ID   PVAT_PELSI              Reviewed;          42 AA.
AC   P84818;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Pelovaterin;
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Eggshell matrix {ECO:0000269|PubMed:15877362};
RX   PubMed=15877362; DOI=10.1021/bm049276f;
RA   Lakshminarayanan R., Chi-Jin E.O., Loh X.J., Kini R.M., Valiyaveettil S.;
RT   "Purification and characterization of a vaterite-inducing peptide,
RT   pelovaterin, from the eggshells of Pelodiscus sinensis (Chinese soft-
RT   shelled turtle).";
RL   Biomacromolecules 6:1429-1437(2005).
RN   [2]
RP   STRUCTURE BY NMR, FUNCTION, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX   PubMed=18341335; DOI=10.1021/ja075659k;
RA   Lakshminarayanan R., Vivekanandan S., Samy R.P., Banerjee Y., Chi-Jin E.O.,
RA   Teo K.W., Jois S.D., Kini R.M., Valiyaveettil S.;
RT   "Structure, self-assembly, and dual role of a beta-defensin-like peptide
RT   from the Chinese soft-shelled turtle eggshell matrix.";
RL   J. Am. Chem. Soc. 130:4660-4668(2008).
CC   -!- FUNCTION: Induces the nucleation and stabilization of vaterite, one of
CC       the crystalline polymorphs of calcium carbonate. Exhibits strong
CC       antimicrobial activity against Pseudomonas aeruginosa and Proteus
CC       vulgaris. {ECO:0000269|PubMed:15877362, ECO:0000269|PubMed:18341335}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:18341335}.
CC   -!- MASS SPECTROMETRY: Mass=4189.92; Mass_error=0.89; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15877362};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PDB; 2JR3; NMR; -; A=1-42.
DR   PDBsum; 2JR3; -.
DR   AlphaFoldDB; P84818; -.
DR   BMRB; P84818; -.
DR   SMR; P84818; -.
DR   EvolutionaryTrace; P84818; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR041579; Pelovaterin.
DR   Pfam; PF17859; Pelovaterin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Biomineralization;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Reference proteome; Secreted.
FT   CHAIN           1..42
FT                   /note="Pelovaterin"
FT                   /id="PRO_0000233908"
FT   DISULFID        8..38
FT                   /evidence="ECO:0000269|PubMed:18341335"
FT   DISULFID        16..32
FT                   /evidence="ECO:0000269|PubMed:18341335"
FT   DISULFID        24..39
FT                   /evidence="ECO:0000269|PubMed:18341335"
FT   TURN            8..10
FT                   /evidence="ECO:0007829|PDB:2JR3"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:2JR3"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:2JR3"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:2JR3"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:2JR3"
SQ   SEQUENCE   42 AA;  4196 MW;  9D385431034112FD CRC64;
     DDTPSSRCGS GGWGPCLPIV DLLCIVHVTV GCSGGFGCCR IG