ID   HYAST_HYAAR             Reviewed;         131 AA.
AC   C4NZN9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Hyastatin {ECO:0000303|PubMed:19487032, ECO:0000312|EMBL:ACQ76432.1};
DE   Flags: Precursor;
OS   Hyas araneus (Atlantic lyre crab) (Great spider crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Majoidea; Majidae; Hyas.
OX   NCBI_TaxID=361634;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ACQ76432.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-67, FUNCTION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Hemocyte {ECO:0000269|PubMed:19487032};
RX   PubMed=19487032; DOI=10.1016/j.molimm.2009.05.002;
RA   Sperstad S.V., Haug T., Vasskog T., Stensvag K.;
RT   "Hyastatin, a glycine-rich multi-domain antimicrobial peptide isolated from
RT   the spider crab (Hyas araneus) hemocytes.";
RL   Mol. Immunol. 46:2604-2612(2009).
CC   -!- FUNCTION: Antimicrobial peptide. Has strong antibacterial activity
CC       against the Gram-positive bacterium C.glutamicum (MIC=0.4 uM) and the
CC       Gram-negative bacterium E.coli (MIC=12.5 uM). Has weak antibacterial
CC       activity against the Gram-positive bacterium S.aureus (MIC>50 uM) and
CC       the Gram-negative bacterium P.aeruginosa (MIC>50 uM). Has antifungal
CC       activity against S.cerevisiae (MIC=12.5) and C.albicans (MIC=6.3 uM).
CC       Has weak antifungal activity against the mold B.cinerea. Presents
CC       chitin-binding activity. {ECO:0000269|PubMed:19487032}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC       {ECO:0000250|UniProtKB:P81058}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in hemocytes, with weaker
CC       expression in gills and epidermis. Expressed at low levels in
CC       hepatopancreas. {ECO:0000269|PubMed:19487032}.
CC   -!- MASS SPECTROMETRY: Mass=11715.10; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19487032};
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=02620";
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DR   EMBL; FJ764995; ACQ76432.1; -; mRNA.
DR   AlphaFoldDB; C4NZN9; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Chitin-binding;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:19487032"
FT   CHAIN           17..130
FT                   /note="Hyastatin"
FT                   /evidence="ECO:0000269|PubMed:19487032"
FT                   /id="PRO_5000467153"
FT   MOD_RES         130
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P81058"
FT   DISULFID        103..117
FT                   /evidence="ECO:0000250|UniProtKB:P81058"
FT   DISULFID        107..124
FT                   /evidence="ECO:0000250|UniProtKB:P81058"
FT   DISULFID        118..125
FT                   /evidence="ECO:0000250|UniProtKB:P81058"
SQ   SEQUENCE   131 AA;  13452 MW;  25F2D4E883DD8221 CRC64;
     MRVLLILVSL AALAHAESFL KSKTGYQGVQ TLPGFIGGSQ PHLGGGIGGG RPFISQPNLG
     GGIGGGIGGG KPFIPQPNLG GGIGSTRPFP RPQYGDYGSR NSCNRQCPST YGGRGICCRR
     WGSCCPTNYK G