ID A0A3B4X2C1_SERLL Unreviewed; 191 AA.
AC A0A3B4X2C1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Caltractin-like {ECO:0000313|Ensembl:ENSSLDP00000011669.1};
GN Name=CETN1 {ECO:0000313|Ensembl:ENSSLDP00000011669.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000011669.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000011669.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Calmodulin acts as part of a calcium signal transduction
CC pathway by mediating the control of a large number of enzymes, ion
CC channels, aquaporins and other proteins through calcium-binding.
CC Calcium-binding is required for the activation of calmodulin. Among the
CC enzymes to be stimulated by the calmodulin-calcium complex are a number
CC of protein kinases, such as myosin light-chain kinases and calmodulin-
CC dependent protein kinase type II (CaMK2), and phosphatases.
CC {ECO:0000256|ARBA:ARBA00037485}.
CC -!- SIMILARITY: Belongs to the centrin family.
CC {ECO:0000256|ARBA:ARBA00005253}.
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DR AlphaFoldDB; A0A3B4X2C1; -.
DR STRING; 1841481.ENSSLDP00000011669; -.
DR Ensembl; ENSSLDT00000012092.1; ENSSLDP00000011669.1; ENSSLDG00000009289.1.
DR GeneTree; ENSGT00940000157209; -.
DR OrthoDB; 67444at2759; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR PANTHER; PTHR23050; CALCIUM BINDING PROTEIN; 1.
DR PANTHER; PTHR23050:SF218; CENTRIN-1; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 47..82
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 83..118
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 120..155
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 156..191
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 191 AA; 21700 MW; A3254D63E9132872 CRC64;
MLNRSAVPLC QSSTRQLMAT SAKRPSLQGP VPPPRKKTAP KPELTEEQKQ EIREAFELFD
TDGSGYIDVK ELKVAMRALG FEPKKEEIKK MTGEVDKDGT GKISFGDFLT VMTQKMAEKD
SKEEILKAFR LFDDDETGKI SFKNLKRVAK ELGENLTDEE LQEMIDEADR DGDGEVNQQE
FLRIMKKTCL Y
//
