CE162_COTCO
ID CE162_COTCO Reviewed; 1251 AA.
AC Q91365;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Centrosomal protein of 162 kDa;
DE Short=Cep162;
DE AltName: Full=Protein quail neuroretina 1;
DE Flags: Fragment;
GN Name=CEP162; Synonyms=QN1;
OS Coturnix coturnix (Common quail) (Tetrao coturnix).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=9091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Neuroretina;
RX PubMed=8297788; DOI=10.1016/0925-4773(93)90033-t;
RA Bidou L., Crisanti P., Blancher C., Pessac B.;
RT "A novel cDNA corresponding to transcripts expressed in retina post-mitotic
RT neurons.";
RL Mech. Dev. 43:159-173(1993).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=11287185; DOI=10.1016/s0925-4773(01)00297-0;
RA Neron B., Marx M., Crisanti P.;
RT "Role of QN1 protein in cell proliferation arrest and differentiation
RT during the neuroretina development.";
RL Mech. Dev. 102:107-117(2001).
RN [3]
RP PRELIMINARY FUNCTION.
RX PubMed=16302001; DOI=10.1038/sj.onc.1209215;
RA Leon A., Omri B., Gely A., Klein C., Crisanti P.;
RT "QN1/KIAA1009: a new essential protein for chromosome segregation and
RT mitotic spindle assembly.";
RL Oncogene 25:1887-1895(2006).
CC -!- FUNCTION: Required to promote assembly of the transition zone in
CC primary cilia. Acts by specifically recognizing and binding the
CC axonemal microtubule (By similarity). Plays a role in cell
CC proliferation and differentiation in the neuroretina. Has an ATPase
CC activity in vitro. {ECO:0000250, ECO:0000269|PubMed:11287185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:11287185, ECO:0000269|PubMed:8297788}.
CC Note=Localizes to the distal end of centrioles throughout the cell
CC cycle. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in retina and brain (at protein level).
CC {ECO:0000269|PubMed:8297788}.
CC -!- DEVELOPMENTAL STAGE: Detected from E5 onward in the neuroretina (at
CC protein level). {ECO:0000269|PubMed:11287185,
CC ECO:0000269|PubMed:8297788}.
CC -!- MISCELLANEOUS: Depletion of QN1 leads to retinal dysplasia.
CC {ECO:0000305|PubMed:11287185}.
CC -!- SIMILARITY: Belongs to the CEP162 family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to regulate chromosome segregation and
CC mitotic spindle assembly (PubMed:16302001). However, it was later shown
CC that its absence neither affect mitosis nor centriole duplication.
CC {ECO:0000305|PubMed:16302001}.
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DR EMBL; S68151; AAD14007.1; -; mRNA.
DR PIR; A56677; A56677.
DR AlphaFoldDB; Q91365; -.
DR SMR; Q91365; -.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR InterPro; IPR038774; CEP162-like.
DR PANTHER; PTHR34031; PTHR34031; 1.
PE 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Nucleus.
FT CHAIN <1..1251
FT /note="Centrosomal protein of 162 kDa"
FT /id="PRO_0000295631"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 559..782
FT /evidence="ECO:0000255"
FT COILED 813..1165
FT /evidence="ECO:0000255"
FT COILED 1210..1242
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 1251 AA; 143966 MW; 189DC75C428BA442 CRC64;
MLEKFHKNKK DSYLNKEEGS LTSDGSDSPK EILETSERIV KKALQLTEET DENVHPEKMQ
LQKSNGVAFS LSRDSLETND SFVASGPNQS NTGLGLDTLE EQEEKEIFFA KLEQEASSPI
DYSRLNKELN LSDSIVLAPF VRNESEKEVE STAEEKCESY SEDFEEDTDA NPAFKTEESQ
EPNSGMLAKV VLLDSQDSTT EFQKAAETSG VALSEHDLPQ EVGGTEMNEA GTLCGQTTSD
TEALHHAYHH HIDQSLGDTD EQKIHSSSMA ISQCLVQVTS QNHNLYSKNT STTESDLPTV
EEFMRPIKGD CYNARGFDLE PESPVKVIGS TVNEHVNHLP YKEHKNESVW ETNLLEKFNR
EDSIFLQTAA NEDSFLRMPG KEIQTSEVQP DVLSKEIIQD CLLSQGSKTK QVLQSCCLKN
EKSESTTTKQ MLYKNIRSTT PLHKKKSSYG PHGVVRSSGY GKSTSYSKQS IPATERKIPK
ETLKKSIMKC RSPADKARSK EALFTTRTIR SAANQQASKE DISRAMPDQS VVQNLGHQVV
DSFRQHHSDL PVSPVKSCER ELRLLRRAQV AEEDLSRARD VIQQLTSTVS EKEKEMETKI
VELKTRYEKE LSQLGQENYV LQSKLRSVEE LSKEKRWIHQ TGTVSVPEEK LAQIQKEMED
QEVIIQGYQQ ENERLYKQMK DLQIQNKKNE EQMYKENQCL MSELIALREK VERINIQSQI
VRESEPARNQ SFTELISELR AARKEETKLR EEIRRLKQDK QALELDLGQA KKERDLAKVQ
ITSTSSEKSY EFKIMEETYK QEILHLKRRL HWYAENQDLL DKDAARLKEA REEIEKLKQE
VKKLRAEAGD HQCVQQKKRL RDRAADAKRI QDLERQIKEM EGILKRRYPN SLPALIYAAA
AAEKTNDLSA KTNTTDFLER RIKKLETELE GKDDEAKTSL RAMEQQFQKI KMQYEQRLAE
LEQLLAYKWK SESPKLNGDK ANCIELELQL QNLKKTHQIT VENLQTEIEN LKSQNSQLKL
RSKKDNKDLQ LADWQMKQGN TKEKLLKLNQ ELITKNREIQ DLTKTVEKLQ KERMAMLSDN
NLRNKTDNKE NRQESLKNNT VATEKRNSCN SEPLIGIFNN DKIYQPHNFS DSNVLEVLQE
NARLKEEVEK LSLEMNQQRV KSQATLAYSE NNIRRIQEDT AEYVAALKAS HQREVEKILS
QYTKDDSASK VAELNGRIST QEILIKHLQE QISEHQRHQE ALLVSQMREE F
