CIAO3_RAT
ID CIAO3_RAT Reviewed; 476 AA.
AC Q5BK18;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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:0000312|RGD:1305982};
GN Synonyms=Narfl {ECO:0000312|RGD:1305982};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
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; BC091240; AAH91240.1; -; mRNA.
DR RefSeq; NP_001013201.1; NM_001013183.1.
DR AlphaFoldDB; Q5BK18; -.
DR SMR; Q5BK18; -.
DR STRING; 10116.ENSRNOP00000026518; -.
DR iPTMnet; Q5BK18; -.
DR PhosphoSitePlus; Q5BK18; -.
DR PaxDb; Q5BK18; -.
DR PRIDE; Q5BK18; -.
DR GeneID; 360496; -.
DR KEGG; rno:360496; -.
DR UCSC; RGD:1305982; rat.
DR CTD; 64428; -.
DR RGD; 1305982; Ciao3.
DR VEuPathDB; HostDB:ENSRNOG00000019522; -.
DR eggNOG; KOG2439; Eukaryota.
DR HOGENOM; CLU_018240_0_0_1; -.
DR InParanoid; Q5BK18; -.
DR OMA; PHEQRAW; -.
DR OrthoDB; 705416at2759; -.
DR PRO; PR:Q5BK18; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000019522; Expressed in heart and 20 other tissues.
DR Genevisible; Q5BK18; RN.
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; ISO:RGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0032364; P:oxygen homeostasis; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
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_0000288488"
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; 53167 MW; DF0909D3A058D349 CRC64;
MASPFSGALQ LTDLDDFIGP SQSCIKPVTV AKKPGSGIAK IHIEDDGSYF QVNPDGRSQK
LEKAKVSLND CLACSGCVTS AETILITQQS HEELRKVLDA NKVAAPGQQR LVVVSVSPQS
RASLAARFQL DSTDTARKLT SFFKKIGVHF VFDTAFARNF SLLESQKEFV QRFREQANSR
EALPMLASAC PGWICYAEKT HGNFILPYIS TARSPQQVMG SLIKDFFAQQ QLLTPDKIYH
VTVMPCYDKK LEASRPDFFN QEYQTRDVDC VLTTGEVFRL LEEEGVSLSE LEPVPLDGLT
RSVSAEEPTS HRGGGSGGYL EHVFRHAAQE LFGIHVADVT YQPMRNKDFQ EVTLEREGQV
LLRFAVAYGF RNIQNLVQKL KRGRCPYHYV EVMACPSGCL NGGGQLKAPD TEGRELLQQV
ERLYSMVRTE APEDAPGVQE LYQHWLQGED SERASHLLHT QYHAVEKINS GLSIRW
