CLUA1_MOUSE
ID CLUA1_MOUSE Reviewed; 413 AA.
AC Q8R3P7; Q6P3Y8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Clusterin-associated protein 1;
GN Name=Cluap1;
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=Medulla oblongata;
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].
RC STRAIN=FVB/N; TISSUE=Jaw, Limb, and Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-324; SER-326 AND
RP SER-409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23351563; DOI=10.1186/2046-2530-1-20;
RA Pasek R.C., Berbari N.F., Lewis W.R., Kesterson R.A., Yoder B.K.;
RT "Mammalian Clusterin associated protein 1 is an evolutionarily conserved
RT protein required for ciliogenesis.";
RL Cilia 1:20-20(2012).
CC -!- FUNCTION: Required for cilia biogenesis. Appears to function within the
CC multiple intraflagellar transport complex B (IFT-B). Key regulator of
CC hedgehog signaling. {ECO:0000269|PubMed:23351563}.
CC -!- SUBUNIT: Interacts with CLU/clusterin. Interacts with UBXN10; the
CC interaction is direct. {ECO:0000250|UniProtKB:Q96AJ1}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:23351563}. Nucleus {ECO:0000250|UniProtKB:Q96AJ1}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including heart,
CC kidney, skeletal muscle, eye, liver, ovary, oviduct, testes, lung and
CC brain. Elevated levels in multiciliated cells such as the bronchioles
CC of the lungs, ependymal cells of the brain and cells with a single
CC primary cilia of heart and kidney. {ECO:0000269|PubMed:23351563}.
CC -!- DISRUPTION PHENOTYPE: E9.5 embryos are still viable but die thereafter.
CC Mutant embryos are runted, have exhibit enlarged pericardial sacs, and
CC defects in neural tube development. There is a complete absence of
CC cilia in E9.5 embryos. Sonic hedgehog (SHH) signaling is severely
CC disrupted with down-regulation of PTCH1 and GLI1.
CC {ECO:0000269|PubMed:23351563}.
CC -!- SIMILARITY: Belongs to the CLUAP1 family. {ECO:0000305}.
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DR EMBL; AK134648; BAE22224.1; -; mRNA.
DR EMBL; BC024910; AAH24910.1; -; mRNA.
DR EMBL; BC063769; AAH63769.1; -; mRNA.
DR CCDS; CCDS27912.1; -.
DR RefSeq; NP_084014.1; NM_029738.2.
DR AlphaFoldDB; Q8R3P7; -.
DR SMR; Q8R3P7; -.
DR BioGRID; 218308; 4.
DR ComplexPortal; CPX-5028; IFT-B complex.
DR CORUM; Q8R3P7; -.
DR STRING; 10090.ENSMUSP00000043397; -.
DR iPTMnet; Q8R3P7; -.
DR PhosphoSitePlus; Q8R3P7; -.
DR MaxQB; Q8R3P7; -.
DR PaxDb; Q8R3P7; -.
DR PeptideAtlas; Q8R3P7; -.
DR PRIDE; Q8R3P7; -.
DR ProteomicsDB; 283386; -.
DR Ensembl; ENSMUST00000040881; ENSMUSP00000043397; ENSMUSG00000014232.
DR GeneID; 76779; -.
DR KEGG; mmu:76779; -.
DR UCSC; uc007xzb.1; mouse.
DR CTD; 23059; -.
DR MGI; MGI:1924029; Cluap1.
DR VEuPathDB; HostDB:ENSMUSG00000014232; -.
DR eggNOG; KOG3647; Eukaryota.
DR GeneTree; ENSGT00390000008957; -.
DR HOGENOM; CLU_034981_1_0_1; -.
DR InParanoid; Q8R3P7; -.
DR OMA; DHHRLEQ; -.
DR OrthoDB; 874966at2759; -.
DR PhylomeDB; Q8R3P7; -.
DR TreeFam; TF314639; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 76779; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cluap1; mouse.
DR PRO; PR:Q8R3P7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8R3P7; protein.
DR Bgee; ENSMUSG00000014232; Expressed in spermatid and 255 other tissues.
DR ExpressionAtlas; Q8R3P7; baseline and differential.
DR Genevisible; Q8R3P7; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0097542; C:ciliary tip; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030991; C:intraciliary transport particle A; IDA:MGI.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0035082; P:axoneme assembly; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0021508; P:floor plate formation; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0042073; P:intraciliary transport; IC:MGI.
DR GO; GO:0060972; P:left/right pattern formation; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR InterPro; IPR019366; Clusterin-associated_protein-1.
DR PANTHER; PTHR21547; PTHR21547; 1.
DR Pfam; PF10234; Cluap1; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..413
FT /note="Clusterin-associated protein 1"
FT /id="PRO_0000239453"
FT REGION 303..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..308
FT /evidence="ECO:0000255"
FT COMPBIAS 359..387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 413 AA; 47953 MW; F0AEDF9320D09B0C CRC64;
MSFRDLRNFT EMMRALGYPR HISMENFRTP NFGLVSEVLL WLVKRYEPQT DIPSDIETEQ
DRVFFIKAIA QFMATKAHIK LNTKKLYQAD GYAVKELLKI TSVLYNAMKT KGMEGSNVGE
EDISKFKFDL GSKIADLKAA RQLASEITAK GASLYDLLGK EVELRELRTE AIARPLEINE
TEKVMRIAIK DLLAQVQKTK DLLNNVASDE ANLEAKIEKR KLELERNRKR LQTLQSVRPA
FMDEYEKVEE DLQKQYDVYL EKFRNLAYLE QQLEDHHRME QERFEEAENT LRLMQNKLKE
EEKRLLKSGS NDDSDIDIQE DDESDSELED RRMSKPRTAM EVLMQGRPSK RIVGAMQGGD
SDEDEDSEDS EIDMEDDEED DDDLEDESIA LSPAKPSRRI RKPEPLDESD NDF
