NUBP2_BOVIN
ID NUBP2_BOVIN Reviewed; 271 AA.
AC Q3MHY6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP2 {ECO:0000255|HAMAP-Rule:MF_03039};
DE AltName: Full=Nucleotide-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_03039};
DE Short=NBP 2 {ECO:0000255|HAMAP-Rule:MF_03039};
GN Name=NUBP2 {ECO:0000255|HAMAP-Rule:MF_03039};
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 MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC assembly (CIA) machinery. Required for maturation of extramitochondrial
CC Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold
CC complex, mediating the de novo assembly of an Fe-S cluster and its
CC transfer to target apoproteins. Negatively regulates cilium formation
CC and structure. {ECO:0000250|UniProtKB:Q9R061, ECO:0000255|HAMAP-
CC Rule:MF_03039}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03039};
CC Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable
CC clusters in the N-termini of NUBP1 and two labile, bridging clusters
CC between subunits of the NUBP1-NUBP2 heterotetramer. {ECO:0000255|HAMAP-
CC Rule:MF_03039};
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts with
CC KIFC1. Interacts with NUBP1. {ECO:0000250|UniProtKB:Q9R061,
CC ECO:0000255|HAMAP-Rule:MF_03039}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03039}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000255|HAMAP-Rule:MF_03039}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9R061}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q9R061}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q9R061}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000250|UniProtKB:Q9R061}. Note=Enriched at the
CC centrosomes during mitosis. Enriched in centrioles of microtubule
CC asters during prophase, prometaphase and telophase stages of mitosis
CC (By similarity). Localized at centrioles and in the nucleus at
CC interphase (By similarity). Colocalizes with nubp-1 at prometaphase (By
CC similarity). {ECO:0000250|UniProtKB:Q9R061, ECO:0000255|HAMAP-
CC Rule:MF_03039}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP2/CFD1 subfamily. {ECO:0000255|HAMAP-Rule:MF_03039}.
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DR EMBL; BC104526; AAI04527.1; -; mRNA.
DR RefSeq; NP_001029677.1; NM_001034505.1.
DR AlphaFoldDB; Q3MHY6; -.
DR SMR; Q3MHY6; -.
DR STRING; 9913.ENSBTAP00000022029; -.
DR PaxDb; Q3MHY6; -.
DR PRIDE; Q3MHY6; -.
DR Ensembl; ENSBTAT00000022029; ENSBTAP00000022029; ENSBTAG00000016561.
DR GeneID; 515660; -.
DR KEGG; bta:515660; -.
DR CTD; 10101; -.
DR VEuPathDB; HostDB:ENSBTAG00000016561; -.
DR VGNC; VGNC:32316; NUBP2.
DR eggNOG; KOG3022; Eukaryota.
DR GeneTree; ENSGT00950000183193; -.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; Q3MHY6; -.
DR OMA; QGWVPVY; -.
DR OrthoDB; 1166096at2759; -.
DR TreeFam; TF354321; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000016561; Expressed in retina and 106 other tissues.
DR ExpressionAtlas; Q3MHY6; baseline and differential.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03039; NUBP2; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264; PTHR23264; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Acetylation; ATP-binding; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..271
FT /note="Cytosolic Fe-S cluster assembly factor NUBP2"
FT /id="PRO_0000288716"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Y2, ECO:0000255|HAMAP-
FT Rule:MF_03039"
SQ SEQUENCE 271 AA; 28789 MW; F02C30153981F90C CRC64;
MEAAAEPGNL AGVRHIVLVL SGKGGVGKST ISTELALALR HAGKKVGILD VDLCGPSIPR
MLRAQGRAVH QGDSGWVPVF VDREQSISLM SVGFLLEQPD EAVVWRGPKK NALIKQFVSD
VAWGQLDYLL VDTPPGTSDE HMAVVDALRP HSPLGALVVT TPQAVSVGDV RRELTFCRKV
GLRVIGLVEN MSGFVCPHCS ECTNVFSKGG GEELARHAGV PFLGSVPLDP ELTRSLEDGR
DFIQDFPDSP AFPALSSIAQ KILSETPAGL S
