CAHS1_HYPDU
ID CAHS1_HYPDU Reviewed; 227 AA.
AC P0CU45;
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 94205 {ECO:0000303|PubMed:28306513};
DE Short=CAHS 94205 {ECO:0000303|PubMed:28306513};
DE AltName: Full=Cytosolic-abundant heat soluble protein a {ECO:0000303|PubMed:22937162};
DE Short=SAHS-a {ECO:0000303|PubMed:22937162};
DE AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS 94205 {ECO:0000303|PubMed:28306513};
DE Short=TDP CAHS 94205 {ECO:0000303|PubMed:28306513};
GN Name=CAHS 94205 {ECO:0000303|PubMed:28306513};
GN Synonyms=CAHS-a {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).
RN [3]
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 (PubMed:22937162). {ECO:0000305|PubMed:22937162}.
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}.
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DR AlphaFoldDB; P0CU45; -.
DR SMR; P0CU45; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR DisProt; DP01380; -.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Repeat; Stress response.
FT CHAIN 1..227
FT /note="Cytosolic-abundant heat soluble protein 94205"
FT /id="PRO_0000440190"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..144
FT /note="CAHS motif 1"
FT /evidence="ECO:0000305|PubMed:22937162"
FT REGION 163..181
FT /note="CAHS motif 2"
FT /evidence="ECO:0000305|PubMed:22937162"
FT REGION 206..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..191
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 227 AA; 25485 MW; DC1DCB9C9166288B CRC64;
MSGRNVESHM ERNEKVVVNN SGHADVKKQQ QQVEHTEFTH TEVKAPLIHP APPIISTGAA
GLAEEIVGQG FTASAARISG GTAEVHLQPS AAMTEEARRD QERYRQEQES IAKQQEREME
KKTEAYRKTA EAEAEKIRKE LEKQHARDVE FRKDLIESTI DRQKREVDLE AKMAKRELDR
EGQLAKEALE RSRLATNVEV NFDSAAGHTV SGGTTISSSD KMEIKRN
