AIP_HYAAS
ID AIP_HYAAS Reviewed; 221 AA.
AC D5LGE0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Immunoregulatory peptides {ECO:0000303|PubMed:20178988};
DE AltName: Full=Anti-inflammatory peptides {ECO:0000305};
DE Contains:
DE RecName: Full=Hyalomin-A1 {ECO:0000303|PubMed:20178988};
DE Contains:
DE RecName: Full=Hyalomin-B1 {ECO:0000303|PubMed:20178988};
DE Contains:
DE RecName: Full=Hyalomin-B2 {ECO:0000303|PubMed:20178988};
DE Contains:
DE RecName: Full=Hyalomin-B3 {ECO:0000303|PubMed:20178988};
DE Flags: Precursor;
OS Hyalomma asiaticum asiaticum (Tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Hyalomminae; Hyalomma.
OX NCBI_TaxID=266039;
RN [1] {ECO:0000312|EMBL:ADE87883.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-56; 95-105; 108-141 AND
RP 144-154, FUNCTION, MASS SPECTROMETRY, AND MUTAGENESIS OF TYR-55; TYR-66 AND
RP TYR-90.
RC TISSUE=Salivary gland;
RX PubMed=20178988; DOI=10.1074/jbc.m109.094615;
RA Wu J., Wang Y., Liu H., Yang H., Ma D., Li J., Li D., Lai R., Yu H.;
RT "Two immunoregulatory peptides with antioxidant activity from tick salivary
RT glands.";
RL J. Biol. Chem. 285:16606-16613(2010).
CC -!- FUNCTION: [Hyalomin-A1]: Suppress host inflammatory response. Exerts
CC significant anti-inflammatory functions, either by directly inhibiting
CC host secretion of inflammatory factors such as tumor necrosis factor-
CC alpha (TNF), monocyte chemotactic protein-1 (CCL2), and interferon-
CC gamma (IFNG) or by indirectly increasing the secretion of
CC immunosuppressant cytokine of interleukin-10 (IL10). Also potently
CC scavenges free radical in vitro in a rapid manner. All tested
CC concentrations of this peptide have little effect on the cell
CC viability. In vivo, inhibits hind paw adjuvant-induced inflammation in
CC mouse in a dose-dependent manner. {ECO:0000269|PubMed:20178988}.
CC -!- FUNCTION: [Hyalomin-B1]: Suppress host inflammatory response. Exerts
CC significant anti-inflammatory functions, either by directly inhibiting
CC host secretion of inflammatory factors such as tumor necrosis factor-
CC alpha (TNF), monocyte chemotactic protein-1 (CCL2), and interferon-
CC gamma (IFNG) or by indirectly increasing the secretion of
CC immunosuppressant cytokine of interleukin-10 (IL10). Also potently
CC scavenges free radical in vitro in a rapid manner. Low concentrations
CC of this peptide have little effect on the cell viability, whereas high
CC concentrations increase the cell viability by 10-20%. In vivo, inhibits
CC hind paw adjuvant-induced inflammation in mouse in a dose-dependent
CC manner. {ECO:0000269|PubMed:20178988}.
CC -!- FUNCTION: [Hyalomin-B2]: Not studied but probably similar to Hyalomin-
CC B1. {ECO:0000305}.
CC -!- FUNCTION: [Hyalomin-B3]: Not studied but probably similar to Hyalomin-
CC B1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20178988}.
CC -!- TISSUE SPECIFICITY: Salivary glands. {ECO:0000305|PubMed:20178988}.
CC -!- MASS SPECTROMETRY: [Hyalomin-A1]: Mass=1231.19; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20178988};
CC -!- MASS SPECTROMETRY: [Hyalomin-B2]: Mass=3688.27; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20178988};
CC -!- CAUTION: The sequence TLRTTTGYWTTVEKGNGTTPAANSTEKGNRPYGR described in
CC the text of Wu et al., 2010 as Hyalomin-B1 is indicated as Hyalomin-B2
CC in Fig.1b. Therefore, it is uncertain whether the function described
CC for Hyalomin-B1 is not the function of Hyalomin-B2.
CC {ECO:0000305|PubMed:20178988}.
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DR EMBL; GU828034; ADE87883.1; -; mRNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..45
FT /evidence="ECO:0000305"
FT /id="PRO_0000455210"
FT PEPTIDE 46..56
FT /note="Hyalomin-A1"
FT /evidence="ECO:0000269|PubMed:20178988"
FT /id="PRO_0000455211"
FT CHAIN 59..92
FT /note="Hyalomin-B1"
FT /evidence="ECO:0000269|PubMed:20178988"
FT /id="PRO_5003074030"
FT PEPTIDE 95..105
FT /note="Hyalomin-A1"
FT /evidence="ECO:0000269|PubMed:20178988"
FT /id="PRO_0000455212"
FT CHAIN 108..141
FT /note="Hyalomin-B2"
FT /evidence="ECO:0000305|PubMed:20178988"
FT /id="PRO_0000455213"
FT PEPTIDE 144..154
FT /note="Hyalomin-A1"
FT /evidence="ECO:0000269|PubMed:20178988"
FT /id="PRO_0000455214"
FT CHAIN 157..188
FT /note="Hyalomin-B3"
FT /evidence="ECO:0000305|PubMed:20178988"
FT /id="PRO_0000455215"
FT PROPEP 191..221
FT /evidence="ECO:0000305"
FT /id="PRO_0000455216"
FT REGION 21..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 55
FT /note="Y->G: High decrease in antioxidant cability."
FT /evidence="ECO:0000269|PubMed:20178988"
FT MUTAGEN 66
FT /note="Y->G: High decrease in antioxidant cability."
FT /evidence="ECO:0000269|PubMed:20178988"
FT MUTAGEN 90
FT /note="Y->G: Low decrease in antioxidant cability."
FT /evidence="ECO:0000269|PubMed:20178988"
SQ SEQUENCE 221 AA; 24578 MW; 2F44E451899395F9 CRC64;
MNYLCLVVTL VAVAGAISGE KFSDDNTGYQ STPSLRIRTT PGRRRQTPRT IGPPYTRRTL
RTTTDYSTTV ENGNLTTPAA NSTEKGNGLY GLRRQTPRTI GPPYTRRTLR TTTGYWTTVE
KGNGTTPAAN STEKGNRPYG RRRQTPRTIG PPYTRRTTTD YWAAVEKGYL TTPAANSTEK
ESRPNATQRR EISWTFGPLY TWRTTKGYGT TLETTNATST S
