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Database: UniProt
Entry: A0A3Q3B2B2_KRYMA
LinkDB: A0A3Q3B2B2_KRYMA
Original site: A0A3Q3B2B2_KRYMA 
ID   A0A3Q3B2B2_KRYMA        Unreviewed;       169 AA.
AC   A0A3Q3B2B2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Troponin C, slow skeletal and cardiac muscles {ECO:0000256|ARBA:ARBA00044185};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000018099.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000018099.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Troponin is the central regulatory protein of striated muscle
CC       contraction. Tn consists of three components: Tn-I which is the
CC       inhibitor of actomyosin ATPase, Tn-T which contains the binding site
CC       for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the
CC       inhibitory action of Tn on actin filaments.
CC       {ECO:0000256|ARBA:ARBA00037722}.
CC   -!- SIMILARITY: Belongs to the troponin C family.
CC       {ECO:0000256|ARBA:ARBA00038202}.
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DR   AlphaFoldDB; A0A3Q3B2B2; -.
DR   Ensembl; ENSKMAT00000018351.1; ENSKMAP00000018099.1; ENSKMAG00000013462.1.
DR   GeneTree; ENSGT00940000153541; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:UniProt.
DR   CDD; cd00051; EFh; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR23048; MYOSIN LIGHT CHAIN 1, 3; 1.
DR   PANTHER; PTHR23048:SF48; TROPONIN C1, SLOW SKELETAL AND CARDIAC TYPE; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT   DOMAIN          23..59
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          60..95
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          100..135
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          136..169
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   169 AA;  19177 MW;  7AEB16D01D37C403 CRC64;
     MHDPTSPPSY HSIVCPLRAA AFLSEPEFKA AFDIFVQDAE DGCISTKELG KVMRMLGQNP
     TPEELQEMID EVDEDGSGTV DFDEFLVMMV RCMKDDSKGK TEEELAELFR MFDKNADGYI
     DLEELKMMLE STGEAITEDD IEELMKDGDK NNDGKIDYDE FLEFMKGVE
//
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