CETN1_BOVIN
ID CETN1_BOVIN Reviewed; 172 AA.
AC Q32LE3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Centrin-1;
GN Name=CETN1;
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 [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a fundamental role in microtubule-organizing center
CC structure and function (By similarity). Plays a role in sperm cilia
CC formation (By similarity). {ECO:0000250|UniProtKB:P41209,
CC ECO:0000250|UniProtKB:Q12798}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with PIFO (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q12798}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome. Note=Centrosome of interphase and mitotic cells.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Binds two moles of calcium per mole of protein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; BC109624; AAI09625.1; -; mRNA.
DR RefSeq; NP_001072974.1; NM_001079506.2.
DR AlphaFoldDB; Q32LE3; -.
DR SMR; Q32LE3; -.
DR STRING; 9913.ENSBTAP00000052557; -.
DR PaxDb; Q32LE3; -.
DR Ensembl; ENSBTAT00000016356; ENSBTAP00000052557; ENSBTAG00000012320.
DR GeneID; 512850; -.
DR KEGG; bta:512850; -.
DR CTD; 1068; -.
DR VEuPathDB; HostDB:ENSBTAG00000012320; -.
DR VGNC; VGNC:27233; CETN1.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000157209; -.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; Q32LE3; -.
DR OMA; GIQKIFA; -.
DR OrthoDB; 1382571at2759; -.
DR TreeFam; TF101141; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000012320; Expressed in semen and 21 other tissues.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR029527; CETN1.
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:SF218; PTHR23050:SF218; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 2: Evidence at transcript level;
KW Calcium; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Metal-binding;
KW Mitosis; Reference proteome; Repeat.
FT CHAIN 1..172
FT /note="Centrin-1"
FT /id="PRO_0000244557"
FT DOMAIN 28..63
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 64..99
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 101..136
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 137..172
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 172 AA; 19697 MW; 45731CA62BF720CC CRC64;
MASSYRKPTV ASTSQKRKVG PKPELTEEQK QEVREAFDLF DADGSGTIDV KELKVAMRAL
GFEPRKEEMK RMIADVDKEG TGKISFNDFL AVMTQKMAEK DTKEEILKAF RLFDDDETGK
ISFKNLKRVA KELGENLTDE ELQEMIDEAD RDGDGEVNED EFLRIMKKTN LY
