ID   CNTLN_RAT               Reviewed;         721 AA.
AC   A9ZSY0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Centlein;
DE   AltName: Full=Centrosomal protein;
DE   Flags: Fragment;
GN   Name=Cntln {ECO:0000250|UniProtKB:Q9NXG0};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAF98578.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=18086554; DOI=10.1016/j.bbrc.2007.12.050;
RA   Makino K., Umeda K., Uezu A., Hiragami Y., Sakamoto T., Ihn H.,
RA   Nakanishi H.;
RT   "Identification and characterization of the novel centrosomal protein
RT   centlein.";
RL   Biochem. Biophys. Res. Commun. 366:958-962(2008).
CC   -!- FUNCTION: Required for centrosome cohesion and recruitment of CEP68 to
CC       centrosomes. {ECO:0000250|UniProtKB:Q9NXG0}.
CC   -!- SUBUNIT: Interacts with CEP250 and CEP68. Interacts with NEK2; the
CC       interaction leads to phosphorylation of CNTLN.
CC       {ECO:0000250|UniProtKB:Q9NXG0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000269|PubMed:18086554}.
CC       Note=Colocalizes with gamma-tubulin during interphase and mitosis
CC       (PubMed:18086554). Appears to associate with the mother centriole
CC       during G1 phase and with daughter centrioles towards G1/S phase
CC       (PubMed:18086554). Localizes to the proximal ends of the centrioles (By
CC       similarity). Levels are high at interphase centrosomes but are reduced
CC       on mitotic spindle poles (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NXG0, ECO:0000269|PubMed:18086554}.
CC   -!- PTM: Phosphorylated directly or indirectly by NEK2.
CC       {ECO:0000250|UniProtKB:Q9NXG0}.
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DR   EMBL; AB369315; BAF98578.1; -; mRNA.
DR   RefSeq; NP_001107874.1; NM_001114402.1.
DR   AlphaFoldDB; A9ZSY0; -.
DR   SMR; A9ZSY0; -.
DR   STRING; 10116.ENSRNOP00000008757; -.
DR   PaxDb; A9ZSY0; -.
DR   PeptideAtlas; A9ZSY0; -.
DR   PRIDE; A9ZSY0; -.
DR   GeneID; 679640; -.
DR   KEGG; rno:679640; -.
DR   UCSC; RGD:1308101; rat.
DR   CTD; 54875; -.
DR   RGD; 1308101; Cntln.
DR   eggNOG; ENOG502QRVC; Eukaryota.
DR   InParanoid; A9ZSY0; -.
DR   OrthoDB; 846281at2759; -.
DR   PhylomeDB; A9ZSY0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005814; C:centriole; ISO:RGD.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR   GO; GO:0010457; P:centriole-centriole cohesion; ISO:RGD.
DR   GO; GO:0033365; P:protein localization to organelle; ISO:RGD.
DR   InterPro; IPR038810; CNTLN.
DR   PANTHER; PTHR18957; PTHR18957; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           <1..721
FT                   /note="Centlein"
FT                   /id="PRO_0000328977"
FT   REGION          156..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          52..164
FT                   /evidence="ECO:0000255"
FT   COILED          345..515
FT                   /evidence="ECO:0000255"
FT   COILED          573..626
FT                   /evidence="ECO:0000255"
FT   MOD_RES         658
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AM05"
FT   NON_TER         1
SQ   SEQUENCE   721 AA;  82721 MW;  D4BC438FFE46A88A CRC64;
     MNLQDELDEL KIYMTIDKTT IQELNRCMAE KREEQLFRHH EDAGVKKSTP EKNEKAISEQ
     TLEKVIELEN RLKSFEKNSR KLKEESKKLK KENDFLKSHL QHYQEDSESR GKELEKLLRV
     SSSVEQDKSE LQTKVTALER EVTTLRRQVA KAKALRDENE EVVNPEEKEH CPTDKAKSEM
     ATTDVRAQHC DCKTTTTKVK FKAAKKKCSV GRHHTVLNHS IKVMSHVENL SKDGWEDMSE
     GSSDSETQTF QNLGTVIVET SQNIRPIEND GNQKETDQTE DSRAQQEVQT YSCEDLKAPQ
     NTKKMTFQNK SGSLQKNLHS ALPARVNREK CKTKPAQKSS SNTILLRERI VSLQQQNSLL
     QNARKAAESS AKEFKEANEK LLHQQQISDH RFQTSRQTIK LTLDLAELRK EKEDLLKKVE
     SSSDITSLAE EVSRIMAPQI QVTTLGPSRS TDLEIKQLQC KLKNATNELT KQSSSVKSLK
     LELLAKDDHM KAMQEKMSRM ERDITMKRHL IEDLKFRQKI NSESNESFNE MLGTLEKKDL
     KMNLLISKLN DTETAMAQIK SAASEQLQGL ALQSEQVLEG TQKKLLLANE KIEEFTVFVQ
     ALVNELQSDA HRTRQQVREL RQTQKSRHAC KTSTHKAQTL AASILNISRS DLEEILHTGD
     EMEIEKTKID AENDKDWMLY IQKLLQGQLP FASYLLEAVL GKIKENKKLT EGYFTVMKDI
     K