CIAO1_MOUSE
ID CIAO1_MOUSE Reviewed; 339 AA.
AC Q99KN2; Q9DCZ7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable cytosolic iron-sulfur protein assembly protein CIAO1 {ECO:0000255|HAMAP-Rule:MF_03037};
DE AltName: Full=WD repeat-containing protein 39 {ECO:0000255|HAMAP-Rule:MF_03037};
GN Name=Ciao1 {ECO:0000255|HAMAP-Rule:MF_03037}; Synonyms=Wdr39;
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=Kidney, and Placenta;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Spleen, 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 INTERACTION WITH CIAO2A.
RX PubMed=23891004; DOI=10.1016/j.cmet.2013.06.015;
RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and
RT maturation of different subsets of cytosolic-nuclear iron-sulfur
RT proteins.";
RL Cell Metab. 18:187-198(2013).
CC -!- FUNCTION: Key component of the cytosolic iron-sulfur protein assembly
CC (CIA) complex, a multiprotein complex that mediates the incorporation
CC of iron-sulfur cluster into extramitochondrial Fe/S proteins (By
CC similarity). As a CIA complex component, interacts specifically with
CC CIAO2A or CIAO2B and MMS19 to assist different branches of iron-sulfur
CC protein assembly, depending of its interactors. The complex
CC CIAO1:CIAO2B:MMS19 binds to and facilitates the assembly of most
CC cytosolic-nuclear Fe/S proteins. CIAO1:CIAO2A specifically matures ACO1
CC and stabilizes IREB2 (By similarity). Seems to specifically modulate
CC the transactivation activity of WT1. As part of the mitotic spindle-
CC associated MMXD complex it may play a role in chromosome segregation
CC (By similarity). {ECO:0000250|UniProtKB:O76071, ECO:0000255|HAMAP-
CC Rule:MF_03037}.
CC -!- SUBUNIT: Component of the CIA complex. Interacts with CIAO2A and forms
CC a complex with CIAO2B and MMS19; the interactions with CIAO2A and
CC CIAO2B are mutually exclusive (PubMed:23891004) (By similarity).
CC Interacts with CHD1L, ERCC2, IREB2 and POLD1 (By similarity). Component
CC of the MMXD complex, which includes CIAO1, ERCC2, CIAO2B, MMS19 and
CC SLC25A5. Interacts with WT1 (By similarity). Interacts with CIAO3 (By
CC similarity). Interacts (via LYR motif) with HSC20.
CC {ECO:0000250|UniProtKB:O76071, ECO:0000255|HAMAP-Rule:MF_03037,
CC ECO:0000269|PubMed:23891004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O76071}.
CC -!- SIMILARITY: Belongs to the WD repeat CIA1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03037}.
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DR EMBL; AK002314; BAB22008.1; -; mRNA.
DR EMBL; AK028376; BAC25915.1; -; mRNA.
DR EMBL; AL845368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004089; AAH04089.1; -; mRNA.
DR CCDS; CCDS16696.1; -.
DR RefSeq; NP_079572.2; NM_025296.4.
DR AlphaFoldDB; Q99KN2; -.
DR SMR; Q99KN2; -.
DR BioGRID; 204931; 3.
DR IntAct; Q99KN2; 4.
DR MINT; Q99KN2; -.
DR STRING; 10090.ENSMUSP00000003759; -.
DR iPTMnet; Q99KN2; -.
DR PhosphoSitePlus; Q99KN2; -.
DR EPD; Q99KN2; -.
DR MaxQB; Q99KN2; -.
DR PaxDb; Q99KN2; -.
DR PeptideAtlas; Q99KN2; -.
DR PRIDE; Q99KN2; -.
DR ProteomicsDB; 283554; -.
DR Antibodypedia; 17416; 245 antibodies from 29 providers.
DR DNASU; 26371; -.
DR Ensembl; ENSMUST00000003759; ENSMUSP00000003759; ENSMUSG00000003662.
DR GeneID; 26371; -.
DR KEGG; mmu:26371; -.
DR UCSC; uc008mfb.2; mouse.
DR CTD; 9391; -.
DR MGI; MGI:1346998; Ciao1.
DR VEuPathDB; HostDB:ENSMUSG00000003662; -.
DR eggNOG; KOG0645; Eukaryota.
DR GeneTree; ENSGT00940000158670; -.
DR InParanoid; Q99KN2; -.
DR OMA; AIWSKSS; -.
DR OrthoDB; 793298at2759; -.
DR PhylomeDB; Q99KN2; -.
DR TreeFam; TF318181; -.
DR BioGRID-ORCS; 26371; 29 hits in 77 CRISPR screens.
DR ChiTaRS; Ciao1; mouse.
DR PRO; PR:Q99KN2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99KN2; protein.
DR Bgee; ENSMUSG00000003662; Expressed in heart right ventricle and 270 other tissues.
DR ExpressionAtlas; Q99KN2; baseline and differential.
DR Genevisible; Q99KN2; MM.
DR GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0071817; C:MMXD complex; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03037; ciao1; 1.
DR InterPro; IPR028608; CIAO1/Cia1.
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 PANTHER; PTHR19920; PTHR19920; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Chromosome partition; Cytoplasm; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..339
FT /note="Probable cytosolic iron-sulfur protein assembly
FT protein CIAO1"
FT /id="PRO_0000281106"
FT REPEAT 14..53
FT /note="WD 1"
FT REPEAT 59..98
FT /note="WD 2"
FT REPEAT 103..142
FT /note="WD 3"
FT REPEAT 148..187
FT /note="WD 4"
FT REPEAT 192..231
FT /note="WD 5"
FT REPEAT 250..289
FT /note="WD 6"
FT REPEAT 301..339
FT /note="WD 7"
FT MOTIF 176..178
FT /note="LYR motif; required for interaction with HSC20"
FT /evidence="ECO:0000250|UniProtKB:O76071"
FT CONFLICT 65
FT /note="R -> M (in Ref. 1; BAB22008)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="S -> N (in Ref. 1; BAB22008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37633 MW; 302A9FCD8E110FC0 CRC64;
MKDSLVLQSR VPAHPDSRCW FLAWNPSGTL LASCGGDRKI RIWGTEGDSW ICKSVLSEGH
QRTVRKVAWS PCGNYLASAS FDATTCIWKK NQDDFECVTT LEGHENEVKS VAWAPSGNLL
ATCSRDKSVW VWEVDEEDEY ECVSVLSSHT QDVKHVVWHP SQELLASASY DDTVKLYQEE
GDDWVCCATL EGHESTVWSI AFDPSGQRLA SCSDDRTVRI WRQYLPGNEQ GVACSGSDPS
WKCICTLSGF HTRTIYDVAW CQLTGALATA CGDDAIRVFE EDPGSDPQQP TFSLTAHLRQ
AHSQDVNCVA WNPKEPGLLA SCSDDGEVAF WEYHQPAGL
