GenomeNet

Database: UniProt
Entry: Q6C5N9_YARLI
LinkDB: Q6C5N9_YARLI
Original site: Q6C5N9_YARLI 
ID   Q6C5N9_YARLI            Unreviewed;       306 AA.
AC   Q6C5N9;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 117.
DE   SubName: Full=YALI0E16478p {ECO:0000313|EMBL:CAG79616.1};
GN   ORFNames=YALI0_E16478g {ECO:0000313|EMBL:CAG79616.1};
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 {ECO:0000313|EMBL:CAG79616.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG79616.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
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., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382131; CAG79616.1; -; Genomic_DNA.
DR   RefSeq; XP_504023.1; XM_504023.1.
DR   AlphaFoldDB; Q6C5N9; -.
DR   EnsemblFungi; CAG79616; CAG79616; YALI0_E16478g.
DR   GeneID; 2911597; -.
DR   KEGG; yli:YALI0E16478g; -.
DR   VEuPathDB; FungiDB:YALI0_E16478g; -.
DR   HOGENOM; CLU_015166_6_1_1; -.
DR   InParanoid; Q6C5N9; -.
DR   OMA; AFYNGMG; -.
DR   OrthoDB; 4772at2759; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051724; F:NAD transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0035352; P:NAD transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR044712; SLC25A32-like.
DR   PANTHER; PTHR45683:SF2; MITOCHONDRIAL NICOTINAMIDE ADENINE DINUCLEOTIDE TRANSPORTER 1-RELATED; 1.
DR   PANTHER; PTHR45683; MITOCHONDRIAL NICOTINAMIDE ADENINE DINUCLEOTIDE TRANSPORTER 1-RELATED-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        177..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          17..108
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          118..205
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          215..301
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   306 AA;  33769 MW;  9A236CE48D16489D CRC64;
     MSSQNSHNIL HETHLLSDTS IHAIAGALAG TLSGIVVCPL DVIKTRLQAE GALDKQRGSL
     KGGLTRTMDS IVKHDGVRGL YRGVIPIILG YSPTWMIYFA VYEKSKYLLS TVPQLDPYPF
     FSHCLSALGA GAASTTITNP IWVVKTRLMS QGRNTPWHYS GTWDAFKTMY KTDGIKVFYS
     GLGPALLGLS HVAIQFPMYE KLKVMLGVSP DSNKPNPWAV TVASSLSKMI ASAITYPHEI
     VRTRMQIQSK DGQYRGIIAS FKKLYQEEGF RIFYTGFGTN LLRTVPASAI TLLSFEMISS
     RLKQIL
//
DBGET integrated database retrieval system