HSP16_SCHPO
ID HSP16_SCHPO Reviewed; 143 AA.
AC O14368;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Heat shock protein 16;
DE AltName: Full=16 kDa heat shock protein;
GN Name=hsp16; ORFNames=SPBC3E7.02c;
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 [GENOMIC DNA].
RC STRAIN=JY746;
RX PubMed=10452954; DOI=10.1016/s0378-1119(99)00237-1;
RA Danjoh I., Fujiyama A.;
RT "Ras-mediated signaling pathway regulates the expression of a low-
RT molecular-weight heat-shock protein in fission yeast.";
RL Gene 236:347-352(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RA Lenaers G., Perret E., Dumont X., Picard A., Caput D.;
RT "hsp16, a major fission yeast heat shock protein homologous to the budding
RT yeast hsp26.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
RN [4]
RP SUBCELLULAR LOCATION, INDUCTION, AND REGULATION.
RX PubMed=11452028; DOI=10.1093/nar/29.14.3030;
RA Taricani L., Feilotter H.E., Weaver C., Young P.G.;
RT "Expression of hsp16 in response to nucleotide depletion is regulated via
RT the spc1 MAPK pathway in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 29:3030-3040(2001).
CC -!- INTERACTION:
CC O14368; O14368: hsp16; NbExp=5; IntAct=EBI-16030516, EBI-16030516;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11452028}. Nucleus
CC {ECO:0000269|PubMed:11452028}.
CC -!- INDUCTION: By heat shock, and under conditions of deoxyribonucleotide
CC depletion and DNA damage. {ECO:0000269|PubMed:11452028}.
CC -!- MISCELLANEOUS: Regulated by the spc1 MAPK signaling pathway.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; AB012619; BAA31521.1; -; Genomic_DNA.
DR EMBL; AJ003817; CAA06031.1; -; mRNA.
DR EMBL; CU329671; CAA19006.1; -; Genomic_DNA.
DR PIR; T40376; T40376.
DR RefSeq; NP_596091.1; NM_001022007.2.
DR PDB; 3W1Z; X-ray; 2.40 A; A/B/C/D=1-143.
DR PDBsum; 3W1Z; -.
DR AlphaFoldDB; O14368; -.
DR SMR; O14368; -.
DR BioGRID; 277493; 24.
DR DIP; DIP-60105N; -.
DR IntAct; O14368; 1.
DR STRING; 4896.SPBC3E7.02c.1; -.
DR iPTMnet; O14368; -.
DR MaxQB; O14368; -.
DR PaxDb; O14368; -.
DR PRIDE; O14368; -.
DR EnsemblFungi; SPBC3E7.02c.1; SPBC3E7.02c.1:pep; SPBC3E7.02c.
DR GeneID; 2540977; -.
DR KEGG; spo:SPBC3E7.02c; -.
DR PomBase; SPBC3E7.02c; hsp16.
DR VEuPathDB; FungiDB:SPBC3E7.02c; -.
DR eggNOG; KOG0710; Eukaryota.
DR HOGENOM; CLU_046737_12_0_1; -.
DR InParanoid; O14368; -.
DR OMA; DESAQWL; -.
DR PhylomeDB; O14368; -.
DR PRO; PR:O14368; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0140453; C:protein aggregate center; IDA:PomBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051082; F:unfolded protein binding; IDA:PomBase.
DR GO; GO:0034605; P:cellular response to heat; IEP:PomBase.
DR GO; GO:0071218; P:cellular response to misfolded protein; IMP:PomBase.
DR GO; GO:0034620; P:cellular response to unfolded protein; IDA:PomBase.
DR GO; GO:0006457; P:protein folding; NAS:PomBase.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..143
FT /note="Heat shock protein 16"
FT /id="PRO_0000126003"
FT DOMAIN 30..143
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3W1Z"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:3W1Z"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:3W1Z"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:3W1Z"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:3W1Z"
SQ SEQUENCE 143 AA; 15968 MW; 321D474116FCE380 CRC64;
MSLQPFFGFP PTVNDLFSDF VSYSPRLNNQ IPGELSPSID VHEGKDTVSV DVELPGVKKE
DVQVHYDSGK LTISGEVVNE RKNESTEGNQ RWSERRFGSF SRTITIPAKI DADRIEANFS
NGLLTVTLPK VEKSQTKKQI AIK
