NUBP1_BOVIN
ID NUBP1_BOVIN Reviewed; 320 AA.
AC Q24K00;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1 {ECO:0000255|HAMAP-Rule:MF_03038};
DE AltName: Full=Nucleotide-binding protein 1 {ECO:0000255|HAMAP-Rule:MF_03038};
DE Short=NBP 1 {ECO:0000255|HAMAP-Rule:MF_03038};
GN Name=NUBP1 {ECO:0000250|UniProtKB:Q9R060, ECO:0000255|HAMAP-Rule:MF_03038};
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] {ECO:0000312|EMBL:AAI14138.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI14138.1};
RC TISSUE=Heart ventricle {ECO:0000312|EMBL:AAI14138.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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. Implicated in the regulation of
CC centrosome duplication. Negatively regulates cilium formation and
CC structure. {ECO:0000250|UniProtKB:Q9R060, ECO:0000255|HAMAP-
CC Rule:MF_03038}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03038};
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_03038};
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts with
CC KIFC1. Interacts with the BBS/CCT complex subunit CCT1.
CC {ECO:0000250|UniProtKB:Q9R060, ECO:0000255|HAMAP-Rule:MF_03038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038}.
CC Nucleus {ECO:0000250|UniProtKB:Q9R060}. Cell projection
CC {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000250|UniProtKB:Q9R060}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000250|UniProtKB:Q9R060}. Note=Enriched in centrioles
CC of microtubule asters during prophase, prometaphase and telophase
CC stages of mitosis. Localized at centrioles and in the nucleus at
CC interphase. Colocalizes with nubp-2 at prometaphase. Specifically
CC localizes to the axenome of motile cilia as opposed to primary non-
CC motile cilia. Localization is independent of NUBP2 and KIFC1.
CC {ECO:0000250|UniProtKB:Q9R060}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP1/NBP35 subfamily. {ECO:0000255|HAMAP-Rule:MF_03038}.
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DR EMBL; BC114137; AAI14138.1; -; mRNA.
DR RefSeq; NP_001068763.1; NM_001075295.2.
DR AlphaFoldDB; Q24K00; -.
DR SMR; Q24K00; -.
DR STRING; 9913.ENSBTAP00000012576; -.
DR PaxDb; Q24K00; -.
DR PRIDE; Q24K00; -.
DR Ensembl; ENSBTAT00000012576; ENSBTAP00000012576; ENSBTAG00000009560.
DR GeneID; 507007; -.
DR KEGG; bta:507007; -.
DR CTD; 4682; -.
DR VEuPathDB; HostDB:ENSBTAG00000009560; -.
DR VGNC; VGNC:32315; NUBP1.
DR eggNOG; KOG3022; Eukaryota.
DR GeneTree; ENSGT00950000183193; -.
DR InParanoid; Q24K00; -.
DR OMA; QHITFKD; -.
DR OrthoDB; 1166096at2759; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000009560; Expressed in oocyte and 105 other tissues.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; ISS:UniProtKB.
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:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
DR GO; GO:0051642; P:centrosome localization; IEA:Ensembl.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IEA:Ensembl.
DR GO; GO:0072697; P:protein localization to cell cortex; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03038; NUBP1; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028601; NUBP1/Nbp35.
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..320
FT /note="Cytosolic Fe-S cluster assembly factor NUBP1"
FT /id="PRO_0000306169"
FT BINDING 8
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 31
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 235
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 238
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P53384"
SQ SEQUENCE 320 AA; 34182 MW; 975CAA1D50DBEEB3 CRC64;
MEEVPHDCPG ADSAQAGRGA SCQGCPNQRL CASGAGAAAD PAIEEIKEKM KTVKHKILVL
SGKGGVGKST FSAHLAHGLA EDENTQVALL DIDICGPSIP KIMGLEGEQV HQSGSGWSPV
FLEDNLGVMS VGFLLSSPDD AVIWRGPKKN GMIKQFLRDV DWGEVDYLIV DTPPGTSDEH
LSVVQYLTAA HIDGAVIITT PQEVSLQDVR KEISFCHKVK LPIIGVVENM SGFICPKCQK
ESQIFPPTTG GAEAMCQDLK IPLLGKVPLD PRIGKSCDKG QSFLVEAPDS PATVAYRSII
QRIQEFCSQR LPEGENLVGS
