ID   NACB_SCHPO              Reviewed;         151 AA.
AC   Q92371; O36026;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Nascent polypeptide-associated complex subunit beta;
DE            Short=NAC-beta;
DE   AltName: Full=Beta-NAC;
GN   Name=btf3; Synonyms=egd1; ORFNames=SPAC4F10.14c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8809106; DOI=10.1016/0167-4781(96)00114-5;
RA   Potashkin J., Wentz-Hunter K., Callaci J.;
RT   "BTF3 is evolutionarily conserved in fission yeast.";
RL   Biochim. Biophys. Acta 1308:182-184(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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. EGD1 may act as a transcription factor that
CC       exert a negative effect on the expression of several genes that are
CC       transcribed by RNA polymerase II. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC       consisting of ucp15 and btf3. NAC associates with ribosomes via btf3
CC       (By 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-beta family. {ECO:0000305}.
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DR   EMBL; U49084; AAB40599.1; -; mRNA.
DR   EMBL; CU329670; CAB11717.1; -; Genomic_DNA.
DR   PIR; S71926; S71926.
DR   PIR; T38818; T38818.
DR   RefSeq; NP_594757.1; NM_001020184.2.
DR   AlphaFoldDB; Q92371; -.
DR   SMR; Q92371; -.
DR   BioGRID; 279933; 33.
DR   STRING; 4896.SPAC4F10.14c.1; -.
DR   iPTMnet; Q92371; -.
DR   MaxQB; Q92371; -.
DR   PaxDb; Q92371; -.
DR   PRIDE; Q92371; -.
DR   EnsemblFungi; SPAC4F10.14c.1; SPAC4F10.14c.1:pep; SPAC4F10.14c.
DR   GeneID; 2543515; -.
DR   KEGG; spo:SPAC4F10.14c; -.
DR   PomBase; SPAC4F10.14c; btf3.
DR   VEuPathDB; FungiDB:SPAC4F10.14c; -.
DR   eggNOG; KOG2240; Eukaryota.
DR   HOGENOM; CLU_098726_3_0_1; -.
DR   InParanoid; Q92371; -.
DR   OMA; KVHKNSM; -.
DR   PhylomeDB; Q92371; -.
DR   PRO; PR:Q92371; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; IPI:PomBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042788; C:polysomal ribosome; IPI:PomBase.
DR   GO; GO:0051083; P:'de novo' cotranslational protein folding; ISO:PomBase.
DR   GO; GO:0006613; P:cotranslational protein targeting to membrane; ISO:PomBase.
DR   Gene3D; 2.20.70.30; -; 1.
DR   InterPro; IPR039370; BTF3.
DR   InterPro; IPR038187; NAC_A/B_dom_sf.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR   PANTHER; PTHR10351; PTHR10351; 1.
DR   Pfam; PF01849; NAC; 1.
DR   SMART; SM01407; NAC; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..151
FT                   /note="Nascent polypeptide-associated complex subunit beta"
FT                   /id="PRO_0000213553"
FT   DOMAIN          35..100
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        103
FT                   /note="I -> N (in Ref. 1; AAB40599)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  16202 MW;  E1250863AB09FDCC CRC64;
     MDPSKLAKLQ AGARIGGKGT PRRKVKKPSK SAMSAADDKK VQGALKKLNM QNLAGIQEVN
     MFKEDGGVIN FRAPTVHSSL PNETTAIYGK AEEKTLSEIL PGILNNLGPE SLTALRQMAE
     QLKVSEGEKG ADAQADDGEI PDLVEKFDEQ D