ID I3IYT6_ORENI Unreviewed; 171 AA.
AC I3IYT6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Caltractin {ECO:0000313|Ensembl:ENSONIP00000001776.2};
GN Name=LOC100695822 {ECO:0000313|Ensembl:ENSONIP00000001776.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000001776.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000001776.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_003443408.1; XM_003443360.4.
DR AlphaFoldDB; I3IYT6; -.
DR STRING; 8128.ENSONIP00000001776; -.
DR Ensembl; ENSONIT00000001775.2; ENSONIP00000001776.2; ENSONIG00000001409.2.
DR GeneID; 100695822; -.
DR KEGG; onl:100695822; -.
DR CTD; 207175; -.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000162309; -.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; I3IYT6; -.
DR OMA; NEQEFLC; -.
DR OrthoDB; 67444at2759; -.
DR TreeFam; TF101141; -.
DR Proteomes; UP000005207; Linkage group LG2.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0022027; P:interkinetic nuclear migration; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
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:SF350; CENTRIN-4; 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; 2.
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:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 27..62
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 63..98
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..171
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 171 AA; 19535 MW; FB49E288479C555C CRC64;
MASSYRKPAS TASQRKKTDL KNDLTEEQKQ EIKEAFDLFD TDGTGTIDVK ELKVAMRALG
FEPKKEEIKK MIADIDKEGS GTIDFGDFLS IMTLKMSEKD TKEEILKAFR LFDDDCTGKI
SFKNLKRVAK ELGENLTDAE LQEMIDEADR DGDGEVNEQE FLRIMRKTNL Y
//
