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Cytosolic Fe-S cluster assembly factor NARFL (Iron-only hydrogenase-like protein 1) (IOP1) (Nuclear prelamin A recognition factor-like protein) (Protein related to Narf)

 CIAO3_HUMAN             Reviewed;         476 AA.
Q9H6Q4; A1L385; B3KTJ3; Q53GC6; Q96S10; Q9H6J8;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 138.
RecName: Full=Cytosolic iron-sulfur assembly component 3 {ECO:0000305};
AltName: Full=Cytosolic Fe-S cluster assembly factor NARFL;
AltName: Full=Iron-only hydrogenase-like protein 1 {ECO:0000303|PubMed:16956324};
Short=IOP1 {ECO:0000303|PubMed:16956324};
AltName: Full=Nuclear prelamin A recognition factor-like protein;
AltName: Full=Protein related to Narf;
Name=CIAO3 {ECO:0000312|HGNC:HGNC:14179};
Synonyms=NARFL {ECO:0000312|HGNC:HGNC:14179}, PRN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Barton R.M., Worman H.J.;
"A comparison of Narf, HPRN and Nar1p in human and yeast cells.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Small intestine;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16956324; DOI=10.1042/BJ20060635;
Huang J., Song D., Flores A., Zhao Q., Mooney S.M., Shaw L.M.,
Lee F.S.;
"IOP1, a novel hydrogenase-like protein that modulates hypoxia-
inducible factor-1alpha activity.";
Biochem. J. 401:341-352(2007).
[9]
FUNCTION.
PubMed=18270200; DOI=10.1074/jbc.M708077200;
Song D., Lee F.S.;
"A role for IOP1 in mammalian cytosolic iron-sulfur protein
biogenesis.";
J. Biol. Chem. 283:9231-9238(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION IN THE CIA COMPLEX.
PubMed=22678362; DOI=10.1126/science.1219723;
Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T.,
Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.;
"MMS19 assembles iron-sulfur proteins required for DNA metabolism and
genomic integrity.";
Science 337:195-199(2012).
[13]
IDENTIFICATION IN THE CIA COMPLEX.
PubMed=22678361; DOI=10.1126/science.1219664;
Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M.,
Boulton S.J.;
"MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA
metabolism.";
Science 337:243-245(2012).
[14]
IDENTIFICATION IN THE CIA COMPLEX, AND INTERACTION WITH CIAO1 AND
MMS19.
PubMed=23585563; DOI=10.1074/jbc.M112.416602;
Seki M., Takeda Y., Iwai K., Tanaka K.;
"IOP1 protein is an external component of the human cytosolic iron-
sulfur cluster assembly (CIA) machinery and functions in the MMS19
protein-dependent CIA pathway.";
J. Biol. Chem. 288:16680-16689(2013).
-!- FUNCTION: Component of the cytosolic iron-sulfur protein assembly
(CIA) complex, a multiprotein complex that mediates the
incorporation of iron-sulfur cluster into extramitochondrial Fe/S
proteins. Seems to negatively regulate the level of HIF1A
expression, although this effect could be indirect.
{ECO:0000269|PubMed:16956324, ECO:0000269|PubMed:18270200}.
-!- SUBUNIT: External component of the CIA complex (PubMed:22678361,
PubMed:22678362, PubMed:23585563). In the CIA complex, interacts
directly with CIAO1 and MMS19 (PubMed:23585563).
{ECO:0000269|PubMed:22678361, ECO:0000269|PubMed:22678362,
ECO:0000269|PubMed:23585563}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H6Q4-1; Sequence=Displayed;
Name=2;
IsoId=Q9H6Q4-2; Sequence=VSP_025694;
Name=3;
IsoId=Q9H6Q4-3; Sequence=VSP_025695;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:16956324}.
-!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK61251.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AY129231; AAM98737.1; -; mRNA.
EMBL; AK025641; BAB15199.1; -; mRNA.
EMBL; AK025861; BAB15261.1; -; mRNA.
EMBL; AK095675; BAG53105.1; -; mRNA.
EMBL; AK223005; BAD96725.1; -; mRNA.
EMBL; AE006464; AAK61251.1; ALT_SEQ; Genomic_DNA.
EMBL; Z98258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85723.1; -; Genomic_DNA.
EMBL; BC030248; AAH30248.1; -; mRNA.
EMBL; BC129940; AAI29941.1; -; mRNA.
