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