NUBP2_RAT
ID NUBP2_RAT Reviewed; 271 AA.
AC Q68FS1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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;
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=Testis;
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 [2]
RP PROTEIN SEQUENCE OF 15-23; 29-40 AND 249-261, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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; BC079386; AAH79386.1; -; mRNA.
DR RefSeq; NP_001011891.1; NM_001011891.1.
DR AlphaFoldDB; Q68FS1; -.
DR SMR; Q68FS1; -.
DR STRING; 10116.ENSRNOP00000020504; -.
DR jPOST; Q68FS1; -.
DR PaxDb; Q68FS1; -.
DR PRIDE; Q68FS1; -.
DR Ensembl; ENSRNOT00000020504; ENSRNOP00000020504; ENSRNOG00000015090.
DR GeneID; 287125; -.
DR KEGG; rno:287125; -.
DR UCSC; RGD:1305113; rat.
DR CTD; 10101; -.
DR RGD; 1305113; Nubp2.
DR eggNOG; KOG3022; Eukaryota.
DR GeneTree; ENSGT00950000183193; -.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; Q68FS1; -.
DR OMA; QGWVPVY; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; Q68FS1; -.
DR TreeFam; TF354321; -.
DR PRO; PR:Q68FS1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000015090; Expressed in thymus and 19 other tissues.
DR Genevisible; Q68FS1; RN.
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; ISO:RGD.
DR GO; GO:0031616; C:spindle pole centrosome; ISO:RGD.
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 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; ATP-binding; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..271
FT /note="Cytosolic Fe-S cluster assembly factor NUBP2"
FT /id="PRO_0000288717"
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; 28926 MW; 1D33E2A6EDA061DF CRC64;
MEAAAEPGNL AGVRHIILVL SGKGGVGKST ISTELALALR HQGKKVGILD VDLCGPSIPH
MLHAQGKAVH QCDSGWVPVF VDQEQSISLM SVGFLLENPD EAVVWRGPKK HALIKQFVSD
VAWGELDYLV VDTPPGTSDE HMATVEALRP YKPLGALVVT TPQAVSIGDV RRELTFCKKT
GLQVIGVIEN MSGFACPHCA ECTNVFSSGG GEELARLAGV PFLGSVPLDP QLTRSLEEGR
DFIQEFPKST AYSALTSIAH KVLHQMPALC S
