HPEP_AEDAE
ID HPEP_AEDAE Reviewed; 128 AA.
AC Q9GQV7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Head peptide;
DE Short=Aea-HP;
DE Short=AeaHP;
DE Contains:
DE RecName: Full=Decapeptide 1;
DE AltName: Full=Decapeptide I;
DE Contains:
DE RecName: Full=Decapeptide 2;
DE AltName: Full=Decapeptide II;
DE Contains:
DE RecName: Full=Decapeptide 3;
DE AltName: Full=Decapeptide III;
DE Flags: Precursor;
GN Name=HP-I {ECO:0000312|EMBL:AAG43377.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG43377.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Head {ECO:0000269|PubMed:11931033};
RX PubMed=11931033; DOI=10.1603/0022-2585-39.2.331;
RA Stracker T.H., Thompson S., Grossman G.L., Riehle M.A., Brown M.R.;
RT "Characterization of the AeaHP gene and its expression in the mosquito
RT Aedes aegypti (Diptera: Culicidae).";
RL J. Med. Entomol. 39:331-342(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 23-32; 56-65 AND 80-89, PYROGLUTAMATE FORMATION AT
RP GLN-23; GLN-56 AND GLN-80, HYDROXYLATION AT PRO-26; PRO-59 AND PRO-83, AND
RP AMIDATION AT PHE-32; PHE-65 AND PHE-89.
RC TISSUE=Head {ECO:0000269|Ref.3};
RA Matsumoto S., Brown M.R., Crim J.W., Vigna S.R., Lea A.O.;
RT "Isolation and primary structure of neuropeptides from the mosquito, Aedes
RT aegypti, immunoreactive to FMRFamide antiserum.";
RL Insect Biochem. 19:277-283(1989).
CC -!- FUNCTION: Has a role in inhibiting host-seeking behavior during a
CC reproductive cycle. {ECO:0000269|PubMed:11931033}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11931033}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, terminal ganglion, and
CC midgut of adults: numerous neurosecretory cells and midgut endocrine
CC cells. Expression is dynamic depending on reproductive cycle.
CC {ECO:0000269|PubMed:11931033}.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
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DR EMBL; AF155738; AAG43377.1; -; mRNA.
DR AlphaFoldDB; Q9GQV7; -.
DR VEuPathDB; VectorBase:AAEL024630; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005184; F:neuropeptide hormone activity; IMP:UniProtKB.
DR GO; GO:0032539; P:negative regulation of host-seeking behavior; IMP:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Hormone; Hydroxylation; Neuropeptide; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|Ref.3"
FT PEPTIDE 23..32
FT /note="Decapeptide 1"
FT /id="PRO_5000056383"
FT PROPEP 35..55
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000289079"
FT PEPTIDE 56..65
FT /note="Decapeptide 2"
FT /id="PRO_5000056384"
FT PROPEP 68..79
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000289080"
FT PEPTIDE 80..89
FT /note="Decapeptide 3"
FT /id="PRO_5000056385"
FT PROPEP 92..128
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000289081"
FT REGION 27..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 26
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 32
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 56
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 59
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 65
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 80
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 83
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 89
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|Ref.3"
SQ SEQUENCE 128 AA; 14605 MW; 8A5BE86B3CB99B5C CRC64;
MWKFASIVVL VVCLAWAVYC EDQRPPSLKT RFGRSADEPE SDNYVSNDIM EKRSAQRPPS
LKTRFGRSEG AEVMEKRSAQ RPPSLKTRFG RSVANPESDG YMRKRSAESE PFVTRIRHGR
ANKKRAAN
