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NAR1_YEAST
ID   NAR1_YEAST              Reviewed;         491 AA.
AC   P23503; D6W0V3;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor NAR1;
DE   AltName: Full=Nuclear architecture-related protein 1;
GN   Name=NAR1; OrderedLocusNames=YNL240C; ORFNames=N1114;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8896273;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA   Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT   "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT   reading frames including a novel gene encoding a globin-like domain.";
RL   Yeast 12:1071-1076(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-491.
RX   PubMed=2269430; DOI=10.1016/0378-1119(90)90248-p;
RA   Nogae I., Johnston M.;
RT   "Isolation and characterization of the ZWF1 gene of Saccharomyces
RT   cerevisiae, encoding glucose-6-phosphate dehydrogenase.";
RL   Gene 96:161-169(1990).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15103330; DOI=10.1038/sj.emboj.7600216;
RA   Balk J., Pierik A.J., Aguilar Netz D.J., Muehlenhoff U., Lill R.;
RT   "The hydrogenase-like Nar1p is essential for maturation of cytosolic and
RT   nuclear iron-sulphur proteins.";
RL   EMBO J. 23:2105-2115(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=15667273; DOI=10.1042/bst0330086;
RA   Balk J., Pierik A.J., Aguilar Netz D.J., Muehlenhoff U., Lill R.;
RT   "Nar1p, a conserved eukaryotic protein with similarity to Fe-only
RT   hydrogenases, functions in cytosolic iron-sulphur protein biogenesis.";
RL   Biochem. Soc. Trans. 33:86-89(2005).
RN   [8]
RP   INTERACTION WITH CIA1.
RX   PubMed=16314508; DOI=10.1128/mcb.25.24.10833-10841.2005;
RA   Balk J., Aguilar Netz D.J.A., Tepper K., Pierik A.J., Lill R.;
RT   "The essential WD40 protein Cia1 is involved in a late step of cytosolic
RT   and nuclear iron-sulfur protein assembly.";
RL   Mol. Cell. Biol. 25:10833-10841(2005).
RN   [9]
RP   FUNCTION, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS, AND MUTAGENESIS OF
RP   CYS-20; CYS-59; CYS-62; CYS-65; CYS-177; CYS-231; CYS-412 AND CYS-416.
RX   PubMed=19385603; DOI=10.1021/bi900312x;
RA   Urzica E., Pierik A.J., Muehlenhoff U., Lill R.;
RT   "Crucial role of conserved cysteine residues in the assembly of two iron-
RT   sulfur clusters on the CIA protein Nar1.";
RL   Biochemistry 48:4946-4958(2009).
CC   -!- FUNCTION: Essential component of a cytosolic Fe/S protein assembly
CC       machinery. Required for maturation of extramitochondrial Fe/S proteins.
CC       May play a role in the transfer of pre-assembled Fe/S clusters to
CC       target apoproteins. {ECO:0000269|PubMed:15103330,
CC       ECO:0000269|PubMed:15667273, ECO:0000269|PubMed:19385603}.
CC   -!- SUBUNIT: Interacts with CIA1. {ECO:0000269|PubMed:16314508}.
CC   -!- INTERACTION:
CC       P23503; Q05583: CIA1; NbExp=2; IntAct=EBI-11864, EBI-32145;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15103330}. Nucleus
CC       {ECO:0000269|PubMed:15103330}. Note=Predominantly cytoplasmic.
CC   -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA34618.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z69381; CAA93358.1; -; Genomic_DNA.
DR   EMBL; Z71516; CAA96145.1; -; Genomic_DNA.
DR   EMBL; AY692992; AAT93011.1; -; Genomic_DNA.
DR   EMBL; M34709; AAA34618.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006947; DAA10319.1; -; Genomic_DNA.
DR   PIR; S63206; S63206.
DR   RefSeq; NP_014159.1; NM_001183078.1.
DR   AlphaFoldDB; P23503; -.
DR   SMR; P23503; -.
DR   BioGRID; 35599; 305.
DR   IntAct; P23503; 5.
DR   STRING; 4932.YNL240C; -.
DR   iPTMnet; P23503; -.
DR   MaxQB; P23503; -.
DR   PaxDb; P23503; -.
DR   PRIDE; P23503; -.
DR   EnsemblFungi; YNL240C_mRNA; YNL240C; YNL240C.
DR   GeneID; 855481; -.
DR   KEGG; sce:YNL240C; -.
DR   SGD; S000005184; NAR1.
DR   VEuPathDB; FungiDB:YNL240C; -.
DR   eggNOG; KOG2439; Eukaryota.
