ID   CAHS2_HYPDU             Reviewed;         237 AA.
AC   P0CU46;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Cytosolic-abundant heat soluble protein 86272 {ECO:0000303|PubMed:28306513};
DE            Short=CAHS 86272 {ECO:0000303|PubMed:28306513};
DE   AltName: Full=Cytosolic-abundant heat soluble protein b {ECO:0000303|PubMed:22937162};
DE            Short=SAHS-b {ECO:0000303|PubMed:22937162};
DE   AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS 86272 {ECO:0000303|PubMed:28306513};
DE            Short=TDP CAHS 86272 {ECO:0000303|PubMed:28306513};
GN   Name=CAHS 86272 {ECO:0000303|PubMed:28306513};
GN   Synonyms=CAHS-b {ECO:0000303|PubMed:22937162};
OS   Hypsibius dujardini (Water bear) (Macrobiotus dujardini).
OC   Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC   Hypsibioidea; Hypsibiidae; Hypsibius.
OX   NCBI_TaxID=232323;
RN   [1]
RP   DOMAIN.
RX   PubMed=22937162; DOI=10.1371/journal.pone.0044209;
RA   Yamaguchi A., Tanaka S., Yamaguchi S., Kuwahara H., Takamura C.,
RA   Imajoh-Ohmi S., Horikawa D.D., Toyoda A., Katayama T., Arakawa K.,
RA   Fujiyama A., Kubo T., Kunieda T.;
RT   "Two novel heat-soluble protein families abundantly expressed in an
RT   anhydrobiotic tardigrade.";
RL   PLoS ONE 7:E44209-E44209(2012).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28306513; DOI=10.1016/j.molcel.2017.02.018;
RA   Boothby T.C., Tapia H., Brozena A.H., Piszkiewicz S., Smith A.E.,
RA   Giovannini I., Rebecchi L., Pielak G.J., Koshland D., Goldstein B.;
RT   "Tardigrades use intrinsically disordered proteins to survive
RT   desiccation.";
RL   Mol. Cell 65:975-984(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=33545053; DOI=10.1016/j.molcel.2020.12.007;
RA   Arakawa K., Numata K.;
RT   "Reconsidering the 'glass transition' hypothesis of intrinsically
RT   unstructured CAHS proteins in desiccation tolerance of tardigrades.";
RL   Mol. Cell 81:409-410(2021).
CC   -!- FUNCTION: CAHS proteins are cytosolic heat soluble proteins that seem
CC       to contribute to the anhydrobiosis in tardigrades, but their specific
CC       mechanisms are yet to be identified (PubMed:28306513, PubMed:33545053).
CC       It is possible that protection during anhydrobiosis might occur via the
CC       stabilization of vitrifying small molecules such as sugars, but not via
CC       the direct glass transition of CAHS proteins themselves (Probable).
CC       {ECO:0000269|PubMed:28306513, ECO:0000269|PubMed:33545053,
CC       ECO:0000305|PubMed:33545053}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:28306513}.
CC   -!- INDUCTION: Expression is highly induced during desiccation
CC       (PubMed:28306513). {ECO:0000269|PubMed:28306513}.
CC   -!- DOMAIN: CAHS proteins contain 2 repeats of 19-mer peptides designated
CC       as CAHS-motifs that comprise each two octapeptides connected by a
CC       tripeptide (PubMed:22937162). {ECO:0000305|PubMed:22937162}.
CC   -!- DISRUPTION PHENOTYPE: Affects slightly survival under dry conditions
CC       but does not affect survival under frozen conditions (PubMed:28306513).
CC       {ECO:0000269|PubMed:28306513}.
CC   -!- MISCELLANEOUS: Trehalose, a disaccharide essential for several
CC       organisms to survive drying, is detected at low levels or not at all in
CC       some tardigrade species, indicating that tardigrades possess
CC       potentially novel mechanisms for surviving desiccation involving
CC       tardigrade-specific intrinsically disordered proteins (TDPs)
CC       (PubMed:28306513). {ECO:0000269|PubMed:28306513}.
CC   -!- SIMILARITY: Belongs to the Cytosolic-abundant heat soluble protein
CC       (CAHS) family. {ECO:0000305}.
CC   -!- CAUTION: It was suggested that CAHS proteins were intrinsically
CC       unstructured and show heat-dependent glass transition, which
CC       contributes to the vitrification of cells, and this further leads to
CC       desiccation tolerance (PubMed:28306513). However, more recent studies
CC       led to the conclusion that there was no evidence supporting glass
CC       transition of CAHS proteins to be contributing to the glass transition
CC       of the whole tardigrade (PubMed:33545053).
CC       {ECO:0000269|PubMed:28306513, ECO:0000269|PubMed:33545053}.
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DR   AlphaFoldDB; P0CU46; -.
DR   SMR; P0CU46; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   DisProt; DP01381; -.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Repeat; Stress response.
FT   CHAIN           1..237
FT                   /note="Cytosolic-abundant heat soluble protein 86272"
FT                   /id="PRO_0000440191"
FT   REGION          96..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..142
FT                   /note="CAHS motif 1"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          161..179
FT                   /note="CAHS motif 2"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          204..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          115..193
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        217..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   237 AA;  26329 MW;  2FA3E24FEA7707A2 CRC64;
     MSQQYEKKVE RTEVVYGGDR RVEGSASASA EKTTNYTHTE IRAPMVNPLP PIISTGAAGL
     AQEIVGEGFT ASATRISGAA ATTQVLESQA SREQAFKDQE KYSREQAAIA RAHDKDLEKK
     TEEYRKTAEA EAEKIRKELE KQHARDVEFR KDLVESAIDR QKREVDLEAK YAKKELEHER
     ELAMNALEQS KMATNVQVQM DTAAGTTVSG GTTVSEHTEV HDGKEKKSLG EKIKSLF