CIAO3_BOVIN
ID CIAO3_BOVIN Reviewed; 476 AA.
AC A4FV58;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A4FV58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A4FV58-2; Sequence=VSP_025692, VSP_025693;
CC -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
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DR EMBL; BC123768; AAI23769.1; -; mRNA.
DR RefSeq; NP_001076880.2; NM_001083411.2.
DR AlphaFoldDB; A4FV58; -.
DR SMR; A4FV58; -.
DR STRING; 9913.ENSBTAP00000003225; -.
DR PaxDb; A4FV58; -.
DR PRIDE; A4FV58; -.
DR Ensembl; ENSBTAT00000003225; ENSBTAP00000003225; ENSBTAG00000002484. [A4FV58-1]
DR Ensembl; ENSBTAT00000086575; ENSBTAP00000062441; ENSBTAG00000002484. [A4FV58-2]
DR GeneID; 511837; -.
DR KEGG; bta:511837; -.
DR CTD; 64428; -.
DR VEuPathDB; HostDB:ENSBTAG00000002484; -.
DR eggNOG; KOG2439; Eukaryota.
DR GeneTree; ENSGT00940000153514; -.
DR HOGENOM; CLU_018240_0_0_1; -.
DR InParanoid; A4FV58; -.
DR OMA; PHEQRAW; -.
DR OrthoDB; 705416at2759; -.
DR TreeFam; TF106273; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000002484; Expressed in laryngeal cartilage and 105 other tissues.
DR ExpressionAtlas; A4FV58; baseline and differential.
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; IEA:Ensembl.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0032364; P:oxygen homeostasis; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
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; 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_0000288484"
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 300..362
FT /note="CSSASAQEPTSHQGGGSGGYLEHVFRHAAQELFGIHVTEVTYRPLRNKDLQE
FT VILEREGQVLL -> YVITGPVGGAVSSPSTGCSPPGGSRRSGQAAGGAVALNAGTGLL
FT PFLWPGLPRPLVCLSVQDT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025692"
FT VAR_SEQ 363..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025693"
SQ SEQUENCE 476 AA; 52606 MW; 204F42C5FB858DA1 CRC64;
MASPFSGALQ LTDLDDFIAP SQDCIKPMKV DRRPGSGVAK IHIEDDGSYF QVSQDGGMKK
LEKAKISLDD CLACSGCVTS AETVLITQQS HEELRKVLGA NKTAAPDQQK LVVISVSPQS
RASLAVRFQL NPTDTARKLT AFFKKIGAHY VFDTAFSRNF SLLESQREFV RRFRGQADPE
QALPVLTSAC PGWICYAEKT HGSTLLPHIS TARSPQQVMG SLVKDFFAQQ QHLTPDKVYH
ATVMPCYDKK LEASRPDFFS QEHQTRDVDC VITTGEVFKL LEEEGVSLSE LEPAPLDSLC
SSASAQEPTS HQGGGSGGYL EHVFRHAAQE LFGIHVTEVT YRPLRNKDLQ EVILEREGQV
LLHFAAAYGF RNIQNLVQKL KRGRCPYHYV EVMACPAGCL NGGGQLKAPD MPGKELLQQV
ERLYGLVRTE APEDAPGIQE LYERWLQGAG SERAGRLLHT SYHAVEKAGS GLSIRW
