ID   CYTAR_HYPDU             Reviewed;         498 AA.
AC   A0A125S9M6;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Cytotardin {ECO:0000303|PubMed:26840051};
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   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DOMAIN, AND FUNCTION.
RX   PubMed=26840051; DOI=10.7554/elife.11117;
RA   Hering L., Bouameur J.E., Reichelt J., Magin T.M., Mayer G.;
RT   "Novel origin of lamin-derived cytoplasmic intermediate filaments in
RT   tardigrades.";
RL   Elife 5:E11117-E11117(2016).
CC   -!- FUNCTION: Intermediate filament (IF) protein that forms both short
CC       filaments and extensive cytoskeletal networks which most likely are
CC       homomeric (PubMed:26840051). Some of the cytotardin arrays display
CC       cage-like perinuclear structures, while others are located in the
CC       periphery close to the cell membrane (PubMed:26840051). The entire
CC       tardigrade body is ensheathed by a grid of belt-like filaments formed
CC       by the cytotardin protein, which retain their integrity even in
CC       contracted specimens (PubMed:26840051). The belt-like structures
CC       encircling each epidermal cell might help to resist the shearing forces
CC       that arise during freezing and thawing cycles, whereas the dense
CC       meshwork at the basis of each claw and around the stylets might provide
CC       the tissue stability necessary for locomotion and feeding
CC       (PubMed:26840051). {ECO:0000269|PubMed:26840051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26840051}.
CC       Cytoplasm, cell cortex {ECO:0000269|PubMed:26840051}. Note=Localizes in
CC       the peripheral cytoplasm of all epidermal and foregut cells, where it
CC       appears to be closely associated or aligned with the plasma membrane
CC       (PubMed:26840051). Occurs close to desmosomes but is not co-localized
CC       with desmoplakin (PubMed:26840051). {ECO:0000269|PubMed:26840051}.
CC   -!- DOMAIN: Contains an alpha-helical IF rod domain organization with three
CC       coiled coil-forming segments (coil 1A, coil 1B, and coil 2)
CC       (PubMed:26840051). {ECO:0000305|PubMed:26840051}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; KU295462; AME17872.1; -; mRNA.
DR   AlphaFoldDB; A0A125S9M6; -.
DR   SMR; A0A125S9M6; -.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   InterPro; IPR039008; IF_rod_dom.
DR   Pfam; PF00038; Filament; 1.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Intermediate filament; Stress response.
FT   CHAIN           1..498
FT                   /note="Cytotardin"
FT                   /id="PRO_0000440213"
FT   DOMAIN          22..378
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188,
FT                   ECO:0000305|PubMed:26840051"
FT   REGION          18..58
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          59..69
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          70..213
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          214..231
FT                   /note="Linker 2"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          232..371
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          381..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  57028 MW;  9784858CD1C559C7 CRC64;
     MYSSMASSIR GSTVHLSDRV HSKDELQALN TRLAKYIDKI RNLENENVAL QRQLQTAEQT
     TVTEIHRVSK NYDEELAKLR KQLEDVLRDN ARLQMERNST ESENKQLQQR VAQLEKQVRT
     LEARLRQAED LVADLQHRLS QSLDVRQQLE SDNKDLKNQI NSLKGQIQQL KQDYDNERVR
     TADLENKLQT KEEEHEFEKN ALHENLREEK SQRQYLLHDL QRGLQDEFES KLVQQLNELR
     AEYDEMIKGV RAEVEAKSES RIRDLMAMAD QQGDTVTRLQ QELEEWRKRS QTTEAELDRL
     RKENANLNAQ LTEIQRQKDD QIRALQQQIR KRQEELQRIN DDLGDLTRQY QDLLYVKLAL
     DAELATYNKL LSGEEQRLGM DGSGTVIRRP TGGATGTGSG IYGGTGSGGY SRDIGSTTTT
     KTTYTSRPTY NYTPIATTPI GGTSTTGRYT PVGGQTLAAR QPSPGGSLGR ERDIPVLREQ
     KITETFKASG RVGPRTDW