POC1A_MOUSE
ID POC1A_MOUSE Reviewed; 405 AA.
AC Q8JZX3; Q9CY09;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=POC1 centriolar protein homolog A;
DE AltName: Full=WD repeat-containing protein 51A;
GN Name=Poc1a; Synonyms=Wdr51a;
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] (ISOFORMS 1 AND 3).
RC STRAIN=NOD; TISSUE=Corpus striatum, Dendritic cell, and Liver;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=22840364; DOI=10.1016/j.ajhg.2012.05.025;
RA Shaheen R., Faqeih E., Shamseldin H.E., Noche R.R., Sunker A.,
RA Alshammari M.J., Al-Sheddi T., Adly N., Al-Dosari M.S., Megason S.G.,
RA Al-Husain M., Al-Mohanna F., Alkuraya F.S.;
RT "POC1A truncation mutation causes a ciliopathy in humans characterized by
RT primordial dwarfism.";
RL Am. J. Hum. Genet. 91:330-336(2012).
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 POC1B to ensure centriole integrity and proper
CC mitotic spindle formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with POC1B. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}. Note=Component of both mother and daughter centrioles.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8JZX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8JZX3-2; Sequence=VSP_017841;
CC Name=3;
CC IsoId=Q8JZX3-3; Sequence=VSP_017840, VSP_017841;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryonic and adult tissues.
CC {ECO:0000269|PubMed:22840364}.
CC -!- SIMILARITY: Belongs to the WD repeat POC1 family. {ECO:0000305}.
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DR EMBL; AK154163; BAE32416.1; -; mRNA.
DR EMBL; AK011064; BAB27371.1; -; mRNA.
DR EMBL; BC034901; AAH34901.1; -; mRNA.
DR CCDS; CCDS23474.1; -. [Q8JZX3-1]
DR RefSeq; NP_081630.2; NM_027354.2. [Q8JZX3-1]
DR AlphaFoldDB; Q8JZX3; -.
DR SMR; Q8JZX3; -.
DR BioGRID; 213931; 6.
DR IntAct; Q8JZX3; 6.
DR STRING; 10090.ENSMUSP00000072064; -.
DR PhosphoSitePlus; Q8JZX3; -.
DR EPD; Q8JZX3; -.
DR MaxQB; Q8JZX3; -.
DR PaxDb; Q8JZX3; -.
DR PeptideAtlas; Q8JZX3; -.
DR PRIDE; Q8JZX3; -.
DR ProteomicsDB; 289863; -. [Q8JZX3-1]
DR ProteomicsDB; 289864; -. [Q8JZX3-2]
DR ProteomicsDB; 289865; -. [Q8JZX3-3]
DR Antibodypedia; 31157; 125 antibodies from 20 providers.
DR DNASU; 70235; -.
DR Ensembl; ENSMUST00000072206; ENSMUSP00000072064; ENSMUSG00000023345. [Q8JZX3-1]
DR Ensembl; ENSMUST00000191434; ENSMUSP00000140374; ENSMUSG00000023345. [Q8JZX3-3]
DR GeneID; 70235; -.
DR KEGG; mmu:70235; -.
DR UCSC; uc009rjk.2; mouse. [Q8JZX3-1]
DR UCSC; uc009rjl.2; mouse. [Q8JZX3-3]
DR CTD; 25886; -.
DR MGI; MGI:1917485; Poc1a.
DR VEuPathDB; HostDB:ENSMUSG00000023345; -.
DR eggNOG; ENOG502QSVJ; Eukaryota.
DR GeneTree; ENSGT00940000157494; -.
DR HOGENOM; CLU_000288_57_17_1; -.
DR InParanoid; Q8JZX3; -.
DR OMA; SEMDCGI; -.
DR OrthoDB; 1196215at2759; -.
DR PhylomeDB; Q8JZX3; -.
DR TreeFam; TF324210; -.
DR BioGRID-ORCS; 70235; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Poc1a; mouse.
DR PRO; PR:Q8JZX3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8JZX3; protein.
DR Bgee; ENSMUSG00000023345; Expressed in animal zygote and 133 other tissues.
DR ExpressionAtlas; Q8JZX3; baseline and differential.
DR Genevisible; Q8JZX3; MM.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0003431; P:growth plate cartilage chondrocyte development; IMP:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
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; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..405
FT /note="POC1 centriolar protein homolog A"
FT /id="PRO_0000231523"
FT REPEAT 17..56
FT /note="WD 1"
FT REPEAT 59..98
FT /note="WD 2"
FT REPEAT 101..140
FT /note="WD 3"
FT REPEAT 143..182
FT /note="WD 4"
FT REPEAT 185..224
FT /note="WD 5"
FT REPEAT 227..266
FT /note="WD 6"
FT REPEAT 269..308
FT /note="WD 7"
FT REGION 313..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 367..395
FT /evidence="ECO:0000255"
FT VAR_SEQ 7
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017840"
FT VAR_SEQ 326..373
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017841"
FT CONFLICT 24
FT /note="C -> R (in Ref. 1; BAB27371)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="P -> S (in Ref. 1; BAE32416 and 2; AAH34901)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="K -> N (in Ref. 1; BAB27371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 45125 MW; 1392C56D894D5659 CRC64;
MAAPSQEDPS LERHFKGHRD AVTCVDFSLN TKHLASGSMD STLMIWHMKP QSRAYRFTGH
KDAVTCVNFS PSGHLLASGS RDKTVRIWVP NVKGESTVFR AHTATVRSVH FCSDGQSLVT
ASDDKTVKVW STHRQRFLFS LTQHINWVRC AKFSPDGRLI VSASDDKTVK LWDKTSRECI
HSYCEHGGFV TYVDFHPSGT CIAAAGMDNT VKVWDARTHR LLQHYQLHSA AVNALSFHPS
GNYLITASSD STLKILDLME GRLLYTLHGH QGPATTVAFS RTGEYFASGG SDEQVMVWKS
NFDIVDYGDM KARRPPPLTS SSGTLPKMDL PVPPGRDRSL ESVQGEPQES ISMPQTLTST
LEHIVGQLDI LTQTVSILEQ RLTLTEDRLK QCLENQQLIM QRTPP
