ID   CAHS5_HYPDU             Reviewed;         414 AA.
AC   P0CU47;
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 89226 {ECO:0000303|PubMed:28306513};
DE            Short=CAHS 89226 {ECO:0000303|PubMed:28306513};
DE   AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS 89226 {ECO:0000303|PubMed:28306513};
DE            Short=TDP CAHS 89226 {ECO:0000303|PubMed:28306513};
GN   Name=CAHS 89226 {ECO:0000303|PubMed:28306513};
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   FUNCTION.
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   [2]
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   -!- 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 (By similarity). {ECO:0000250|UniProtKB:J7M799}.
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; P0CU47; -.
DR   SMR; P0CU47; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   DisProt; DP01382; -.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Repeat; Stress response.
FT   CHAIN           1..414
FT                   /note="Cytosolic-abundant heat soluble protein 89226"
FT                   /id="PRO_0000440194"
FT   REGION          27..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..323
FT                   /note="CAHS motif 1"
FT                   /evidence="ECO:0000250|UniProtKB:J7M799"
FT   REGION          342..360
FT                   /note="CAHS motif 2"
FT                   /evidence="ECO:0000250|UniProtKB:J7M799"
FT   REGION          388..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          341..376
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        67..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  45529 MW;  E8085D25C99444A2 CRC64;
     MATKESKYER VEKVNVDADG ATLVKNIGED RGKEDPGMNF QDKRPANLVP GAPAGVIPNR
     IESLPTDRAG QRLREHLSES ERLRVSRSST SSKSSSFVEP SLKYRGEIGP IGKNGEFVAS
     SNRQNSSSNV SSSDNSERAS PASRNSNPGM NNGMTTQRTT VITESSVQGL GAQRTVPIQP
     HQQREDHEVI THESHARAPE TTVVTIPTTR FESAQLESRR DGRTYTEDKE LTIPAPVVAP
     QIHAHQQVNM SGGTSATIHA TTDLHLASEA QINDMGPEEY ERYRAKVEAL ARIHEDETSR
     KAAAYRNAVE ADAELIRQTL ERQHMRDIEF RKDLVESSVD RQQQEIRLEA EYAMRALEQE
     RVNARAALDQ AMASTNIDVN IDSAIGTTHS QGRVTTTSES RTSQARGPAT AAVI