(data stored in ACNUC8465 zone)

SWISSPROT: NACA_CANGA

ID   NACA_CANGA              Reviewed;         165 AA.
AC   Q6FJD5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 81.
DE   RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE            Short=NAC-alpha;
DE   AltName: Full=Alpha-NAC;
GN   Name=EGD2; OrderedLocusNames=CAGL0M07161g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., 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   -!- FUNCTION: Component of the nascent polypeptide-associated complex
CC       (NAC), a dynamic component of the ribosomal exit tunnel,
CC       protecting the emerging polypeptides from interaction with other
CC       cytoplasmic proteins to ensure appropriate nascent protein
CC       targeting. The NAC complex also promotes mitochondrial protein
CC       import by enhancing productive ribosome interactions with the
CC       outer mitochondrial membrane and blocks the inappropriate
CC       interaction of ribosomes translating non-secretory nascent
CC       polypeptides with translocation sites in the membrane of the
CC       endoplasmic reticulum. EGD2 may also be involved in transcription
CC       regulation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC       consisting of EGD2 and EGD1. NAC associates with ribosomes via
CC       EGD1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Predominantly cytoplasmic, may also
CC       transiently localize to the nucleus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000305}.
DR   EMBL; CR380959; CAG62635.1; -; Genomic_DNA.
DR   RefSeq; XP_449659.1; XM_449659.1.
DR   ProteinModelPortal; Q6FJD5; -.
DR   SMR; Q6FJD5; -.
DR   STRING; 284593.XP_449659.1; -.
DR   EnsemblFungi; CAG62635; CAG62635; CAGL0M07161g.
DR   KEGG; cgr:CAGL0M07161g; -.
DR   CGD; CAL0137119; EGD2.
DR   EuPathDB; FungiDB:CAGL0M07161g; -.
DR   eggNOG; KOG2239; Eukaryota.
DR   eggNOG; COG1308; LUCA.
DR   HOGENOM; HOG000239674; -.
DR   InParanoid; Q6FJD5; -.
DR   KO; K03626; -.
DR   OMA; MANPRVE; -.
DR   OrthoDB; EOG092C57O4; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042788; C:polysomal ribosome; IEA:EnsemblFungi.
DR   GO; GO:0070300; F:phosphatidic acid binding; IEA:EnsemblFungi.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0051083; P:'de novo' cotranslational protein folding; IEA:EnsemblFungi.
DR   GO; GO:0006620; P:posttranslational protein targeting to endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   InterPro; IPR016641; EGD2/NACA.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR   InterPro; IPR009060; UBA-like.
DR   PANTHER; PTHR21713; PTHR21713; 1.
DR   Pfam; PF01849; NAC; 1.
DR   PIRSF; PIRSF015901; NAC_alpha; 1.
DR   SMART; SM01407; NAC; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJD5.
DR   SWISS-2DPAGE; Q6FJD5.
KW   Complete proteome; Cytoplasm; Nucleus; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN         1    165       Nascent polypeptide-associated complex
FT                                subunit alpha.
FT                                /FTId=PRO_0000273484.
FT   DOMAIN       14     78       NAC-A/B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00507}.
FT   DOMAIN      126    165       UBA.
SQ   SEQUENCE   165 AA;  17894 MW;  B757BB9D6E0317EF CRC64;
     MAEIPEGANV TILNRNEKKA RELISKLGLK KVPGIIRVTF RKKDNQIFAI EKPEVFRSVG
     GNYVVFGEAK VDNFTQRLAA AQQQAQSQTA TKTPEDIQAD MQAAAVANEN KTEGDAAEED
     VDAGDLSNDD IDLVVQQTNA TKGQAIKALK EHNGDIVNAI MSLSK
//

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