AURE_AURAU
ID AURE_AURAU Reviewed; 84 AA.
AC Q0MWV8; P84891;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Antimicrobial peptide aurelin {ECO:0000303|PubMed:16890198, ECO:0000303|PubMed:23137541};
DE Flags: Precursor;
OS Aurelia aurita (Moon jellyfish) (Medusa aurita).
OC Eukaryota; Metazoa; Cnidaria; Scyphozoa; Semaeostomeae; Ulmaridae; Aurelia.
OX NCBI_TaxID=6145;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-84, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mesoglea;
RX PubMed=16890198; DOI=10.1016/j.bbrc.2006.07.078;
RA Ovchinnikova T.V., Balandin S.V., Aleshina G.M., Tagaev A.A., Leonova Y.F.,
RA Krasnodembsky E.D., Men'shenin A.V., Kokryakov V.N.;
RT "Aurelin, a novel antimicrobial peptide from jellyfish Aurelia aurita with
RT structural features of defensins and channel-blocking toxins.";
RL Biochem. Biophys. Res. Commun. 348:514-523(2006).
RN [2]
RP STRUCTURE BY NMR, DISULFIDE BOND, FUNCTION, AND SITES OF INTERACTION WITH
RP MEMBRANES.
RX PubMed=23137541; DOI=10.1016/j.bbrc.2012.10.092;
RA Shenkarev Z.O., Panteleev P.V., Balandin S.V., Gizatullina A.K.,
RA Altukhov D.A., Finkina E.I., Kokryakov V.N., Arseniev A.S.,
RA Ovchinnikova T.V.;
RT "Recombinant expression and solution structure of antimicrobial peptide
RT aurelin from jellyfish Aurelia aurita.";
RL Biochem. Biophys. Res. Commun. 429:63-69(2012).
CC -!- FUNCTION: Antimicrobial peptide with modest activity (PubMed:16890198,
CC PubMed:23137541). Active against the Gram-positive bacterium
CC L.monocytogenes (MIC=22.64 ug/ml), B.megaterium (MIC=10 uM),
CC B.mycoides, B.subtilis, M.luteus (MIC=40 uM), M.phlei, and S.aureus,
CC and the Gram-negative bacterium E.coli (MIC=7.66 ug/ml) and
CC P.aeruginosa (PubMed:16890198, PubMed:23137541). Shows moderate
CC affinity to the negatively charged (POPC/DOPG 3:1) lipid vesicles
CC (PubMed:23137541). The peptide interacts with the surface of DPC
CC micelles by two alpha-helical regions (PubMed:23137541). It does not
CC interact with the zwitterionic (POPC) lipid vesicles, which model
CC membranes of eukaryotic cells (PubMed:23137541).
CC {ECO:0000269|PubMed:16890198, ECO:0000269|PubMed:23137541}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane
CC {ECO:0000269|PubMed:16890198, ECO:0000269|PubMed:23137541}.
CC Note=Isolated from mesoglea. {ECO:0000305|PubMed:16890198}.
CC -!- DOMAIN: The peptide interacts with the surface of DPC micelles by two
CC alpha-helical regions. {ECO:0000269|PubMed:23137541}.
CC -!- MASS SPECTROMETRY: Mass=4297.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16890198};
CC -!- SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin
CC family. {ECO:0000305}.
CC -!- CAUTION: Shows similarity to potassium channel (Kv) toxins, but does
CC not possess the 'functional dyad' element required for binding to Kv
CC channels. As a consequence, it may not be a channel blocker.
CC {ECO:0000305|PubMed:23137541}.
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DR EMBL; DQ837210; ABI18349.1; -; mRNA.
DR PDB; 2LG4; NMR; -; A=45-84.
DR PDBsum; 2LG4; -.
DR AlphaFoldDB; Q0MWV8; -.
DR BMRB; Q0MWV8; -.
DR SMR; Q0MWV8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR InterPro; IPR003582; ShKT_dom.
DR Pfam; PF01549; ShK; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Membrane; Secreted; Signal; Target cell membrane;
KW Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..44
FT /evidence="ECO:0000269|PubMed:16890198"
FT /id="PRO_0000253932"
FT PEPTIDE 45..84
FT /note="Antimicrobial peptide aurelin"
FT /evidence="ECO:0000269|PubMed:16890198"
FT /id="PRO_0000253933"
FT DOMAIN 47..84
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT SITE 50
FT /note="The positively charged side chain either protrude
FT into the micelle interior or reside in close proximity to
FT its surface"
FT /evidence="ECO:0000305|PubMed:23137541"
FT SITE 52
FT /note="The positively charged side chain either protrude
FT into the micelle interior or reside in close proximity to
FT its surface"
FT /evidence="ECO:0000305|PubMed:23137541"
FT SITE 54
FT /note="The positively charged side chain either protrude
FT into the micelle interior or reside in close proximity to
FT its surface"
FT /evidence="ECO:0000305|PubMed:23137541"
FT SITE 55
FT /note="The hydrophobic side chain is located at the binding
FT interface of DPC micelle"
FT /evidence="ECO:0000305|PubMed:23137541"
FT SITE 59
FT /note="The hydrophobic side chain is located at the binding
FT interface of DPC micelle"
FT /evidence="ECO:0000305|PubMed:23137541"
FT SITE 68
FT /note="The positively charged side chain either protrude
FT into the micelle interior or reside in close proximity to
FT its surface"
FT /evidence="ECO:0000305|PubMed:23137541"
FT SITE 71
FT /note="The hydrophobic side chain is located at the binding
FT interface of DPC micelle"
FT /evidence="ECO:0000305|PubMed:23137541"
FT SITE 72
FT /note="The positively charged side chain either protrude
FT into the micelle interior or reside in close proximity to
FT its surface"
FT /evidence="ECO:0000305|PubMed:23137541"
FT SITE 73
FT /note="The hydrophobic side chain is located at the binding
FT interface of DPC micelle"
FT /evidence="ECO:0000305|PubMed:23137541"
FT DISULFID 47..84
FT /evidence="ECO:0000269|PubMed:23137541,
FT ECO:0000312|PDB:2LG4"
FT DISULFID 56..77
FT /evidence="ECO:0000269|PubMed:23137541,
FT ECO:0000312|PDB:2LG4"
FT DISULFID 63..81
FT /evidence="ECO:0000269|PubMed:23137541,
FT ECO:0000312|PDB:2LG4"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:2LG4"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:2LG4"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:2LG4"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:2LG4"
SQ SEQUENCE 84 AA; 9184 MW; 3370F543F7615E35 CRC64;
MGCFKVLVLF AAILCMSLLV CAEDEVNLQA QIEEGPMEAI RSRRAACSDR AHGHICESFK
SFCKDSGRNG VKLRANCKKT CGLC
