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POC1B_MOUSE
ID   POC1B_MOUSE             Reviewed;         476 AA.
AC   Q8BHD1;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=POC1 centriolar protein homolog B;
DE   AltName: Full=WD repeat-containing protein 51B;
GN   Name=Poc1b; Synonyms=Wdr51b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Submandibular gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=25044745; DOI=10.1002/humu.22618;
RA   Beck B.B., Phillips J.B., Bartram M.P., Wegner J., Thoenes M., Pannes A.,
RA   Sampson J., Heller R., Goebel H., Koerber F., Neugebauer A., Hedergott A.,
RA   Nuernberg G., Nuernberg P., Thiele H., Altmueller J., Toliat M.R.,
RA   Staubach S., Boycott K.M., Valente E.M., Janecke A.R., Eisenberger T.,
RA   Bergmann C., Tebbe L., Wang Y., Wu Y., Fry A.M., Westerfield M.,
RA   Wolfrum U., Bolz H.J.;
RT   "Mutation of POC1B in a severe syndromic retinal ciliopathy.";
RL   Hum. Mutat. 35:1153-1162(2014).
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:0000269|PubMed:25044745}. Cytoplasm,
CC       cytoskeleton, cilium basal body {ECO:0000269|PubMed:25044745}.
CC       Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8TC44}.
CC       Note=Component of both mother and daughter centrioles. Localizes to the
CC       basal body and centriole adjacent to the connecting cilium of
CC       photoreceptors and in synapses of the outer plexiform layer.
CC       {ECO:0000269|PubMed:25044745}.
CC   -!- TISSUE SPECIFICITY: Expressed in the retina.
CC       {ECO:0000269|PubMed:25044745}.
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   EMBL; AK045302; BAC32302.1; -; mRNA.
DR   EMBL; AK050233; BAC34138.1; -; mRNA.
DR   EMBL; AK090075; BAC41080.1; -; mRNA.
DR   CCDS; CCDS36045.1; -.
DR   RefSeq; NP_082016.1; NM_027740.6.
DR   AlphaFoldDB; Q8BHD1; -.
DR   SMR; Q8BHD1; -.
DR   BioGRID; 238351; 23.
DR   IntAct; Q8BHD1; 25.
DR   STRING; 10090.ENSMUSP00000020113; -.
DR   iPTMnet; Q8BHD1; -.
DR   PhosphoSitePlus; Q8BHD1; -.
DR   MaxQB; Q8BHD1; -.
DR   PaxDb; Q8BHD1; -.
DR   PRIDE; Q8BHD1; -.
DR   ProteomicsDB; 289866; -.
DR   Antibodypedia; 29964; 117 antibodies from 21 providers.
DR   DNASU; 382406; -.
DR   Ensembl; ENSMUST00000020113; ENSMUSP00000020113; ENSMUSG00000019952.
DR   GeneID; 382406; -.
DR   KEGG; mmu:382406; -.
DR   UCSC; uc007gxh.1; mouse.
DR   CTD; 282809; -.
DR   MGI; MGI:1918511; Poc1b.
DR   VEuPathDB; HostDB:ENSMUSG00000019952; -.
DR   eggNOG; ENOG502QSVJ; Eukaryota.
DR   GeneTree; ENSGT00940000160413; -.
DR   InParanoid; Q8BHD1; -.
DR   OMA; HYKAHEA; -.
DR   OrthoDB; 1196215at2759; -.
DR   PhylomeDB; Q8BHD1; -.
DR   TreeFam; TF324210; -.
DR   BioGRID-ORCS; 382406; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Poc1b; mouse.
DR   PRO; PR:Q8BHD1; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8BHD1; protein.
DR   Bgee; ENSMUSG00000019952; Expressed in ear vesicle and 169 other tissues.
DR   ExpressionAtlas; Q8BHD1; baseline and differential.
DR   Genevisible; Q8BHD1; MM.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..476
FT                   /note="POC1 centriolar protein homolog B"
FT                   /id="PRO_0000051411"
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          429..468
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   476 AA;  53504 MW;  307BF5A63E5F0794 CRC64;
     MASGLEDPIL ERSFKGHKAA ITSADFSPNC KQIATASWDT FLMLWSLKPH ARAYRYVGHK
     DVVTSLQFSP QGNLLASASR DRTVRLWVLD RKGKSSEFKA HTAPVRSVDF SADGQLLVTA
     SEDKSIKVWS MFRQRFLYSL YRHTHWVRCA KFSPDGRLIV SCSEDKTIKI WDTTNKQCVN
     NFSDSVGFAN FVDFNPNGTC IASAGSDHAV KIWDIRMNKL LQHYQVHSCG VNCLSFHPLG
     NSLVTASSDG TVKMLDLIEG RLIYTLQGHT GPVFTVSFSK DGELLTSGGA DAQVLIWRTN
     FIHLHCKDPK RNLKRLHFEA SPHLLDIYPR SPHSHEDRKE TIEINPKREV MDLQSSSPPV
     VDVLSFDSTT MTDSTYRAVP GKGEDICRYF LNPLLMPECS STTVKKRPED VSDVPSESLR
     SVPLAVADAL EHIMEQLNIL TQTVSILEQR LSLTEDKLRD CLENQQKLFS AVQQKS
 
 
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