ID   SAHS2_HYPDU             Reviewed;         163 AA.
AC   P0CU40;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Secretory-abundant heat soluble protein 53582 {ECO:0000303|PubMed:28306513};
DE            Short=SAHS 53582 {ECO:0000303|PubMed:28306513};
DE   AltName: Full=Secretory-abundant heat soluble protein b {ECO:0000303|PubMed:22937162};
DE            Short=SAHS-b {ECO:0000303|PubMed:22937162};
DE   AltName: Full=Tardigrade-specific intrinsically disordered protein SAHS 53582 {ECO:0000303|PubMed:28306513};
DE            Short=TDP SAHS 53582 {ECO:0000303|PubMed:28306513};
DE   Flags: Precursor;
GN   Name=SAHS 53582 {ECO:0000303|PubMed:28306513};
GN   Synonyms=SAHS-b {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; P0CU40; -.
DR   SMR; P0CU40; -.
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; IPR031259; ILBP.
DR   PANTHER; PTHR11955; PTHR11955; 1.
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..163
FT                   /note="Secretory-abundant heat soluble protein 53582"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000440184"
FT   REGION          22..51
FT                   /note="SAHS-c1"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          67..95
FT                   /note="SAHS-c2"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          108..157
FT                   /note="SAHS-c3"
FT                   /evidence="ECO:0000305|PubMed:22937162"
SQ   SEQUENCE   163 AA;  18483 MW;  2478A403D835A648 CRC64;
     MARLFVAVAL FGVVAFAAAE KEWTGKTWLG SWASTDRAEN WEAFVDALGL PSDQYPREVQ
     RTIHTIYKQG DKYHHEVSIP SKNFKKAIEY TLGTETDVQH GPHTIKLKYT EDGEKLVADV
     QIPSKNKQIH DIYEVQGDTL TKTYKVGDVV AKRWFTREAN PTA