ID   SAHS3_HYPDU             Reviewed;         172 AA.
AC   P0CU41;
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 64681 {ECO:0000303|PubMed:28306513};
DE            Short=SAHS 63681 {ECO:0000303|PubMed:28306513};
DE   AltName: Full=Secretory-abundant heat soluble protein c {ECO:0000303|PubMed:22937162};
DE            Short=SAHS-c {ECO:0000303|PubMed:22937162};
DE   AltName: Full=Tardigrade-specific intrinsically disordered protein SAHS 64681 {ECO:0000303|PubMed:28306513};
DE            Short=TDP SAHS 64681 {ECO:0000303|PubMed:28306513};
DE   Flags: Precursor;
GN   Name=SAHS 64681 {ECO:0000303|PubMed:28306513};
GN   Synonyms=SAHS-c {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; P0CU41; -.
DR   SMR; P0CU41; -.
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   Glycoprotein; Secreted; Signal; Stress response.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..172
FT                   /note="Secretory-abundant heat soluble protein 64681"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000440185"
FT   REGION          30..59
FT                   /note="SAHS-c1"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          74..102
FT                   /note="SAHS-c2"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          115..164
FT                   /note="SAHS-c3"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   172 AA;  19346 MW;  C8F0B6A5A20E08EE CRC64;
     MSRTIVALIL LGLAALAAAD HHEGHGAEKE WAGKAWLGKW VSTDRSENWD AFVEALGLPL
     AAYGGNHKTV HKLWKEGDHY HHQIIIADKS YKQDIQFKLG EEGRTAHNGT EVTFKYTEVG
     DNLQNEVKIP SKNKTISDSY VVKGDELEKT YKINDVVAKR WYKKHAHEPS TA