NUBP1_RAT
ID NUBP1_RAT Reviewed; 320 AA.
AC Q5I0L4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
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:0000312|EMBL:AAH88221.1};
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] {ECO:0000312|EMBL:AAH88221.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:AAH88221.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC088221; AAH88221.1; -; mRNA.
DR RefSeq; NP_001009619.1; NM_001009619.1.
DR AlphaFoldDB; Q5I0L4; -.
DR SMR; Q5I0L4; -.
DR STRING; 10116.ENSRNOP00000003479; -.
DR iPTMnet; Q5I0L4; -.
DR PhosphoSitePlus; Q5I0L4; -.
DR jPOST; Q5I0L4; -.
DR PaxDb; Q5I0L4; -.
DR PRIDE; Q5I0L4; -.
DR GeneID; 287042; -.
DR KEGG; rno:287042; -.
DR UCSC; RGD:1310514; rat.
DR CTD; 4682; -.
DR RGD; 1310514; Nubp1.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; Q5I0L4; -.
DR OMA; QHITFKD; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; Q5I0L4; -.
DR TreeFam; TF300755; -.
DR PRO; PR:Q5I0L4; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002574; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5I0L4; 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; ISS:UniProtKB.
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; 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; ISO:RGD.
DR GO; GO:0051642; P:centrosome localization; ISO:RGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; ISO:RGD.
DR GO; GO:0072697; P:protein localization to cell cortex; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03038; NUBP1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..320
FT /note="Cytosolic Fe-S cluster assembly factor NUBP1"
FT /id="PRO_0000306170"
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"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 320 AA; 34045 MW; 3C9981B055278BD7 CRC64;
MEGAPHGCPG ADSAQAGRGA SCQGCPNQKL CASGAGAAPD PAVEEIREKM KTVRHRILVL
SGKGGVGKST FSAHLAHGLA EDGDTQVALL DIDICGPSIP KIMGLEGEQV HQSGSGWSPV
YVEDNLGVMS VGFLLSSPDD AVIWRGPKKN GMIKQFLRDV DWGDVDYLVI DTPPGTSDEH
LSVVQYLAAA HIDGAVILTT PQEVALQDVR KEISFCHKVK LPIIGVVENM SGFICPKCKR
ESQIFPPTTG GAEAMCQALK IPLLGKVPLD PHIGKSCDKG QSFFVEAPDS PATAAYKSII
QRIREFCNSR QSHDENLISP
