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SNPF_AEDAE
ID   SNPF_AEDAE              Reviewed;         215 AA.
AC   A0SIX6; Q16LS3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Short neuropeptide F;
DE   Contains:
DE     RecName: Full=sNPF-associated peptide;
DE   Contains:
DE     RecName: Full=sNPF peptide 2;
DE   Contains:
DE     RecName: Full=sNPF peptide 3;
DE   Contains:
DE     RecName: Full=RLRF peptide 1;
DE   Contains:
DE     RecName: Full=RLRF peptide 2;
DE   Contains:
DE     RecName: Full=RLRF peptide 3;
DE   Contains:
DE     RecName: Full=RLRW peptide;
DE   Flags: Precursor;
GN   Name=sNPF {ECO:0000250|UniProtKB:Q9VIQ0}; ORFNames=AAEL012542;
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:ABE72968.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC   TISSUE=Head {ECO:0000312|EMBL:ABE72968.1};
RX   PubMed=17140700; DOI=10.1016/j.peptides.2006.09.019;
RA   Garczynski S.F., Crim J.W., Brown M.R.;
RT   "Characterization and expression of the short neuropeptide F receptor in
RT   the African malaria mosquito, Anopheles gambiae.";
RL   Peptides 28:109-118(2007).
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).
CC   -!- FUNCTION: Plays a role in controlling food intake and regulating body
CC       size. {ECO:0000250|UniProtKB:Q9VIQ0}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A {ECO:0000269|PubMed:17140700};
CC         IsoId=A0SIX6-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=A0SIX6-2; Sequence=VSP_052376;
CC   -!- SIMILARITY: Belongs to the NPY family. {ECO:0000255}.
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DR   EMBL; DQ459411; ABE72968.1; -; mRNA.
DR   EMBL; CH477894; EAT35275.1; -; Genomic_DNA.
DR   RefSeq; XP_001662646.1; XM_001662596.1.
DR   AlphaFoldDB; A0SIX6; -.
DR   STRING; 7159.AAEL012542-PA; -.
DR   VEuPathDB; VectorBase:AAEL019691; -.
DR   eggNOG; ENOG502SEMZ; Eukaryota.
DR   HOGENOM; CLU_1171457_0_0_1; -.
DR   InParanoid; A0SIX6; -.
DR   OMA; YADHQIK; -.
DR   Proteomes; UP000008820; Chromosome 2.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
DR   GO; GO:0032095; P:regulation of response to food; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW   Neuropeptide; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..56
FT                   /evidence="ECO:0000250|UniProtKB:Q9VIQ0"
FT                   /id="PRO_0000284734"
FT   PEPTIDE         59..69
FT                   /note="RLRF peptide 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VIQ0"
FT                   /id="PRO_0000284735"
FT   PEPTIDE         73..89
FT                   /note="sNPF-associated peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VIQ0"
FT                   /id="PRO_0000284736"
FT   PEPTIDE         91..101
FT                   /note="RLRF peptide 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VIQ0"
FT                   /id="PRO_0000284737"
FT   PEPTIDE         104..119
FT                   /note="sNPF peptide 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VIQ0"
FT                   /id="PRO_0000284738"
FT   PEPTIDE         122..129
FT                   /note="RLRW peptide"
FT                   /evidence="ECO:0000250|UniProtKB:A0SIF1"
FT                   /id="PRO_0000284739"
FT   PEPTIDE         132..145
FT                   /note="sNPF peptide 3"
FT                   /evidence="ECO:0000250|UniProtKB:A0SIF1"
FT                   /id="PRO_0000284740"
FT   PEPTIDE         147..157
FT                   /note="RLRF peptide 3"
FT                   /evidence="ECO:0000250|UniProtKB:A0SIF1"
FT                   /id="PRO_0000284741"
FT   PROPEP          160..215
FT                   /evidence="ECO:0000250|UniProtKB:A0SIF1"
FT                   /id="PRO_0000284742"
FT   REGION          173..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         69
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         101
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         129
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         157
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         201..215
FT                   /note="QVESEENSPSNMDEK -> SAQCVSSSEAQR (in isoform B)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_052376"
FT   CONFLICT        14
FT                   /note="V -> A (in Ref. 1; ABE72968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="V -> M (in Ref. 1; ABE72968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="P -> T (in Ref. 1; ABE72968)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   215 AA;  24637 MW;  1A0236899C40B0A8 CRC64;
     MCRINFTTLS LILVLWSGSL MSEPSQNADG SIKGLYEYLL QREYAAPVSY ADHQIKRKAV
     RSPSLRLRFG RRSDPSVPVE PEDDDMVDQR SIRAPQLRLR FGRTDPLWSS FNENALLEEK
     RAPSQRLRWG RSGGGMFSTN DVMQQKAIRA PQLRLRFGRS DPSWAMFNEH QLDEQQFADA
     TRQPSKTLRG DEPTSIESTE QVESEENSPS NMDEK
 
 
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