ID   SAHS4_HYPDU             Reviewed;         174 AA.
AC   P0CU42;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Secretory-abundant heat soluble protein 68234 {ECO:0000303|PubMed:28306513};
DE            Short=SAHS 68234 {ECO:0000303|PubMed:28306513};
DE   AltName: Full=Tardigrade-specific intrinsically disordered protein SAHS 68234 {ECO:0000303|PubMed:28306513};
DE            Short=TDP SAHS 68234 {ECO:0000303|PubMed:28306513};
DE   Flags: Precursor;
GN   Name=SAHS 68234 {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).
CC   -!- FUNCTION: Secreted heat soluble protein acting as a molecular shield in
CC       water-deficient condition (PubMed:28306513). Tardigrade-specific
CC       intrinsically disordered proteins (TDPs) are essential for desiccation
CC       tolerance by forming non-crystalline amorphous solids upon desiccation,
CC       and this vitrified state mirrors their protective capabilities
CC       (PubMed:28306513). {ECO:0000269|PubMed:28306513}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28306513}.
CC   -!- INDUCTION: Expression is highly induced during desiccation
CC       (PubMed:28306513). {ECO:0000269|PubMed:28306513}.
CC   -!- DOMAIN: SAHS-c1, SAHS-c2 and SAHS-c3 are 3 highly conserved regions
CC       within the SAHS protein family (By similarity).
CC       {ECO:0000250|UniProtKB:J7MFT5}.
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 Secretory-abundant heat soluble protein
CC       (SAHS) family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CU42; -.
DR   SMR; P0CU42; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; SSF50814; 1.
PE   2: Evidence at transcript level;
KW   Secreted; Signal; Stress response.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..174
FT                   /note="Secretory-abundant heat soluble protein 68234"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000440186"
FT   REGION          26..57
FT                   /note="SAHS-c1"
FT                   /evidence="ECO:0000250|UniProtKB:J7MFT5"
FT   REGION          72..100
FT                   /note="SAHS-c2"
FT                   /evidence="ECO:0000250|UniProtKB:J7MFT5"
FT   REGION          113..162
FT                   /note="SAHS-c3"
FT                   /evidence="ECO:0000250|UniProtKB:J7MFT5"
SQ   SEQUENCE   174 AA;  19369 MW;  1FBE2AE16D0141B3 CRC64;
     MARFLVALAL FGVVAMTAAT GDAPKEWSGK PWLGKFVAEV TDKSENWEAF VDALGLPEQF
     GRAPVKTIQK IYKQGDHYHH IFALPDKNFE KDIEFTLGQE VEIKQGEHIA KTKYSEDGEK
     LVADVSIPTK GKTIRSEYEV QGDQLIKTYK TGDIVAKKWF KKVANPTEAP AQAA