BOLA2_HUMAN
ID BOLA2_HUMAN Reviewed; 86 AA.
AC Q9H3K6; A1L454; A7YDY3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=BolA-like protein 2;
GN Name=BOLA2; Synonyms=BOLA2A; ORFNames=My016;
GN and
GN Name=BOLA2B;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Huang X.Y., Ying K., Dai J.L.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Kidney;
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 [3]
RP PROTEIN SEQUENCE OF 1-9, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [4]
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 [5]
RP INTERACTION WITH GLRX3.
RX PubMed=22309771; DOI=10.1021/bi2019089;
RA Li H., Mapolelo D.T., Randeniya S., Johnson M.K., Outten C.E.;
RT "Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2.";
RL Biochemistry 51:1687-1696(2012).
RN [6]
RP FUNCTION, AND INTERACTION WITH GLRX3.
RX PubMed=26613676; DOI=10.1021/jacs.5b10592;
RA Banci L., Camponeschi F., Ciofi-Baffoni S., Muzzioli R.;
RT "Elucidating the molecular function of human BOLA2 in GRX3-dependent
RT anamorsin maturation pathway.";
RL J. Am. Chem. Soc. 137:16133-16143(2015).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=22746225; DOI=10.1089/ars.2011.4253;
RA Willems P., Wanschers B.F., Esseling J., Szklarczyk R., Kudla U.,
RA Duarte I., Forkink M., Nooteboom M., Swarts H., Gloerich J., Nijtmans L.,
RA Koopman W., Huynen M.A.;
RT "BOLA1 is an aerobic protein that prevents mitochondrial morphology changes
RT induced by glutathione depletion.";
RL Antioxid. Redox Signal. 18:129-138(2013).
RN [8]
RP FUNCTION, AND INTERACTION WITH GLRX3.
RX PubMed=27519415; DOI=10.1074/jbc.m116.744946;
RA Frey A.G., Palenchar D.J., Wildemann J.D., Philpott C.C.;
RT "A glutaredoxin-BolA complex serves as an iron-sulfur cluster chaperone for
RT the cytosolic cluster assembly machinery.";
RL J. Biol. Chem. 291:22344-22356(2016).
CC -!- FUNCTION: Acts as a cytosolic iron-sulfur (Fe-S) cluster assembly
CC factor that facilitates [2Fe-2S] cluster insertion into a subset of
CC cytosolic proteins (PubMed:26613676, PubMed:27519415). Acts together
CC with the monothiol glutaredoxin GLRX3 (PubMed:26613676,
CC PubMed:27519415). {ECO:0000269|PubMed:26613676,
CC ECO:0000269|PubMed:27519415}.
CC -!- SUBUNIT: Interacts with GLRX3; forms a heterotrimeric complex composed
CC by two BOLA2 molecules and one GLRX3 molecule; linked by [2Fe-2S]
CC clusters (PubMed:22309771, PubMed:26613676, PubMed:27519415).
CC {ECO:0000269|PubMed:22309771, ECO:0000269|PubMed:26613676,
CC ECO:0000269|PubMed:27519415}.
CC -!- INTERACTION:
CC Q9H3K6; Q6FI81: CIAPIN1; NbExp=2; IntAct=EBI-1642537, EBI-750511;
CC Q9H3K6; O76003: GLRX3; NbExp=3; IntAct=EBI-1642537, EBI-374781;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22746225}. Nucleus
CC {ECO:0000269|PubMed:22746225}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H3K6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H3K6-2; Sequence=VSP_010092, VSP_010093;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BolA/IbaG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22832.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI30402.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI30404.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI37533.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI37535.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI44689.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AF060511; AAG43129.1; -; mRNA.
DR EMBL; BC022832; AAH22832.1; ALT_INIT; mRNA.
DR EMBL; BC062756; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC130401; AAI30402.1; ALT_INIT; mRNA.
DR EMBL; BC130403; AAI30404.1; ALT_INIT; mRNA.
DR EMBL; BC137532; AAI37533.1; ALT_INIT; mRNA.
DR EMBL; BC137534; AAI37535.1; ALT_INIT; mRNA.
DR EMBL; BC144688; AAI44689.1; ALT_INIT; mRNA.
DR CCDS; CCDS32426.1; -. [Q9H3K6-1]
DR CCDS; CCDS32430.1; -. [Q9H3K6-1]
DR RefSeq; NP_001026997.1; NM_001031827.2. [Q9H3K6-1]
DR RefSeq; NP_001034271.1; NM_001039182.2. [Q9H3K6-1]
DR RefSeq; NP_001307508.1; NM_001320579.1.
DR RefSeq; XP_016855107.1; XM_016999618.1.
DR AlphaFoldDB; Q9H3K6; -.
DR SMR; Q9H3K6; -.
DR BioGRID; 139268; 106.
DR BioGRID; 576388; 56.
