ARA1_HYAAR
ID ARA1_HYAAR Reviewed; 64 AA.
AC A6XMY0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Arasin 1 {ECO:0000303|PubMed:17658600};
DE Short=Ara-1 {ECO:0000303|PubMed:17658600};
DE AltName: Full=Proline-rich antimicrobial peptide {ECO:0000303|PubMed:23326415};
DE Short=PR-AMP {ECO:0000303|PubMed:23326415, ECO:0000303|PubMed:26860543};
DE Short=Pro-rich AMP {ECO:0000303|PubMed:23326415};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-62, FUNCTION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, SYNTHESIS, AND DISULFIDE BOND.
RC TISSUE=Hemocyte;
RX PubMed=17658600; DOI=10.1016/j.dci.2007.06.002;
RA Stensvag K., Haug T., Sperstad S.V., Rekdal O., Indrevoll B.,
RA Styrvold O.B.;
RT "Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the
RT spider crab, Hyas araneus.";
RL Dev. Comp. Immunol. 32:275-285(2008).
RN [2]
RP FUNCTION OF N-TERMINAL PEPTIDE 26-48, SUBUNIT, AND SYNTHESIS.
RX PubMed=23326415; DOI=10.1371/journal.pone.0053326;
RA Paulsen V.S., Blencke H.M., Benincasa M., Haug T., Eksteen J.J.,
RA Styrvold O.B., Scocchi M., Stensvaag K.;
RT "Structure-activity relationships of the antimicrobial peptide arasin 1
RT - and mode of action studies of the N-terminal, proline-rich region.";
RL PLoS ONE 8:E53326-E53326(2013).
RN [3]
RP FUNCTION OF N-TERMINAL PEPTIDE 26-50.
RX PubMed=26860543; DOI=10.1099/mic.0.000249;
RA Paulsen V.S., Mardirossian M., Blencke H.M., Benincasa M., Runti G.,
RA Nepa M., Haug T., Stensvaag K., Scocchi M.;
RT "Inner membrane proteins YgdD and SbmA are required for the complete
RT susceptibility of Escherichia coli to the proline-rich antimicrobial
RT peptide arasin 1(1-25).";
RL Microbiology 162:601-609(2016).
CC -!- FUNCTION: Antimicrobial peptide that has a large activity spectrum with
CC activity against Gram-positive, Gram-negative bacteria, as well as
CC against fungi (PubMed:17658600, PubMed:23326415). Shows activity at
CC micromolar concentrations (PubMed:17658600, PubMed:23326415). Displays
CC minimal inhibitory concentration (MIC) values lower than minimal
CC bactericidal concentrations (MBC) (PubMed:17658600). Synthetic peptides
CC with similar activities than the full length peptide (composed of the
CC first 23 or 25 amino acids (Arasin 1(26-48) or Arasin 1(26-50))) may
CC have a dual mode of action depending on the peptide concentrations
CC (PubMed:23326415, PubMed:26860543). At MIC concentrations, the peptide
CC penetrates into the cytoplasm of target cells (tested on the Gram-
CC negative E.Coli) (PubMed:26860543). The two inner membrane proteins
CC YgdD and SbmA may be required for this uptake (PubMed:26860543). At
CC concentrations higher than MIC, arasin may act by disrupting membranes
CC (PubMed:23326415). Full-length and N-terminal peptides do not show
CC hemolytic activity (PubMed:23326415). {ECO:0000269|PubMed:17658600,
CC ECO:0000269|PubMed:23326415, ECO:0000269|PubMed:26860543}.
CC -!- SUBUNIT: Interacts with chitin through the N-terminal region (26-48)
CC (PubMed:23326415). This interaction may be important, since chitin is a
CC component of the fungal cell wall, as well as of the crab exoskeleton
CC (permitting a possible action of arasin in wound healing in case of
CC lesions) (PubMed:23326415). {ECO:0000269|PubMed:23326415}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in hemocytes. No or very low
CC expression in heart, gills, inestines, and epidermis.
CC {ECO:0000269|PubMed:17658600}.
CC -!- PTM: Disulfide bonds are important for activity especially against
CC Gram-negative bacteria, since the linearization of the peptide causes a
CC strong decrease of activity on these bacteria.
CC {ECO:0000269|PubMed:23326415}.
CC -!- MASS SPECTROMETRY: Mass=4342.06; Method=Electrospray; Note=Monoisotopic
CC mass.; Evidence={ECO:0000269|PubMed:17658600};
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00987";
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DR EMBL; DQ859904; ABI74601.1; -; mRNA.
DR AlphaFoldDB; A6XMY0; -.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Chitin-binding; Direct protein sequencing;
KW Disulfide bond; Fungicide; Immunity; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:17658600"
FT CHAIN 26..62
FT /note="Arasin 1"
FT /evidence="ECO:0000269|PubMed:17658600"
FT /id="PRO_5002704929"
FT PROPEP 63..64
FT /evidence="ECO:0000269|PubMed:17658600"
FT /id="PRO_0000449320"
FT REGION 22..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..48
FT /note="Pro/Arg-rich region responsible for antibacterial
FT and antifungal activity"
FT /evidence="ECO:0000269|PubMed:23326415"
FT REGION 49..62
FT /note="Cystein-containing C-terminal region important for
FT stability but not essential for antimicrobial activity"
FT /evidence="ECO:0000305|PubMed:23326415"
FT COMPBIAS 29..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 50..59
FT /evidence="ECO:0000269|PubMed:17658600"
FT DISULFID 52..57
FT /evidence="ECO:0000269|PubMed:17658600"
SQ SEQUENCE 64 AA; 7227 MW; D751151B1534B1FD CRC64;
MERRTLLVVL LVCSCVVAAA AEASPSRWPS PGRPRPFPGR PKPIFRPRPC NCYAPPCPCD
RWRH
