ID   POC1B_RAT               Reviewed;         477 AA.
AC   D3ZW91;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=POC1 centriolar protein homolog B;
DE   AltName: Full=WD repeat-containing protein 51B;
GN   Name=Poc1b; Synonyms=Wdr51b;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
CC   -!- FUNCTION: Plays an important role in centriole assembly and/or
CC       stability and ciliogenesis. Involved in early steps of centriole
CC       duplication, as well as in the later steps of centriole length control.
CC       Acts in concert with POC1A to ensure centriole integrity and proper
CC       mitotic spindle formation. Required for primary cilia formation,
CC       ciliary length and also cell proliferation. Required for retinal
CC       integrity. {ECO:0000250|UniProtKB:Q8TC44}.
CC   -!- SUBUNIT: Interacts with POC1A. Interacts with FAM161A. Interacts with
CC       CEP44; the interaction is direct and recruits POC1B to centriolar
CC       microtubules. {ECO:0000250|UniProtKB:Q8TC44}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000250|UniProtKB:Q8TC44}.
CC       Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250|UniProtKB:Q8TC44}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:Q8TC44}. Note=Component of both mother and
CC       daughter centrioles. Localizes to the basal body and centriole adjacent
CC       to the connecting cilium of photoreceptors and in synapses of the outer
CC       plexiform layer. {ECO:0000250|UniProtKB:Q8BHD1}.
CC   -!- PTM: Phosphorylated in mitotic cells that may be mediated by CDK1.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat POC1 family. {ECO:0000305}.
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DR   AlphaFoldDB; D3ZW91; -.
DR   SMR; D3ZW91; -.
DR   STRING; 10116.ENSRNOP00000032069; -.
DR   PaxDb; D3ZW91; -.
DR   UCSC; RGD:2323942; rat.
DR   RGD; 2323942; Poc1b.
DR   eggNOG; ENOG502QSVJ; Eukaryota.
DR   InParanoid; D3ZW91; -.
DR   PhylomeDB; D3ZW91; -.
DR   TreeFam; TF324210; -.
DR   PRO; PR:D3ZW91; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISO:RGD.
DR   GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR   GO; GO:0001895; P:retina homeostasis; ISO:RGD.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 7.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 7.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..477
FT                   /note="POC1 centriolar protein homolog B"
FT                   /id="PRO_0000420366"
FT   REPEAT          16..55
FT                   /note="WD 1"
FT   REPEAT          58..97
FT                   /note="WD 2"
FT   REPEAT          100..139
FT                   /note="WD 3"
FT   REPEAT          142..181
FT                   /note="WD 4"
FT   REPEAT          183..223
FT                   /note="WD 5"
FT   REPEAT          226..265
FT                   /note="WD 6"
FT   REPEAT          268..307
FT                   /note="WD 7"
FT   COILED          449..469
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   477 AA;  53512 MW;  5681C5D99FF5E50C CRC64;
     MASGPEDPIL ERYFKGHKAA ITSADFSPNC KQIATASWDT FLMLWSLKPH ARAYRYVGHK
     DVVTSLQFSP QGNLLASASR DKTVRLWVLD RKGKSSEFKA HTAPVRSVDF SADGQFLVTA
     SEDKSIKVWS MYRQRFLYSL YRHTHWVRCA KFSPDGRLIV SCSEDKTIKI WDTTSKQCVN
     NFSDSVGFAN FVDFSPNGTC IASAGSDHAV RIWDIRMNRL LQHYQVHSCG VNCLSFHPSG
     NSLVTASSDG TVKILDLVEG RLIYTLQGHT GPVFTVSFSK DGELFTSGGA DAQVLVWRTS
     FNQVHYRDPS KRNLKRLHLE ASPHLLDIYP RTPHGHEDKR ETIEINPKLE VMDLHSSSPP
     VVDVLSFDST TVTDSTCRAV PGKGEDICRY FLNPLLMPEC SSTIMKKKPE DVGDPPSENQ
     RSVPLAVADA LEHIMEQLNI LTQSVSIVEQ RLSLTEDKLK DCLENQQKLF SVIQQKS