ID   CAHS4_HYPDU             Reviewed;         224 AA.
AC   P0CU44;
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 77611 {ECO:0000303|PubMed:28306513};
DE            Short=CAHS 77611 {ECO:0000303|PubMed:28306513};
DE   AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS 77611 {ECO:0000303|PubMed:28306513};
DE            Short=TDP CAHS 77611 {ECO:0000303|PubMed:28306513};
GN   Name=CAHS 77611 {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, 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   [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   -!- 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 (By similarity). {ECO:0000250|UniProtKB:J7M799}.
CC   -!- DISRUPTION PHENOTYPE: Results in a significant decrease in survival
CC       after desiccation but does not affect survival under frozen conditions
CC       (PubMed:28306513). {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0CU44; -.
DR   SMR; P0CU44; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   DisProt; DP01379; -.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Repeat; Stress response.
FT   CHAIN           1..224
FT                   /note="Cytosolic-abundant heat soluble protein 77611"
FT                   /id="PRO_0000440193"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..140
FT                   /note="CAHS motif 1"
FT                   /evidence="ECO:0000250|UniProtKB:J7M799"
FT   REGION          159..177
FT                   /note="CAHS motif 2"
FT                   /evidence="ECO:0000250|UniProtKB:J7M799"
FT   REGION          200..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          80..191
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   224 AA;  25905 MW;  F4BA13EEFD1A87D7 CRC64;
     MSNYQQESSY QYSDRSNNGQ QQEQQEKKEV EHSSYTHTDV KVNMPNLIAP FISSSAGLAQ
     ELVGEGFQAS VSRITGASGE LTVIDTEAET EEARRDLEAK AREQELLSRQ FEKELERKTE
     AYRKQQEVET EKIRKELEKQ HLRDVEFRKE LMEQTIENQK RQIDLEARYA KKELERERNK
     VKRVLERSKF HTDIQVNMEA AAGSTHSGSS SVAVSESEKF QTNN