ARA2_HYAAR
ID ARA2_HYAAR Reviewed; 67 AA.
AC A6XMY1;
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 2 {ECO:0000303|PubMed:17658600};
DE Short=Ara-2 {ECO:0000303|PubMed:17658600};
DE AltName: Full=Proline/arginine-rich antimicrobial peptide {ECO:0000303|PubMed:17658600};
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], AND TISSUE SPECIFICITY.
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).
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. Shows activity at micromolar concentrations. Displays
CC minimal inhibitory concentration (MIC) values lower than minimal
CC bactericidal concentrations (MBC). May have a dual mode of action
CC depending on the peptide concentrations. At MIC concentrations, the
CC peptide penetrates into the cytoplasm of target cells (tested on the
CC Gram-negative E.Coli). The two inner membrane proteins YgdD and SbmA
CC may be required for this uptake. At concentrations higher than MIC,
CC arasin may act by disrupting membranes. Does not show hemolytic
CC activity. {ECO:0000250|UniProtKB:A6XMY0}.
CC -!- SUBUNIT: Interacts with chitin through the N-terminal region (26-48).
CC This interaction may be important, since chitin is a component of the
CC fungal cell wall, as well as of the crab exoskeleton (permitting a
CC possible action of arasin in wound healing in case of lesions).
CC {ECO:0000250|UniProtKB:A6XMY0}.
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:0000250|UniProtKB:A6XMY0}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00988";
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DR EMBL; DQ859905; ABI74602.1; -; mRNA.
DR AlphaFoldDB; A6XMY1; -.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Disulfide bond; Immunity; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250|UniProtKB:A6XMY0"
FT CHAIN 26..67
FT /note="Arasin 2"
FT /evidence="ECO:0000250|UniProtKB:A6XMY0"
FT /id="PRO_5002705399"
FT REGION 22..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 50..59
FT /evidence="ECO:0000250|UniProtKB:A6XMY0"
FT DISULFID 52..57
FT /evidence="ECO:0000250|UniProtKB:A6XMY0"
SQ SEQUENCE 67 AA; 7463 MW; 5D55275BDC3FAD46 CRC64;
MERRTLLVVL LVCSCVVAAA AEASPSRWPS PGRPRPFPGR PNPIFRPRPC ICVRQPCPCD
TYGGNRW