CCDS; CCDS10425.1; -. [Q9H6Q4-1]
CCDS; CCDS76798.1; -. [Q9H6Q4-3]
RefSeq; NP_001291728.1; NM_001304799.1. [Q9H6Q4-3]
RefSeq; NP_071938.1; NM_022493.2. [Q9H6Q4-1]
UniGene; Hs.513247; -.
ProteinModelPortal; Q9H6Q4; -.
SMR; Q9H6Q4; -.
BioGrid; 122176; 14.
CORUM; Q9H6Q4; -.
IntAct; Q9H6Q4; 1.
STRING; 9606.ENSP00000251588; -.
iPTMnet; Q9H6Q4; -.
PhosphoSitePlus; Q9H6Q4; -.
BioMuta; NARFL; -.
DMDM; 74733617; -.
EPD; Q9H6Q4; -.
MaxQB; Q9H6Q4; -.
PaxDb; Q9H6Q4; -.
PeptideAtlas; Q9H6Q4; -.
PRIDE; Q9H6Q4; -.
ProteomicsDB; 81009; -.
ProteomicsDB; 81010; -. [Q9H6Q4-2]
ProteomicsDB; 81011; -. [Q9H6Q4-3]
DNASU; 64428; -.
Ensembl; ENST00000251588; ENSP00000251588; ENSG00000103245. [Q9H6Q4-1]
Ensembl; ENST00000540986; ENSP00000444008; ENSG00000103245. [Q9H6Q4-3]
Ensembl; ENST00000568545; ENSP00000457058; ENSG00000103245. [Q9H6Q4-3]
GeneID; 64428; -.
KEGG; hsa:64428; -.
UCSC; uc002cjp.4; human. [Q9H6Q4-1]
CTD; 64428; -.
EuPathDB; HostDB:ENSG00000103245.13; -.
GeneCards; CIAO3; -.
HGNC; HGNC:14179; CIAO3.
HPA; HPA040851; -.
MIM; 611118; gene.
neXtProt; NX_Q9H6Q4; -.
OpenTargets; ENSG00000103245; -.
PharmGKB; PA128394707; -.
eggNOG; KOG2439; Eukaryota.
eggNOG; COG4624; LUCA.
GeneTree; ENSGT00940000153514; -.
HOGENOM; HOG000191744; -.
HOVERGEN; HBG055005; -.
InParanoid; Q9H6Q4; -.
OMA; QEHQTRD; -.
OrthoDB; EOG091G0BWP; -.
PhylomeDB; Q9H6Q4; -.
TreeFam; TF106273; -.
Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
ChiTaRS; NARFL; human.
GenomeRNAi; 64428; -.
PRO; PR:Q9H6Q4; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103245; Expressed in 163 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_NARFL; -.
ExpressionAtlas; Q9H6Q4; baseline and differential.
Genevisible; Q9H6Q4; HS.
GO; GO:0097361; C:CIA complex; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
GO; GO:0032364; P:oxygen homeostasis; IDA:HGNC.
GO; GO:0010468; P:regulation of gene expression; IDA:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IDA:HGNC.
InterPro; IPR009016; Fe_hydrogenase.
InterPro; IPR004108; Fe_hydrogenase_lsu_C.
InterPro; IPR003149; Fe_hydrogenase_ssu.
Pfam; PF02906; Fe_hyd_lg_C; 1.
Pfam; PF02256; Fe_hyd_SSU; 1.
SMART; SM00902; Fe_hyd_SSU; 1.
SUPFAM; SSF53920; SSF53920; 1.
1: Evidence at protein level;
4Fe-4S; Acetylation; Alternative splicing; Complete proteome; Iron;
Iron-sulfur; Metal-binding; Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231}.
CHAIN 2 476 Cytosolic iron-sulfur assembly component
3.
/FTId=PRO_0000288485.
METAL 24 24 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
METAL 71 71 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
METAL 74 74 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
METAL 77 77 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
METAL 190 190 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
METAL 246 246 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
METAL 395 395 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
METAL 399 399 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 243 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_025694.
VAR_SEQ 1 102 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_025695.
VARIANT 38 38 V -> M (in dbSNP:rs8045850).
/FTId=VAR_053911.
VARIANT 444 444 H -> R (in dbSNP:rs7188554).
/FTId=VAR_053912.
CONFLICT 205 205 I -> T (in Ref. 3; BAD96725).
{ECO:0000305}.
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


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