SAHS1_RAMVA
ID SAHS1_RAMVA Reviewed; 169 AA.
AC J7MFT5;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Secretory-abundant heat soluble protein 1 {ECO:0000303|PubMed:22937162};
DE Short=SAHS1 {ECO:0000303|PubMed:22937162};
DE AltName: Full=Tardigrade-specific intrinsically disordered protein SAHS1 {ECO:0000305};
DE Short=TDP SAHS1 {ECO:0000305};
DE Flags: Precursor;
GN Name=SAHS1 {ECO:0000303|PubMed:22937162}; ORFNames=RvY_02423;
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 SUBCELLULAR LOCATION, AND DOMAIN.
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).
CC -!- FUNCTION: Secreted heat soluble protein acting as a molecular shield in
CC water-deficient condition (PubMed:22937162). 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 (By
CC similarity). {ECO:0000250|UniProtKB:P0CU39,
CC ECO:0000269|PubMed:22937162}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22937162}.
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 -!- 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:P0CU39}.
CC -!- SIMILARITY: Belongs to the Secretory-abundant heat soluble protein
CC (SAHS) family. {ECO:0000305}.
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DR EMBL; AB650497; BAM37956.1; -; mRNA.
DR EMBL; BDGG01000001; GAU89931.1; -; Genomic_DNA.
DR PDB; 5XN9; X-ray; 1.45 A; A/B=31-167.
DR PDB; 5XNA; X-ray; 1.80 A; A/B=31-167.
DR PDBsum; 5XN9; -.
DR PDBsum; 5XNA; -.
DR AlphaFoldDB; J7MFT5; -.
DR SMR; J7MFT5; -.
DR Proteomes; UP000186922; Unassembled WGS sequence.
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; IPR000463; Fatty_acid-bd.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Reference proteome; Secreted; Signal;
KW Stress response.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..169
FT /note="Secretory-abundant heat soluble protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5003795924"
FT REGION 31..60
FT /note="SAHS-c1"
FT /evidence="ECO:0000305|PubMed:22937162"
FT REGION 75..103
FT /note="SAHS-c2"
FT /evidence="ECO:0000305|PubMed:22937162"
FT REGION 116..165
FT /note="SAHS-c3"
FT /evidence="ECO:0000305|PubMed:22937162"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT STRAND 39..49
FT /evidence="ECO:0007829|PDB:5XN9"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:5XN9"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:5XN9"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:5XN9"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:5XN9"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:5XN9"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:5XN9"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5XN9"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:5XN9"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:5XN9"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5XN9"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:5XN9"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:5XN9"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:5XN9"
SQ SEQUENCE 169 AA; 19130 MW; 1D3946622D1F08AE CRC64;
MSRAAVAIAL LGCVVAAYGA PAEGHDDAKA EWTGKSWMGK WESTDRIENF DAFISALGLP
LEQYGGNHKT FHKIWKEGDH YHHQISVPDK NYKNDVNFKL NEEGTTQHNN TEIKYKYTED
GGNLKAEVHV PSRNKVIHDE YKVNGDELEK TYKVGDVTAK RWYKKSSSS
