CIAO3_HUMAN
ID CIAO3_HUMAN Reviewed; 476 AA.
AC Q9H6Q4; A1L385; B3KTJ3; Q53GC6; Q96S10; Q9H6J8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
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 {ECO:0000303|PubMed:16956324};
DE Short=IOP1 {ECO:0000303|PubMed:16956324};
DE AltName: Full=Nuclear prelamin A recognition factor-like protein;
DE AltName: Full=Protein related to Narf;
GN Name=CIAO3 {ECO:0000312|HGNC:HGNC:14179};
GN Synonyms=NARFL {ECO:0000312|HGNC:HGNC:14179}, PRN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Barton R.M., Worman H.J.;
RT "A comparison of Narf, HPRN and Nar1p in human and yeast cells.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16956324; DOI=10.1042/bj20060635;
RA Huang J., Song D., Flores A., Zhao Q., Mooney S.M., Shaw L.M., Lee F.S.;
RT "IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible
RT factor-1alpha activity.";
RL Biochem. J. 401:341-352(2007).
RN [9]
RP FUNCTION.
RX PubMed=18270200; DOI=10.1074/jbc.m708077200;
RA Song D., Lee F.S.;
RT "A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis.";
RL J. Biol. Chem. 283:9231-9238(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION IN THE CIA COMPLEX.
RX PubMed=22678362; DOI=10.1126/science.1219723;
RA Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T.,
RA Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "MMS19 assembles iron-sulfur proteins required for DNA metabolism and
RT genomic integrity.";
RL Science 337:195-199(2012).
RN [13]
RP IDENTIFICATION IN THE CIA COMPLEX.
RX PubMed=22678361; DOI=10.1126/science.1219664;
RA Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M., Boulton S.J.;
RT "MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism.";
RL Science 337:243-245(2012).
RN [14]
RP IDENTIFICATION IN THE CIA COMPLEX, AND INTERACTION WITH CIAO1 AND MMS19.
RX PubMed=23585563; DOI=10.1074/jbc.m112.416602;
RA Seki M., Takeda Y., Iwai K., Tanaka K.;
RT "IOP1 protein is an external component of the human cytosolic iron-sulfur
RT cluster assembly (CIA) machinery and functions in the MMS19 protein-
RT dependent CIA pathway.";
RL J. Biol. Chem. 288:16680-16689(2013).
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. {ECO:0000269|PubMed:16956324,
CC ECO:0000269|PubMed:18270200}.
CC -!- SUBUNIT: External component of the CIA complex (PubMed:22678361,
CC PubMed:22678362, PubMed:23585563). In the CIA complex, interacts
CC directly with CIAO1 and MMS19 (PubMed:23585563).
CC {ECO:0000269|PubMed:22678361, ECO:0000269|PubMed:22678362,
CC ECO:0000269|PubMed:23585563}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H6Q4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6Q4-2; Sequence=VSP_025694;
CC Name=3;
CC IsoId=Q9H6Q4-3; Sequence=VSP_025695;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16956324}.
CC -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK61251.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY129231; AAM98737.1; -; mRNA.
DR EMBL; AK025641; BAB15199.1; -; mRNA.
DR EMBL; AK025861; BAB15261.1; -; mRNA.
DR EMBL; AK095675; BAG53105.1; -; mRNA.
DR EMBL; AK223005; BAD96725.1; -; mRNA.
DR EMBL; AE006464; AAK61251.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z98258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85723.1; -; Genomic_DNA.
DR EMBL; BC030248; AAH30248.1; -; mRNA.
DR EMBL; BC129940; AAI29941.1; -; mRNA.
DR CCDS; CCDS10425.1; -. [Q9H6Q4-1]
DR CCDS; CCDS76798.1; -. [Q9H6Q4-3]
DR RefSeq; NP_001291728.1; NM_001304799.1. [Q9H6Q4-3]
DR RefSeq; NP_071938.1; NM_022493.2. [Q9H6Q4-1]
DR AlphaFoldDB; Q9H6Q4; -.
DR SMR; Q9H6Q4; -.
DR BioGRID; 122176; 25.
DR CORUM; Q9H6Q4; -.
DR IntAct; Q9H6Q4; 7.
DR STRING; 9606.ENSP00000251588; -.
DR iPTMnet; Q9H6Q4; -.
DR MetOSite; Q9H6Q4; -.
DR PhosphoSitePlus; Q9H6Q4; -.
DR BioMuta; NARFL; -.
DR DMDM; 74733617; -.
DR EPD; Q9H6Q4; -.
DR jPOST; Q9H6Q4; -.
DR MassIVE; Q9H6Q4; -.
DR MaxQB; Q9H6Q4; -.
