ID   MAXA_LUTLO              Reviewed;          86 AA.
AC   P30659;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Maxadilan;
DE   Flags: Precursor;
OS   Lutzomyia longipalpis (Sand fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC   Lutzomyia; Lutzomyia.
OX   NCBI_TaxID=7200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-36.
RC   TISSUE=Salivary gland;
RX   PubMed=1730635; DOI=10.1016/s0021-9258(18)48395-0;
RA   Lerner E.A., Shoemaker C.B.;
RT   "Maxadilan. Cloning and functional expression of the gene encoding this
RT   potent vasodilator peptide.";
RL   J. Biol. Chem. 267:1062-1066(1992).
RN   [2]
RP   DISULFIDE BONDS.
RX   PubMed=8624417;
RX   DOI=10.1002/(sici)1097-0231(199604)10:6<641::aid-rcm548>3.0.co;2-e;
RA   Yoshida S., Takamatsu T., Denda S., Ohnuma M., Tajima M., Lerner E.A.,
RA   Kanda F.;
RT   "Structural characterization and location of disulphide linkages of a
RT   potent vasodilatory peptide, recombinant maxadilan, by a multiple mass
RT   spectrometric approach.";
RL   Rapid Commun. Mass Spectrom. 10:641-648(1996).
RN   [3]
RP   POLYMORPHISM.
RX   PubMed=10380110; DOI=10.1046/j.1365-2583.1999.820267.x;
RA   Lanzaro G.C., Lopes A.H., Ribeiro J.M.C., Shoemaker C.B., Warburg A.,
RA   Soares M., Titus R.G.;
RT   "Variation in the salivary peptide, maxadilan, from species in the
RT   Lutzomyia longipalpis complex.";
RL   Insect Mol. Biol. 8:267-275(1999).
CC   -!- FUNCTION: Potent vasodilator. It would act as an antagonist at the
CC       endothelin receptor. This peptide may play a critical role in the
CC       enhancement of Leishmania infectivity attributed to Sand fly saliva.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- POLYMORPHISM: Extensive amino acid sequence differentiation, up to 23%,
CC       was observed among maxadilan from different populations. This is a
CC       remarkable degree of polymorphism considering the small size of this
CC       peptide. {ECO:0000269|PubMed:10380110}.
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DR   EMBL; M77090; AAA29288.1; -; Genomic_DNA.
DR   PIR; A41772; A41772.
DR   PDB; 6M1H; EM; 3.60 A; B=24-82.
DR   PDB; 7JQD; X-ray; 2.70 A; B=24-85.
DR   PDBsum; 6M1H; -.
DR   PDBsum; 7JQD; -.
DR   AlphaFoldDB; P30659; -.
DR   SMR; P30659; -.
DR   Proteomes; UP000092461; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Secreted; Signal;
KW   Vasoactive; Vasodilator.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:1730635"
FT   CHAIN           24..86
FT                   /note="Maxadilan"
FT                   /id="PRO_0000021655"
FT   DISULFID        24..28
FT                   /evidence="ECO:0000269|PubMed:8624417"
FT   DISULFID        37..74
FT                   /evidence="ECO:0000269|PubMed:8624417"
FT   HELIX           26..40
FT                   /evidence="ECO:0007829|PDB:7JQD"
FT   HELIX           69..84
FT                   /evidence="ECO:0007829|PDB:7JQD"
SQ   SEQUENCE   86 AA;  9488 MW;  D102E21D1D895DDF CRC64;
     MKQILLISLV VVLAVFAFNV AEGCDATCQF RKAIDDCQKQ AHHSNVLQTS VQTTATFTSM
     DTSQLPGNSV FKECMKQKKK EFSSGK