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ACHC_LISFU
ID   ACHC_LISFU              Reviewed;         531 AA.
AC   P35903;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Achacin;
DE   Flags: Precursor;
OS   Lissachatina fulica (Giant African land snail) (Achatina fulica).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC   Helicina; Achatinoidea; Achatinidae; Lissachatina.
OX   NCBI_TaxID=2315439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-41; 206-216 AND
RP   285-294.
RC   STRAIN=Ferussac; TISSUE=Collar;
RX   PubMed=1396687; DOI=10.1111/j.1432-1033.1992.tb17254.x;
RA   Obara K., Otsuka-Fuchino H., Sattayasai N., Nonomura Y., Tsuchiya T.,
RA   Tamiya T.;
RT   "Molecular cloning of the antibacterial protein of the giant African snail,
RT   Achatina fulica Ferussac.";
RL   Eur. J. Biochem. 209:1-6(1992).
CC   -!- FUNCTION: Antibacterial glycoprotein.
CC   -!- SUBUNIT: Homodimer.
CC   -!- TISSUE SPECIFICITY: Collar tissue.
CC   -!- SIMILARITY: To A.kurodai aplysianin-A. {ECO:0000305}.
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DR   EMBL; X64584; CAA45871.1; -; mRNA.
DR   PIR; S28260; S28260.
DR   AlphaFoldDB; P35903; -.
DR   SMR; P35903; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Glycoprotein; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..29
FT                   /evidence="ECO:0000269|PubMed:1396687"
FT                   /id="PRO_0000020621"
FT   CHAIN           30..531
FT                   /note="Achacin"
FT                   /id="PRO_0000020622"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   531 AA;  59087 MW;  D8A92302BDDD8A4E CRC64;
     MLLLNSALFI LCLVCWLPGT SSSRVLTRRE GPQCSRSVDV AVVGAGPSGT YSAYKLRNKG
     QTVELFEYSN RIGGRLFTTH LPNVPDLNLE SGGMRYFKNH HKIFGVLVKE LNLSNKEFTE
     GFGKPGRTRF FARGKSLTLE EMTSGDVPYN LSTEEKANQA NLAGYYLKKL TGFDGEVLTI
     PQANKLEVDD GRKLYQLTVD EALDKVGTPE GKEFLKAFST GNTEFIEGVS AVNYFLVELG
     EREEEILTLT DGMSALPQAL ADAFLKSSTS HALTLNRKLQ SLSKTDNGLY LLEFLETNTH
     EGYTEESNIT DLVCARKVIL AIPQSALIHL DWKPLRSETV NEAFNAVKFI PTSKVFLTFP
     TAWWLSDAVK NPAFVVKSTS PFNQMYDWKS SNVTGDAAMI ASYADTSDTK FQENLNSKGE
     LIPGSAPGAN RVTVALKEEL LSQLSQAYGI ERSDIPEPKS GTSQFWSSYP FEGDWTVWKA
     GYHCEYTQYI IERPSLIDDV FVVGSDHVNC IENAWTESAF LSVENVFEKY F
 
 
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