IND1_YARLI
ID IND1_YARLI Reviewed; 312 AA.
AC Q6CE48;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Iron-sulfur protein IND1;
DE AltName: Full=Iron-sulfur protein required for NADH dehydrogenase 1;
DE Flags: Precursor;
GN Name=IND1; OrderedLocusNames=YALI0B18590g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP PROTEIN SEQUENCE OF 35-38, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-242; CYS-245 AND CYS-279.
RX PubMed=18497740; DOI=10.1038/emboj.2008.98;
RA Bych K., Kerscher S., Netz D.J.A., Pierik A.J., Zwicker K., Huynen M.A.,
RA Lill R., Brandt U., Balk J.;
RT "The iron-sulphur protein Ind1 is required for effective complex I
RT assembly.";
RL EMBO J. 27:1736-1746(2008).
CC -!- FUNCTION: Required for the effective assembly of the mitochondrial
CC membrane respiratory chain NADH dehydrogenase (Complex I). Probably
CC facilitates the assembly of Fe-S cofactors and subunits of complex I.
CC {ECO:0000269|PubMed:18497740}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:18497740};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:18497740};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18497740}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18497740}; Matrix side
CC {ECO:0000269|PubMed:18497740}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC {ECO:0000305}.
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DR EMBL; CR382128; CAG83317.1; -; Genomic_DNA.
DR RefSeq; XP_501064.1; XM_501064.1.
DR AlphaFoldDB; Q6CE48; -.
DR SMR; Q6CE48; -.
DR STRING; 4952.CAG83317; -.
DR EnsemblFungi; CAG83317; CAG83317; YALI0_B18590g.
DR GeneID; 2907193; -.
DR KEGG; yli:YALI0B18590g; -.
DR VEuPathDB; FungiDB:YALI0_B18590g; -.
DR HOGENOM; CLU_024839_0_2_1; -.
DR InParanoid; Q6CE48; -.
DR OMA; NMAYFTP; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR044304; NUBPL-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR42961; PTHR42961; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:18497740"
FT CHAIN 35..312
FT /note="Iron-sulfur protein IND1"
FT /id="PRO_0000352527"
FT REGION 32..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 242
FT /note="C->A,E,S: Reduces the amount of fully assembled
FT complex I."
FT /evidence="ECO:0000269|PubMed:18497740"
FT MUTAGEN 245
FT /note="C->A,E,S: Reduces the amount of fully assembled
FT complex I."
FT /evidence="ECO:0000269|PubMed:18497740"
FT MUTAGEN 279
FT /note="C->A,S: No effect."
FT /evidence="ECO:0000269|PubMed:18497740"
FT MUTAGEN 279
FT /note="C->E: Abolishes most of complex I activity."
FT /evidence="ECO:0000269|PubMed:18497740"
SQ SEQUENCE 312 AA; 33167 MW; 25F5F96432C8A327 CRC64;
MRGFRLIAPI QRSIAIISRL QPITANFHSS PALRSHENPL GIPKSPASAP RIPRKTTRRP
EPIAGVKKTI VVSSAKGGVG KSTVSVNTAL SLAKRGLRVG LLDVDIFGPS IPTMFGLSGE
PRMTHEGKLI PMSKFGIQVM SMGFLVDPNK AVAWRGLLVQ KALEQLLQDV DWGTLDVLVM
DLPPGTGDVQ LTIAQTVKID GAIIVSTPQD VALVDVVRGL DLFEKTYTKV LGLVQNMSVF
VCPNCNHETH IFGVDGAVSK AKSRGLGVLG NVPLDPQICS QSDKGVPVAV SGGVQAKYYD
KIAEGVAEQL GV