DR ComplexPortal; CPX-6861; BOLA2-GLRX3 iron-sulfur cluster assembly complex.
DR CORUM; Q9H3K6; -.
DR IntAct; Q9H3K6; 27.
DR MINT; Q9H3K6; -.
DR STRING; 9606.ENSP00000306752; -.
DR GlyGen; Q9H3K6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H3K6; -.
DR MetOSite; Q9H3K6; -.
DR PhosphoSitePlus; Q9H3K6; -.
DR BioMuta; BOLA2; -.
DR DMDM; 46577124; -.
DR EPD; Q9H3K6; -.
DR jPOST; Q9H3K6; -.
DR MassIVE; Q9H3K6; -.
DR MaxQB; Q9H3K6; -.
DR PaxDb; Q9H3K6; -.
DR PeptideAtlas; Q9H3K6; -.
DR PRIDE; Q9H3K6; -.
DR ProteomicsDB; 80726; -. [Q9H3K6-1]
DR ProteomicsDB; 80727; -. [Q9H3K6-2]
DR TopDownProteomics; Q9H3K6-1; -. [Q9H3K6-1]
DR Antibodypedia; 66708; 66 antibodies from 12 providers.
DR Antibodypedia; 68804; 11 antibodies from 4 providers.
DR DNASU; 552900; -.
DR Ensembl; ENST00000330978.4; ENSP00000331127.4; ENSG00000183336.9. [Q9H3K6-1]
DR Ensembl; ENST00000651894.2; ENSP00000498355.1; ENSG00000169627.9. [Q9H3K6-1]
DR GeneID; 552900; -.
DR GeneID; 654483; -.
DR KEGG; hsa:552900; -.
DR KEGG; hsa:654483; -.
DR MANE-Select; ENST00000330978.4; ENSP00000331127.4; NM_001031827.3; NP_001026997.2.
DR MANE-Select; ENST00000651894.2; ENSP00000498355.1; NM_001039182.4; NP_001034271.2.
DR UCSC; uc002dss.3; human. [Q9H3K6-1]
DR CTD; 552900; -.
DR CTD; 654483; -.
DR DisGeNET; 552900; -.
DR DisGeNET; 654483; -.
DR GeneCards; BOLA2; -.
DR GeneCards; BOLA2B; -.
DR HGNC; HGNC:29488; BOLA2.
DR HGNC; HGNC:32479; BOLA2B.
DR HPA; ENSG00000169627; Low tissue specificity.
DR HPA; ENSG00000183336; Low tissue specificity.
DR MIM; 613182; gene.
DR neXtProt; NX_Q9H3K6; -.
DR OpenTargets; ENSG00000261740; -.
DR PharmGKB; PA143485317; -.
DR VEuPathDB; HostDB:ENSG00000169627; -.
DR VEuPathDB; HostDB:ENSG00000183336; -.
DR eggNOG; KOG0891; Eukaryota.
DR eggNOG; KOG3348; Eukaryota.
DR GeneTree; ENSGT00510000047760; -.
DR HOGENOM; CLU_152301_0_0_1; -.
DR InParanoid; Q9H3K6; -.
DR OrthoDB; 1571278at2759; -.
DR PhylomeDB; Q9H3K6; -.
DR TreeFam; TF313141; -.
DR PathwayCommons; Q9H3K6; -.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; Q9H3K6; -.
DR BioGRID-ORCS; 552900; 87 hits in 564 CRISPR screens.
DR BioGRID-ORCS; 654483; 15 hits in 241 CRISPR screens.
DR ChiTaRS; BOLA2B; human.
DR Pharos; Q9H3K6; Tbio.
DR PRO; PR:Q9H3K6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H3K6; protein.
DR Bgee; ENSG00000169627; Expressed in mucosa of transverse colon and 98 other tissues.
DR ExpressionAtlas; Q9H3K6; baseline and differential.
DR Genevisible; Q9H3K6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:ComplexPortal.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:ComplexPortal.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:UniProtKB.
DR InterPro; IPR045115; BOL2.
DR InterPro; IPR002634; BolA.
DR InterPro; IPR036065; BolA-like_sf.
DR PANTHER; PTHR12735; PTHR12735; 1.
DR Pfam; PF01722; BolA; 1.
DR PIRSF; PIRSF003113; BolA; 1.
DR SUPFAM; SSF82657; SSF82657; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Nucleus; Reference proteome.
FT CHAIN 1..86
FT /note="BolA-like protein 2"
FT /id="PRO_0000201236"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:12665801"
FT VAR_SEQ 55..58
FT /note="LVNA -> FCTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010092"
FT VAR_SEQ 59..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010093"
SQ SEQUENCE 86 AA; 10117 MW; CA95C76A225B5384 CRC64;
MELSAEYLRE KLQRDLEAEH VEVEDTTLNR CSCSFRVLVV SAKFEGKPLL QRHRLVNACL
AEELPHIHAF EQKTLTPDQW ARERQK