chain-like {ECO:0000313|Ensembl:ENSMAMP00000012005.2};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000012005.2, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000012005.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037240}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the tropomyosin family.
CC       {ECO:0000256|ARBA:ARBA00009036, ECO:0000256|RuleBase:RU004515}.
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DR   AlphaFoldDB; A0A3Q3RWK6; -.
DR   Ensembl; ENSMAMT00000012328.2; ENSMAMP00000012005.2; ENSMAMG00000020113.2.
DR   GeneTree; ENSGT01030000234542; -.
DR   Proteomes; UP000261640; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.170; -; 2.
DR   Gene3D; 1.20.5.340; -; 1.
DR   InterPro; IPR000533; Tropomyosin.
DR   PANTHER; PTHR19269; TROPOMYOSIN; 1.
DR   PANTHER; PTHR19269:SF38; TROPOMYOSIN ALPHA-3 CHAIN; 1.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640}.
FT   COILED          5..288
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   288 AA;  33131 MW;  A197070485CEE9C5 CRC64;
     VTAAMDAIKK KMQMLKLDKE NALDRAEQAE SDKKAAEDRS KQLEDDLVAL QKKLKATEDE
     LDKYSEALKD AQEKLELAEK KATDAEGDVA SLNRRIQLVE EELDRAQERL ATALTKLEEA
     EKAADESERG MKVIENRAMK DEEKMELQEI QLKEAKHIAE EADRKYEEVA RKLVIIESDL
     ERTEERAELS ESKCSELEEE LKTVQNNLKS LEAQAEKYSQ KEDKYEEEIK VLTDKLKEAE
     TRAEFAERSV AKLEKSIDDL EDELYAQKLK YKAISEELDH ALNDMTSM
//
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