ID   SAHS1_HYPDU             Reviewed;         168 AA.
AC   P0CU39;
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 33020 {ECO:0000303|PubMed:28306513};
DE            Short=SAHS 33020 {ECO:0000303|PubMed:28306513};
DE   AltName: Full=Secretory-abundant heat soluble protein d {ECO:0000303|PubMed:22937162};
DE            Short=SAHS-d {ECO:0000303|PubMed:22937162};
DE   AltName: Full=Tardigrade-specific intrinsically disordered protein SAHS 33020 {ECO:0000303|PubMed:28306513};
DE            Short=TDP SAHS 33020 {ECO:0000303|PubMed:28306513};
DE   Flags: Precursor;
GN   Name=SAHS 33020 {ECO:0000303|PubMed:28306513};
GN   Synonyms=SAHS-d {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).
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 (PubMed:22937162).
CC       {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 Secretory-abundant heat soluble protein
CC       (SAHS) family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CU39; -.
DR   SMR; P0CU39; -.
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..168
FT                   /note="Secretory-abundant heat soluble protein 33020"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000440183"
FT   REGION          26..57
FT                   /note="SAHS-c1"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          72..100
FT                   /note="SAHS-c2"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          113..162
FT                   /note="SAHS-c3"
FT                   /evidence="ECO:0000305|PubMed:22937162"
SQ   SEQUENCE   168 AA;  18752 MW;  4BD355B6BD24E16D CRC64;
     MARFLVALAL FGVVAMTAAS GDAPKEWSGK PWLGKFVAEV SDKSENWEAF VDALGLPDQY
     PRAQLKTIHS FYKQGEHYHH ILSLPDKNIN KDIEFTLGQE VEIKHGEHSL KIKYFEDGNK
     LVADVSIPAK GKSIHDVYDV QGDQLIKSYK VGDVVAKKWF KKVANPAA