DR   GeneTree; ENSGT00940000153514; -.
DR   HOGENOM; CLU_018240_0_1_1; -.
DR   InParanoid; P23503; -.
DR   OMA; PHEQRAW; -.
DR   BioCyc; YEAST:G3O-33238-MON; -.
DR   PRO; PR:P23503; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P23503; protein.
DR   GO; GO:0097361; C:CIA complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; ISS:SGD.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR   InterPro; IPR009016; Fe_hydrogenase.
DR   InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR   Pfam; PF02906; Fe_hyd_lg_C; 1.
DR   SUPFAM; SSF53920; SSF53920; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..491
FT                   /note="Cytosolic Fe-S cluster assembly factor NAR1"
FT                   /id="PRO_0000096718"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         59
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         62
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         65
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         177
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         231
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         412
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         416
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         20
FT                   /note="C->A: Weakly reduced iron content and impaired
FT                   maturation of cytosolic Fe/S proteins. Strongly impaired
FT                   maturation of cytosolic Fe/S proteins; when associated with
FT                   A-62 or A-65."
FT                   /evidence="ECO:0000269|PubMed:19385603"
FT   MUTAGEN         59
FT                   /note="C->A: Reduced iron content and strongly impaired
FT                   maturation of cytosolic Fe/S proteins."
FT                   /evidence="ECO:0000269|PubMed:19385603"
FT   MUTAGEN         62
FT                   /note="C->A: Reduced iron content and strongly impaired
FT                   maturation of cytosolic Fe/S proteins."
FT                   /evidence="ECO:0000269|PubMed:19385603"
FT   MUTAGEN         65
FT                   /note="C->A: Reduced iron content and strongly impaired
FT                   maturation of cytosolic Fe/S proteins."
FT                   /evidence="ECO:0000269|PubMed:19385603"
FT   MUTAGEN         177
FT                   /note="C->A: Impaired maturation of cytosolic Fe/S
FT                   proteins. Reduced iron content and strongly impaired
FT                   maturation of cytosolic Fe/S proteins; when associated with
FT                   A-416."
FT                   /evidence="ECO:0000269|PubMed:19385603"
FT   MUTAGEN         177
FT                   /note="C->S: Reduced iron content and strongly impaired
FT                   maturation of cytosolic Fe/S proteins; when associated with
FT                   S-412."
FT                   /evidence="ECO:0000269|PubMed:19385603"
FT   MUTAGEN         231
FT                   /note="C->A: Impaired maturation of cytosolic Fe/S
FT                   proteins. Strongly impaired maturation of cytosolic Fe/S
FT                   proteins; when associated with A-416."
FT                   /evidence="ECO:0000269|PubMed:19385603"
FT   MUTAGEN         412
FT                   /note="C->S: Reduced iron content and strongly impaired
FT                   maturation of cytosolic Fe/S proteins; when associated with
FT                   S-177."
FT                   /evidence="ECO:0000269|PubMed:19385603"
FT   MUTAGEN         416
FT                   /note="C->A: Reduced iron content and strongly impaired
FT                   maturation of cytosolic Fe/S proteins; when associated with
FT                   A-177 or A-231."
FT                   /evidence="ECO:0000269|PubMed:19385603"
SQ   SEQUENCE   491 AA;  54151 MW;  FFEB2A07A881BBC1 CRC64;
     MSALLSESDL NDFISPALAC VKPTQVSGGK KDNVNMNGEY EVSTEPDQLE KVSITLSDCL
     ACSGCITSSE EILLSSQSHS VFLKNWGKLS QQQDKFLVVS VSPQCRLSLA QYYGLTLEAA
     DLCLMNFFQK HFQCKYMVGT EMGRIISISK TVEKIIAHKK QKENTGADRK PLLSAVCPGF
     LIYTEKTKPQ LVPMLLNVKS PQQITGSLIR ATFESLAIAR ESFYHLSLMP CFDKKLEASR
     PESLDDGIDC VITPREIVTM LQELNLDFKS FLTEDTSLYG RLSPPGWDPR VHWASNLGGT
     CGGYAYQYVT AVQRLHPGSQ MIVLEGRNSD IVEYRLLHDD RIIAAASELS GFRNIQNLVR
     KLTSGSGSER KRNITALRKR RTGPKANSRE MAAATAATAD PYHSDYIEVN ACPGACMNGG
     GLLNGEQNSL KRKQLVQTLN KRHGEELAMV DPLTLGPKLE EAAARPLSLE YVFAPVKQAV
     EKDLVSVGST W
 
 
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