DR PaxDb; Q9H6Q4; -.
DR PeptideAtlas; Q9H6Q4; -.
DR PRIDE; Q9H6Q4; -.
DR ProteomicsDB; 81009; -. [Q9H6Q4-1]
DR ProteomicsDB; 81010; -. [Q9H6Q4-2]
DR ProteomicsDB; 81011; -. [Q9H6Q4-3]
DR Antibodypedia; 42404; 196 antibodies from 28 providers.
DR DNASU; 64428; -.
DR Ensembl; ENST00000251588.7; ENSP00000251588.2; ENSG00000103245.14. [Q9H6Q4-1]
DR Ensembl; ENST00000540986.5; ENSP00000444008.1; ENSG00000103245.14. [Q9H6Q4-3]
DR Ensembl; ENST00000568545.5; ENSP00000457058.1; ENSG00000103245.14. [Q9H6Q4-3]
DR GeneID; 64428; -.
DR KEGG; hsa:64428; -.
DR MANE-Select; ENST00000251588.7; ENSP00000251588.2; NM_022493.3; NP_071938.1.
DR UCSC; uc002cjp.4; human. [Q9H6Q4-1]
DR CTD; 64428; -.
DR DisGeNET; 64428; -.
DR GeneCards; CIAO3; -.
DR HGNC; HGNC:14179; CIAO3.
DR HPA; ENSG00000103245; Low tissue specificity.
DR MIM; 611118; gene.
DR neXtProt; NX_Q9H6Q4; -.
DR OpenTargets; ENSG00000103245; -.
DR PharmGKB; PA128394707; -.
DR VEuPathDB; HostDB:ENSG00000103245; -.
DR eggNOG; KOG2439; Eukaryota.
DR GeneTree; ENSGT00940000153514; -.
DR HOGENOM; CLU_018240_0_0_1; -.
DR InParanoid; Q9H6Q4; -.
DR OMA; PHEQRAW; -.
DR OrthoDB; 705416at2759; -.
DR PhylomeDB; Q9H6Q4; -.
DR TreeFam; TF106273; -.
DR PathwayCommons; Q9H6Q4; -.
DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
DR SignaLink; Q9H6Q4; -.
DR BioGRID-ORCS; 64428; 799 hits in 1083 CRISPR screens.
DR ChiTaRS; CIAO3; human.
DR GenomeRNAi; 64428; -.
DR Pharos; Q9H6Q4; Tbio.
DR PRO; PR:Q9H6Q4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H6Q4; protein.
DR Bgee; ENSG00000103245; Expressed in apex of heart and 123 other tissues.
DR ExpressionAtlas; Q9H6Q4; baseline and differential.
DR Genevisible; Q9H6Q4; HS.
DR GO; GO:0097361; C:CIA complex; IDA: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; IEA:Ensembl.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0032364; P:oxygen homeostasis; IDA:HGNC-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IDA:HGNC-UCL.
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:0007744|PubMed:20068231"
FT CHAIN 2..476
FT /note="Cytosolic iron-sulfur assembly component 3"
FT /id="PRO_0000288485"
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:0007744|PubMed:20068231"
FT VAR_SEQ 1..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025694"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025695"
FT VARIANT 38
FT /note="V -> M (in dbSNP:rs8045850)"
FT /id="VAR_053911"
FT VARIANT 444
FT /note="H -> R (in dbSNP:rs7188554)"
FT /id="VAR_053912"
FT CONFLICT 205
FT /note="I -> T (in Ref. 3; BAD96725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53020 MW; 88A019DA4D7988EA CRC64;
MASPFSGALQ LTDLDDFIGP SQECIKPVKV EKRAGSGVAK IRIEDDGSYF QINQDGGTRR
LEKAKVSLND CLACSGCITS AETVLITQQS HEELKKVLDA NKMAAPSQQR LVVVSVSPQS
RASLAARFQL NPTDTARKLT SFFKKIGVHF VFDTAFSRHF SLLESQREFV RRFRGQADCR
QALPLLASAC PGWICYAEKT HGSFILPHIS TARSPQQVMG SLVKDFFAQQ QHLTPDKIYH
VTVMPCYDKK LEASRPDFFN QEHQTRDVDC VLTTGEVFRL LEEEGVSLPD LEPAPLDSLC
SGASAEEPTS HRGGGSGGYL EHVFRHAARE LFGIHVAEVT YKPLRNKDFQ EVTLEKEGQV
LLHFAMAYGF RNIQNLVQRL KRGRCPYHYV EVMACPSGCL NGGGQLQAPD RPSRELLQHV
ERLYGMVRAE APEDAPGVQE LYTHWLQGTD SECAGRLLHT QYHAVEKAST GLGIRW
