ID   ANPY1_TENMO             Reviewed;         112 AA.
AC   O16119;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Thermal hysteresis protein YL-1;
DE            Short=THP YL-1;
DE   AltName: Full=Beta-helix antifreeze protein 2-14;
DE            Short=THP 2-14;
DE   Flags: Precursor;
OS   Tenebrio molitor (Yellow mealworm beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrio.
OX   NCBI_TaxID=7067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Larval fat body;
RX   PubMed=9285581; DOI=10.1038/41908;
RA   Graham L.A., Liou Y.C., Walker V.K., Davies P.L.;
RT   "Hyperactive antifreeze protein from beetles.";
RL   Nature 388:727-728(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Larval fat body;
RX   PubMed=10471292; DOI=10.1021/bi990613s;
RA   Liou Y.C., Thibault P., Walker V.K., Davies P.L., Graham L.A.;
RT   "A complex family of highly heterogeneous and internally repetitive
RT   hyperactive antifreeze proteins from the beetle Tenebrio molitor.";
RL   Biochemistry 38:11415-11424(1999).
RN   [3]
RP   FUNCTION, DISULFIDE BOND, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX   PubMed=10833402; DOI=10.1006/prep.2000.1219;
RA   Liou Y.C., Daley M.E., Graham L.A., Kay C.M., Walker V.K., Sykes B.D.,
RA   Davies P.L.;
RT   "Folding and structural characterization of highly disulfide-bonded beetle
RT   antifreeze protein produced in bacteria.";
RL   Protein Expr. Purif. 19:148-157(2000).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 29-112, DISULFIDE BOND, AND
RP   DOMAIN.
RX   PubMed=10917536; DOI=10.1038/35018604;
RA   Liou Y.C., Tocilj A., Davies P.L., Jia Z.;
RT   "Mimicry of ice structure by surface hydroxyls and water of a beta-helix
RT   antifreeze protein.";
RL   Nature 406:322-324(2000).
RN   [5]
RP   STRUCTURE BY NMR OF 29-112, DISULFIDE BOND, AND DOMAIN.
RX   PubMed=11969412; DOI=10.1021/bi0121252;
RA   Daley M.E., Spyracopoulos L., Jia Z., Davies P.L., Sykes B.D.;
RT   "Structure and dynamics of a beta-helical antifreeze protein.";
RL   Biochemistry 41:5515-5525(2002).
CC   -!- FUNCTION: Contributes to protect body fluid from freezing at subzero
CC       temperatures. Lowers the freezing point of the hemolymph by about 2.5
CC       degrees at a concentration of 1 mg/ml. Binds to nascent ice crystals
CC       and prevents further growth. {ECO:0000269|PubMed:10471292,
CC       ECO:0000269|PubMed:10833402, ECO:0000269|PubMed:9285581}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10833402}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: Forms a right-handed beta-helix that is stabilized by disulfide
CC       bonds. The building blocks of this beta-helix correspond to tandem
CC       repeats with the consensus sequence T-C-T-X-S-X-X-C-X-X-A-X.
CC       {ECO:0000269|PubMed:10917536, ECO:0000269|PubMed:11969412}.
CC   -!- SIMILARITY: Belongs to the insect antifreeze protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF160494; AAB70750.1; -; mRNA.
DR   PDB; 1EZG; X-ray; 1.40 A; A/B=29-112.
DR   PDB; 1L1I; NMR; -; A=29-112.
DR   PDBsum; 1EZG; -.
DR   PDBsum; 1L1I; -.
DR   AlphaFoldDB; O16119; -.
DR   SMR; O16119; -.
DR   EvolutionaryTrace; O16119; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR003460; Insect_antifreeze_prot_motif.
DR   InterPro; IPR016133; Insect_cyst_antifreeze_prot.
DR   Pfam; PF02420; AFP; 8.
DR   SUPFAM; SSF51156; SSF51156; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antifreeze protein; Disulfide bond; Repeat; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..112
FT                   /note="Thermal hysteresis protein YL-1"
FT                   /id="PRO_5000056897"
FT   DISULFID        30..39
FT   DISULFID        36..46
FT   DISULFID        43..49
FT   DISULFID        55..61
FT   DISULFID        67..73
FT   DISULFID        79..85
FT   DISULFID        91..97
FT   DISULFID        103..109
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:1EZG"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:1EZG"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:1EZG"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:1EZG"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:1EZG"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:1L1I"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:1EZG"
FT   STRAND          101..105
FT                   /evidence="ECO:0007829|PDB:1EZG"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:1L1I"
SQ   SEQUENCE   112 AA;  11558 MW;  C06D7AB6401BC909 CRC64;
     MAFKTCGFSK KWLVIAVIVM CLCTECYCQC TGGADCTSCT GACTGCGNCP NAVTCTNSQH
     CVKANTCTGS TDCNTAQTCT NSKDCFEANT CTDSTNCYKA TACTNSSGCP GH