ID   CIAO3_PONAB             Reviewed;         476 AA.
AC   Q5RF36;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
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 {ECO:0000250|UniProtKB:Q9H6Q4};
GN   Synonyms=NARFL {ECO:0000250|UniProtKB:Q9H6Q4};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR857325; CAH89621.1; -; mRNA.
DR   RefSeq; NP_001124725.1; NM_001131253.1.
DR   AlphaFoldDB; Q5RF36; -.
DR   SMR; Q5RF36; -.
DR   STRING; 9601.ENSPPYP00000007848; -.
DR   GeneID; 100171574; -.
DR   KEGG; pon:100171574; -.
DR   CTD; 64428; -.
DR   eggNOG; KOG2439; Eukaryota.
DR   InParanoid; Q5RF36; -.
DR   OrthoDB; 705416at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   4Fe-4S; Acetylation; Iron; Iron-sulfur; 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_0000288487"
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"
SQ   SEQUENCE   476 AA;  52986 MW;  B44BFE6E37224879 CRC64;
     MASPFSGALQ LTDLDDFIGP SQECIKPVKV EKRAGSGVAK IRIEDDGSYF QINQDGGTRR
     LEKAKVSLND CLACSGCITS AETVLITQQS HEELKKVLDA NKMVAPSQQR LVVVSVSPQS
     RASLAARFQL NPTDTARKLT SFFKKIGVHF VFDTAFSRHF SLLESQREFV RRFRGQADCK
     QALPLLASAC PGWICYAEKT HGSFILPHIS TARSPQQVMG SLVKDFFAQQ QHLTPDKIYH
     VTVMPCYDKK LEASRPDFFN QEHQTRDVDC VLTTGEVFRL LEEEGVSLPD LEPAPLDSLC
     SGASAEEPTS HRGGGSGGYL EHVFRHAARE LFGIHVAEVT YKPLRNKDFQ EVTLEKEGQV
     LLHLAMAYGF RNIQNLVQRL KRGRCPYHYV EVMACPSGCL NGGGQLQAPD RPSRELLQHV
     ERLYGMVRAE APEDAPGVQE LYTHWLQGTD SECAGRLLHT QYHAVEKAST GLGIRW