ID   CAHS6_HYPDU             Reviewed;         227 AA.
AC   P0CU48;
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 94205 {ECO:0000303|PubMed:28306513};
DE            Short=CAHS 94205 {ECO:0000303|PubMed:28306513};
DE   AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS 94205 {ECO:0000303|PubMed:28306513};
DE            Short=TDP CAHS 94205 {ECO:0000303|PubMed:28306513};
GN   Name=CAHS 94205 {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; P0CU48; -.
DR   SMR; P0CU48; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   DisProt; DP01385; -.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Repeat; Stress response.
FT   CHAIN           1..227
FT                   /note="Cytosolic-abundant heat soluble protein 94205"
FT                   /id="PRO_0000440195"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..144
FT                   /note="CAHS motif 1"
FT                   /evidence="ECO:0000250|UniProtKB:J7M799"
FT   REGION          163..181
FT                   /note="CAHS motif 2"
FT                   /evidence="ECO:0000250|UniProtKB:J7M799"
FT   REGION          205..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          91..191
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   227 AA;  25485 MW;  DC1B10843266288B CRC64;
     MSGRNVESHM ERNEKVVVNN SGHADVKKQQ QQVEHTEFTH TEVKAPLIHP APPIISTGAA
     GLAEEIVGQG FTASAARISG GTAEVHLQPS AAMTEEARRD QERYRQEQES IAKQQEREME
     KKTEAYRKTA EAEAEKIRKE LEKQHARDVE FRKDLIESTI DRQKREVDLE AKMAKRELDR
     EGQLAKEALE RSRLATNVEV NFDSAAGHTV SGGTTVSTSD KMEIKRN