CETN2_BOVIN
ID CETN2_BOVIN Reviewed; 172 AA.
AC Q2TBN3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Centrin-2;
GN Name=CETN2;
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. Required for centriole duplication and correct
CC spindle formation. Has a role in regulating cytokinesis and genome
CC stability via cooperation with CALM1 and CCP110 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Involved in global genome nucleotide excision repair (GG-NER)
CC by acting as component of the XPC complex. Cooperatively with RAD23B
CC appears to stabilize XPC. In vitro, stimulates DNA binding of the
CC XPC:RAD23B dimer (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The XPC complex is proposed to represent the first factor
CC bound at the sites of DNA damage and together with other core
CC recognition factors, XPA, RPA and the TFIIH complex, is part of the
CC pre-incision (or initial recognition) complex. The XPC complex
CC recognizes a wide spectrum of damaged DNA characterized by distortions
CC of the DNA helix such as single-stranded loops, mismatched bubbles or
CC single-stranded overhangs. The orientation of XPC complex binding
CC appears to be crucial for inducing a productive NER. XPC complex is
CC proposed to recognize and to interact with unpaired bases on the
CC undamaged DNA strand which is followed by recruitment of the TFIIH
CC complex and subsequent scanning for lesions in the opposite strand in a
CC 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers
CC (CPDs) which are formed upon UV-induced DNA damage esacpe detection by
CC the XPC complex due to a low degree of structural perurbation. Instead
CC they are detected by the UV-DDB complex which in turn recruits and
CC cooperates with the XPC complex in the respective DNA repair (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: As a component of the TREX-2 complex, involved in the export
CC of mRNAs to the cytoplasm through the nuclear pores.
CC {ECO:0000250|UniProtKB:P41208}.
CC -!- SUBUNIT: Monomer. Homooligomer. Interacts with CCP110, SFI1. Component
CC of the XPC complex composed of XPC, RAD23B and CETN2 (By similarity).
CC Component of the nuclear pore complex (NPC)-associated TREX-2 complex
CC (transcription and export complex 2), composed of at least GANP, 2
CC copies of ENY2, PCID2, SEM1/DSS1, and either centrin CETN2 or centrin
CC CETN3. The TREX-2 complex also associates with ALYREF/ALY and with the
CC nucleoporin NUP153 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P41208}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:P41208}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:P41208}. Nucleus {ECO:0000250|UniProtKB:P41208}.
CC Nucleus envelope {ECO:0000250|UniProtKB:P41208}. Nucleus, nuclear pore
CC complex {ECO:0000250|UniProtKB:P41208}.
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; BC109888; AAI09889.1; -; mRNA.
DR RefSeq; NP_001033604.1; NM_001038515.1.
DR AlphaFoldDB; Q2TBN3; -.
DR SMR; Q2TBN3; -.
DR STRING; 9913.ENSBTAP00000010319; -.
DR PaxDb; Q2TBN3; -.
DR PRIDE; Q2TBN3; -.
DR Ensembl; ENSBTAT00000010319; ENSBTAP00000010319; ENSBTAG00000007844.
DR GeneID; 508601; -.
DR KEGG; bta:508601; -.
DR CTD; 1069; -.
DR VEuPathDB; HostDB:ENSBTAG00000007844; -.
DR VGNC; VGNC:27234; CETN2.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000155935; -.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; Q2TBN3; -.
DR OMA; YDEFEYM; -.
DR OrthoDB; 1382571at2759; -.
DR TreeFam; TF101141; -.
DR Reactome; R-BTA-5696394; DNA Damage Recognition in GG-NER.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000007844; Expressed in oviduct epithelium and 107 other tissues.
DR GO; GO:0097729; C:9+2 motile cilium; IEA:Ensembl.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0070390; C:transcription export complex 2; ISS:UniProtKB.
DR GO; GO:0071942; C:XPC complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:Ensembl.
DR GO; GO:0032795; F:heterotrimeric G-protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR037629; Centrin_2.
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:SF305; PTHR23050:SF305; 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 Acetylation; Calcium; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW DNA damage; DNA repair; Isopeptide bond; Metal-binding; Mitosis;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P41208"
FT CHAIN 2..172
FT /note="Centrin-2"
FT /id="PRO_0000244558"
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..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..25
FT /note="Required for self-assembly"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..19
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"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P41208"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41208"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P41208"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41208"
SQ SEQUENCE 172 AA; 19810 MW; FE2BA956FC2FDCF1 CRC64;
MASNFKKANM ASTTQRKRMS PKPELTEEQK QEIREAFDLF DADGTGTIDV KELKVAMRAL
GFEPKKEEIK KMISEIDKEG TGKMNFSDFL TVMTQKMSEK DTKEEILKAF KLFDDDETGK
ISFKNLKRVA KELGENLSDE ELQEMIDEAD RDGDGEVNEQ EFLRIMKKTS LY
