ID   NACA_CAEEL              Reviewed;         195 AA.
AC   Q86S66; Q9N2Z8;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE            Short=NAC-alpha;
DE   AltName: Full=Alpha-NAC;
DE   AltName: Full=Inhibitor of cell death 2 {ECO:0000312|WormBase:Y65B4BR.5};
GN   Name=icd-2 {ECO:0000303|PubMed:22957041, ECO:0000312|WormBase:Y65B4BR.5};
GN   ORFNames=Y65B4BR.5 {ECO:0000312|WormBase:Y65B4BR.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22957041; DOI=10.1371/journal.pone.0044038;
RA   Arsenovic P.T., Maldonado A.T., Colleluori V.D., Bloss T.A.;
RT   "Depletion of the C. elegans NAC engages the unfolded protein response,
RT   resulting in increased chaperone expression and apoptosis.";
RL   PLoS ONE 7:e44038-e44038(2012).
CC   -!- FUNCTION: May prevent inappropriate targeting of non-secretory
CC       polypeptides to the endoplasmic reticulum (ER) (By similarity). Plays a
CC       role in the response to heat stress (PubMed:22957041).
CC       {ECO:0000250|UniProtKB:Q13765, ECO:0000269|PubMed:22957041}.
CC   -!- SUBUNIT: May be part of the nascent polypeptide-associated complex
CC       (NAC), which is a heterodimer of icd-2 and icd-1 (via NAC-A/B domains).
CC       {ECO:0000250|UniProtKB:Q13765}.
CC   -!- INTERACTION:
CC       Q86S66; H2KZY3: CELE_F49E8.7; NbExp=5; IntAct=EBI-326549, EBI-326535;
CC       Q86S66; Q18885: icd-1; NbExp=6; IntAct=EBI-326549, EBI-326530;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13765}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in larvae results in
CC       increased survival and mobility in response to a constant temperature
CC       of 36 degrees Celsius, when compared to wild-type.
CC       {ECO:0000269|PubMed:22957041}.
CC   -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000305}.
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DR   EMBL; BX284601; CCD71933.1; -; Genomic_DNA.
DR   RefSeq; NP_490749.1; NM_058348.5.
DR   AlphaFoldDB; Q86S66; -.
DR   SMR; Q86S66; -.
DR   BioGRID; 37146; 21.
DR   ComplexPortal; CPX-5744; Nascent polypeptide-associated complex.
DR   DIP; DIP-25064N; -.
DR   IntAct; Q86S66; 6.
DR   STRING; 6239.Y65B4BR.5b; -.
DR   iPTMnet; Q86S66; -.
DR   EPD; Q86S66; -.
DR   PaxDb; Q86S66; -.
DR   PeptideAtlas; Q86S66; -.
DR   EnsemblMetazoa; Y65B4BR.5.1; Y65B4BR.5.1; WBGene00022042.
DR   GeneID; 171646; -.
DR   KEGG; cel:CELE_Y65B4BR.5; -.
DR   UCSC; Y65B4BR.5a.1; c. elegans.
DR   CTD; 171646; -.
DR   WormBase; Y65B4BR.5; CE22740; WBGene00022042; icd-2.
DR   eggNOG; KOG2239; Eukaryota.
DR   GeneTree; ENSGT00440000033468; -.
DR   InParanoid; Q86S66; -.
DR   OrthoDB; 1331328at2759; -.
DR   PhylomeDB; Q86S66; -.
DR   PRO; PR:Q86S66; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00022042; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; IC:ComplexPortal.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:1905551; P:negative regulation of protein localization to endoplasmic reticulum; IC:ComplexPortal.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR   GO; GO:1900034; P:regulation of cellular response to heat; IC:ComplexPortal.
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   1: Evidence at protein level;
KW   Cytoplasm; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..195
FT                   /note="Nascent polypeptide-associated complex subunit
FT                   alpha"
FT                   /id="PRO_0000135585"
FT   DOMAIN          56..121
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   195 AA;  21802 MW;  0158E4BCCC1775B0 CRC64;
     MTGSTETRQK EVKEPQVDVS DDSDNEAVEQ ELTEEQRRVA EAAGLGDHID KQAKQSRSEK
     KARKLFSKLG LKQVTGVSRV CIRKSKNILF VINKPDVFKS PGSDTYIIFG EAKIEDLTQH
     AQMSAIENLK PTREAPQLKT VEEDENEDVE EDSTGIEEKD IELVISQANT TRNKAIRALK
     EADNDIVNAI MSLTM