ID   LEAM_HYPDU              Reviewed;         238 AA.
AC   P0CU49;
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=Group 3 late-embryogenesis abundant protein, mitochondrial {ECO:0000250|UniProtKB:A0A0E4AVP3};
DE            Short=LEAM {ECO:0000250|UniProtKB:A0A0E4AVP3};
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   FUNCTION.
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   [2]
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: Mitochondrial heat soluble protein acting as a molecular
CC       shield in water-deficient condition. {ECO:0000250|UniProtKB:A0A0E4AVP3,
CC       ECO:0000269|PubMed:28306513, ECO:0000269|PubMed:33545053}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:A0A0E4AVP3}.
CC   -!- DOMAIN: Contiguous repeats of the 11-mer LEA motif is characteristic of
CC       group 3 LEA proteins and form an amphipathic helical structure under
CC       water-deficient conditions. {ECO:0000250|UniProtKB:A0A0E4AVP3}.
CC   -!- SIMILARITY: Belongs to the LEA type 4 family. {ECO:0000305}.
CC   -!- CAUTION: Was identified as a CAHS family protein, an intrinsically
CC       unstructured protein that shows heat-dependent glass transition, which
CC       contributes to the vitrification of cells, and this further leads to
CC       desiccation tolerance (PubMed:28306513). However, it actually belongs
CC       to the LEA type 4 family of proteins and there was no evidence
CC       supporting glass transition itself to be contributing to the glass
CC       transition of the whole tardigrade (PubMed:33545053).
CC       {ECO:0000269|PubMed:28306513, ECO:0000269|PubMed:33545053}.
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DR   AlphaFoldDB; P0CU49; -.
DR   SMR; P0CU49; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   DisProt; DP01386; -.
PE   3: Inferred from homology;
KW   Coiled coil; Mitochondrion; Repeat; Stress response.
FT   CHAIN           1..238
FT                   /note="Group 3 late-embryogenesis abundant protein,
FT                   mitochondrial"
FT                   /id="PRO_0000440196"
FT   REPEAT          64..74
FT                   /note="LEA 11-mer repeat 1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E4AVP3"
FT   REPEAT          89..99
FT                   /note="LEA 11-mer repeat 2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E4AVP3"
FT   REPEAT          140..150
FT                   /note="LEA 11-mer repeat 3"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E4AVP3"
FT   REPEAT          151..161
FT                   /note="LEA 11-mer repeat 4"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E4AVP3"
FT   REPEAT          179..189
FT                   /note="LEA 11-mer repeat 5"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E4AVP3"
FT   REPEAT          190..200
FT                   /note="LEA 11-mer repeat 6"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E4AVP3"
FT   REGION          41..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          50..202
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        182..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   238 AA;  25461 MW;  B4F60A3D30AC1BF0 CRC64;
     MFLARNVSRV ALRSASLSPA AIPQQQHAGV AAVYAVRFAS SSGSGRPADN WAESQKEKAK
     AGLKDAQAEV GKVAREVKDK AAGGIEQAKD AVKQGANDLK RSGSRTFENA KDDIQAKAQH
     AKSDLKGAKH QAEGVVENVK EAAENAWEKT KDVAENLKDK VQSPGGLADK AANAWETVKD
     RAQDAASEVK HKAGDLKDKA QQVIHDATTQ SGDNRKQDQQ QRRDSQGSQS GQNSRSRN