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ALLT_AGRIP
ID   ALLT_AGRIP              Reviewed;         135 AA.
AC   C0HKS1; C0HKS2;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Allatotropins {ECO:0000305};
DE   Contains:
DE     RecName: Full=Allatotropin-PP-1 {ECO:0000303|PubMed:29466015};
DE              Short=AT-PP-1 {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=Allatotropin {ECO:0000303|PubMed:29466015};
DE              Short=AT {ECO:0000303|PubMed:29466015};
DE   Flags: Precursor;
OS   Agrotis ipsilon (Black cutworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Noctuinae; Noctuini; Agrotis.
OX   NCBI_TaxID=56364;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-37 AND 39-51, TISSUE
RP   SPECIFICITY, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   AMIDATION AT PHE-51.
RX   PubMed=29466015; DOI=10.1021/acs.jproteome.7b00779;
RA   Diesner M., Gallot A., Binz H., Gaertner C., Vitecek S., Kahnt J.,
RA   Schachtner J., Jacquin-Joly E., Gadenne C.;
RT   "Mating-induced differential peptidomics of neuropeptides and protein
RT   hormones in Agrotis ipsilon moths.";
RL   J. Proteome Res. 17:1397-1414(2018).
CC   -!- FUNCTION: Neuropeptide stimulator of juvenile hormone synthesis.
CC       {ECO:0000250|UniProtKB:P21786}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Allatotropin: Expressed in corpora cardiaca (CC),
CC       corpora allata (CA), antennal lobe (AL) and gnathal ganglion (GNG)
CC       (protein level). Expression in AL detected in all animals, expression
CC       in GNG detected in most animals and expression in CA and CC detected in
CC       few animals (at protein level). Allatotropin-PP-1: Expressed in corpora
CC       cardiaca (CC), corpora allata (CA), antennal lobe (AL) and gnathal
CC       ganglion (GNG) (at protein level). Expression in AL detected in all
CC       animals and expression in GNG, CA and CC detected in some animals (at
CC       protein level). {ECO:0000269|PubMed:29466015}.
CC   -!- MASS SPECTROMETRY: [Allatotropin]: Mass=1486.73; Mass_error=0.01;
CC       Method=MALDI; Note=Allatotropin-PP-1.;
CC       Evidence={ECO:0000269|PubMed:29466015};
CC   -!- MASS SPECTROMETRY: [Allatotropin-PP-1]: Mass=1738.97; Mass_error=0.01;
CC       Method=MALDI; Note=Allatotropin.;
CC       Evidence={ECO:0000269|PubMed:29466015};
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DR   AlphaFoldDB; C0HKS1; -.
DR   SMR; C0HKS1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Neuropeptide; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..37
FT                   /note="Allatotropin-PP-1"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444171"
FT   PEPTIDE         39..51
FT                   /note="Allatotropin"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444172"
FT   PROPEP          55..135
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444173"
FT   MOD_RES         51
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
SQ   SEQUENCE   135 AA;  15347 MW;  CDB4A55F3101A63A CRC64;
     MNFSMHLVLA VAAAACLCVV TAAPEGRLTR TKQQRPTRGF KNVEMMTARG FGKRDRPHTR
     AELYGLDNFW EMLEAAPERE GQESTDEKTL ESIPLDWFVN EMLNNPDFAR SVVRKFIDLN
     QDGMLSSEEL LRNVA
 
 
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