ID   CAHS1_RAMVA             Reviewed;         237 AA.
AC   J7M799;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Cytosolic-abundant heat soluble protein 1 {ECO:0000303|PubMed:22937162};
DE            Short=CAHS1 {ECO:0000303|PubMed:22937162};
DE   AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS1 {ECO:0000305};
DE            Short=TDP CAHS1 {ECO:0000305};
GN   Name=CAHS1 {ECO:0000303|PubMed:22937162}; ORFNames=RvY_00944;
OS   Ramazzottius varieornatus (Water bear) (Tardigrade).
OC   Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC   Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX   NCBI_TaxID=947166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP   DOMAIN, AND SUBCELLULAR LOCATION.
RC   STRAIN=YOKOZUNA-1;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YOKOZUNA-1;
RX   PubMed=27649274; DOI=10.1038/ncomms12808;
RA   Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA   Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA   Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA   Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA   Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT   "Extremotolerant tardigrade genome and improved radiotolerance of human
RT   cultured cells by tardigrade-unique protein.";
RL   Nat. Commun. 7:12808-12808(2016).
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:22937162, 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:22937162, ECO:0000269|PubMed:33545053,
CC       ECO:0000305|PubMed:33545053}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22937162}. Nucleus
CC       {ECO:0000269|PubMed:22937162}. Note=Is distributed mostly in the
CC       cytoplasm and weakly in the nucleus (PubMed:22937162).
CC       {ECO:0000269|PubMed:22937162}.
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   -!- 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) (By
CC       similarity). {ECO:0000250|UniProtKB:P0CU44}.
CC   -!- SIMILARITY: Belongs to the Cytosolic-abundant heat soluble protein
CC       (CAHS) family. {ECO:0000305}.
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DR   EMBL; AB650499; BAM37958.1; -; mRNA.
DR   EMBL; BDGG01000001; GAU88202.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7M799; -.
DR   SMR; J7M799; -.
DR   Proteomes; UP000186922; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   DisProt; DP01377; -.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW   Stress response.
FT   CHAIN           1..237
FT                   /note="Cytosolic-abundant heat soluble protein 1"
FT                   /id="PRO_0000440187"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..150
FT                   /note="CAHS motif 1"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          169..187
FT                   /note="CAHS motif 2"
FT                   /evidence="ECO:0000305|PubMed:22937162"
FT   REGION          212..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          98..201
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        14..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   237 AA;  26979 MW;  F496EC5D8A83A670 CRC64;
     MPYEKHVEQT VVEKTEQPGH SSTHHAPAQR TVAREQEEVV HKEFTHTDIR VPHIDAPPPI
     IAASAVGLAE EIVSHGFQAS AARISGASTE VDMRPSPKLA EEARRDAERY QKEHEMINRQ
     AEATLQKKAE EYRHQTEAEA EKIRRELEKQ HERDIQFRKD LIDQTIEKQK REVDLEAKMA
     KRELDREAQL AKEALERSRM ATNVEVTLDT AAGHTVSGGT TVSSVDKVET VRERKHH