ID   NACA_CANAL              Reviewed;         178 AA.
AC   Q5ANP2; A0A1D8PJU3;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE            Short=NAC-alpha;
DE   AltName: Full=Alpha-NAC;
GN   Name=EGD2; OrderedLocusNames=CAALFM_C304140CA;
GN   ORFNames=CaO19.13280, CaO19.5858;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: Component of the nascent polypeptide-associated complex
CC       (NAC), a dynamic component of the ribosomal exit tunnel, protecting the
CC       emerging polypeptides from interaction with other cytoplasmic proteins
CC       to ensure appropriate nascent protein targeting. The NAC complex also
CC       promotes mitochondrial protein import by enhancing productive ribosome
CC       interactions with the outer mitochondrial membrane and blocks the
CC       inappropriate interaction of ribosomes translating non-secretory
CC       nascent 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 EGD1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Predominantly cytoplasmic, may also transiently localize to the
CC       nucleus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000305}.
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DR   EMBL; CP017625; AOW28435.1; -; Genomic_DNA.
DR   RefSeq; XP_723074.1; XM_717981.1.
DR   AlphaFoldDB; Q5ANP2; -.
DR   STRING; 237561.Q5ANP2; -.
DR   PRIDE; Q5ANP2; -.
DR   GeneID; 3635284; -.
DR   KEGG; cal:CAALFM_C304140CA; -.
DR   CGD; CAL0000185584; EGD2.
DR   VEuPathDB; FungiDB:C3_04140C_A; -.
DR   eggNOG; KOG2239; Eukaryota.
DR   HOGENOM; CLU_057806_2_1_1; -.
DR   InParanoid; Q5ANP2; -.
DR   OMA; LVMCQAN; -.
DR   OrthoDB; 1331328at2759; -.
DR   PRO; PR:Q5ANP2; -.
DR   Proteomes; UP000000559; Chromosome 3.
DR   GO; GO:0009986; C:cell surface; IDA:CGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR   Gene3D; 2.20.70.30; -; 1.
DR   InterPro; IPR016641; EGD2/NACA.
DR   InterPro; IPR044034; NAC-like_UBA.
DR   InterPro; IPR038187; NAC_A/B_dom_sf.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR   PANTHER; PTHR21713; PTHR21713; 1.
DR   Pfam; PF19026; HYPK_UBA; 1.
DR   Pfam; PF01849; NAC; 1.
DR   PIRSF; PIRSF015901; NAC_alpha; 1.
DR   SMART; SM01407; NAC; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..178
FT                   /note="Nascent polypeptide-associated complex subunit
FT                   alpha"
FT                   /id="PRO_0000273483"
FT   DOMAIN          16..80
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   DOMAIN          140..178
FT                   /note="UBA"
FT   REGION          82..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..139
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   178 AA;  19510 MW;  419313E4F3226AE5 CRC64;
     MSIEEIPQGA DVNVIPKNEK KARELIKKLN LKQIKGISRV TFKQRGNLIY AIDSPDVYRS
     AAGTYVVFGE AKVDDMNQRI AEAQAQQAQQ EALQKAAADA GKTEDKSPEA ITADLEKASL
     GDKKAEDEEE DEGEIDETGL DPKDIEIVVE QTQVSRAKAV KALRNHDGDM VNAIMDLS