CIAO3_MOUSE
ID CIAO3_MOUSE Reviewed; 476 AA.
AC Q7TMW6; Q3ULM7; Q8BRR3; Q9CXS6; Q9D320;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cytosolic iron-sulfur assembly component 3 {ECO:0000305};
DE AltName: Full=Cytosolic Fe-S cluster assembly factor NARFL;
DE AltName: Full=Iron-only hydrogenase-like protein 1;
DE Short=IOP1;
DE AltName: Full=Nuclear prelamin A recognition factor-like protein;
GN Name=Ciao3; Synonyms=Narfl {ECO:0000312|MGI:MGI:1914813};
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 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Colon, and Head;
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=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Pancreas, and Spleen;
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).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA)
CC complex, a multiprotein complex that mediates the incorporation of
CC iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to
CC negatively regulate the level of HIF1A expression, although this effect
CC could be indirect (By similarity). {ECO:0000250|UniProtKB:Q9H6Q4}.
CC -!- SUBUNIT: External component of the CIA complex. In the CIA complex,
CC interacts directly with CIAO1 and MMS19.
CC {ECO:0000250|UniProtKB:Q9H6Q4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TMW6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TMW6-2; Sequence=VSP_025696;
CC -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
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DR EMBL; AK014038; BAB29126.1; -; mRNA.
DR EMBL; AK018548; BAB31268.1; -; mRNA.
DR EMBL; AK043694; BAC31620.1; -; mRNA.
DR EMBL; AK145408; BAE26421.1; -; mRNA.
DR EMBL; BC052830; AAH52830.1; -; mRNA.
DR CCDS; CCDS50034.1; -. [Q7TMW6-1]
DR RefSeq; NP_080514.3; NM_026238.4. [Q7TMW6-1]
DR AlphaFoldDB; Q7TMW6; -.
DR SMR; Q7TMW6; -.
DR BioGRID; 212278; 1.
DR STRING; 10090.ENSMUSP00000002350; -.
DR iPTMnet; Q7TMW6; -.
DR PhosphoSitePlus; Q7TMW6; -.
DR EPD; Q7TMW6; -.
DR MaxQB; Q7TMW6; -.
DR PaxDb; Q7TMW6; -.
DR PeptideAtlas; Q7TMW6; -.
DR PRIDE; Q7TMW6; -.
DR ProteomicsDB; 252775; -. [Q7TMW6-1]
DR ProteomicsDB; 252776; -. [Q7TMW6-2]
DR Antibodypedia; 42404; 196 antibodies from 28 providers.
DR Ensembl; ENSMUST00000002350; ENSMUSP00000002350; ENSMUSG00000002280. [Q7TMW6-1]
DR Ensembl; ENSMUST00000134108; ENSMUSP00000117136; ENSMUSG00000002280. [Q7TMW6-2]
DR GeneID; 67563; -.
DR KEGG; mmu:67563; -.
DR UCSC; uc008bbq.2; mouse. [Q7TMW6-1]
DR UCSC; uc012anj.1; mouse. [Q7TMW6-2]
DR CTD; 64428; -.
DR MGI; MGI:1914813; Ciao3.
DR VEuPathDB; HostDB:ENSMUSG00000002280; -.
DR eggNOG; KOG2439; Eukaryota.
DR GeneTree; ENSGT00940000153514; -.
DR HOGENOM; CLU_018240_0_0_1; -.
DR InParanoid; Q7TMW6; -.
DR OMA; PHEQRAW; -.
DR OrthoDB; 705416at2759; -.
DR PhylomeDB; Q7TMW6; -.
DR TreeFam; TF106273; -.
DR BioGRID-ORCS; 67563; 29 hits in 75 CRISPR screens.
DR PRO; PR:Q7TMW6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q7TMW6; protein.
DR Bgee; ENSMUSG00000002280; Expressed in proximal tubule and 69 other tissues.
DR ExpressionAtlas; Q7TMW6; baseline and differential.
DR Genevisible; Q7TMW6; MM.
DR GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:MGI.
DR GO; GO:0032364; P:oxygen homeostasis; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR003149; Fe_hydrogenase_ssu.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF02256; Fe_hyd_SSU; 1.
DR SMART; SM00902; Fe_hyd_SSU; 1.
DR SUPFAM; SSF53920; SSF53920; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; Alternative splicing; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Q4"
FT CHAIN 2..476
FT /note="Cytosolic iron-sulfur assembly component 3"
FT /id="PRO_0000288486"
FT REGION 297..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 190
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 246
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 395
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 399
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Q4"
FT VAR_SEQ 299
FT /note="L -> LDLSCVAPPALTRPSPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025696"
FT CONFLICT 286
FT /note="V -> A (in Ref. 2; AAH52830)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="K -> T (in Ref. 1; BAB29126)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="E -> G (in Ref. 1; BAC31620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53108 MW; E9ACAA9A826173E5 CRC64;
MASPFSGALQ LTDLDDFIGP SQNCIKPVKV AKKPGSGIAK IHIEDDGSYF QVNQDGRTQK
LEKAKVSLND CLACSGCVTS AETVLITQQS HEELRKVLDA NKEAAPGQQR LVVVSISPQS
RASLAARFRL DPTDTARKLT SFFKKIGVHF VFDTAFARNF SLLESQKEFV QRFREQANSR
EALPVLASAC PGWICYAEKT HGNFILPYIS TARSPQQVMG SLVKDFFAQQ QLLTPDKIYH
VTVMPCYDKK LEASRPDFFN QEYQTRDVDC VLTTGEVFRL LEEEGVSLTE LEPAPLDGLT
SSVSAEEPSS HRGGGSGGYL EHVFRHAAQE LFGIHVAEVT YQPLRNKDFQ EVTLEREGQV
LLRFAVAYGF RNIQNLVQKL KRGRCPYHYV EVMACPSGCL NGGGQLKAPD TEGSELLQQL
ERLYSMVRTE APEDAPGVQE LYQHWLQGED SERASRLLHT QYHAVEKPSS GLSIRW
