ALLA_AGRIP
ID ALLA_AGRIP Reviewed; 229 AA.
AC C0HKR2; C0HKR3; C0HKR4; C0HKR5; C0HKR6; C0HKR7; C0HKR8; C0HKR9;
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=Allatostatin-A {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Allatostatin-A-1 {ECO:0000303|PubMed:29466015};
DE Short=AST-A-1 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Allatostatin-A-3 {ECO:0000303|PubMed:29466015};
DE Short=AST-A-3 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Allatostatin-A-4 {ECO:0000303|PubMed:29466015};
DE Short=AST-A-4 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Allatostatin-A-5 {ECO:0000303|PubMed:29466015};
DE Short=AST-A-5 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Allatostatin-A-6 {ECO:0000303|PubMed:29466015};
DE Short=AST-A-6 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Allatostatin-A-7 {ECO:0000303|PubMed:29466015};
DE Short=AST-A-7 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Allatostatin-A-8 {ECO:0000303|PubMed:29466015};
DE Short=AST-A-8 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Allatostatin-A-9 {ECO:0000303|PubMed:29466015};
DE Short=AST-A-9 {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 51-58; 83-90; 133-140;
RP 155-162; 166-173; 177-184; 188-196 AND 200-210, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT LEU-58;
RP LEU-90; LEU-140; LEU-162; LEU-173; LEU-184; LEU-196 AND LEU-210.
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 inhibitors of juvenile hormone synthesis and gut
CC muscle contraction. {ECO:0000250|UniProtKB:P12764}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Allatostatin-A-1: Expressed in antennal lobe (AL),
CC corpora cardiaca (CC), corpora allata (CA) and gnathal ganglion (GNG)
CC (at protein level). Expression in AL and GNG detected in most animals,
CC in CC and CA in some animals (at protein level). Allatostatin-A-3:
CC Expressed in antennal lobe (AL), corpora cardiaca (CC), corpora allata
CC (CA) and gnathal ganglion (GNG) (at protein level). Expression in AL
CC detected in all animals, in GNG, CC and CA in most animals (at protein
CC level). Allatostatin-A-4: Expressed in antennal lobe (AL), corpora
CC cardiaca (CC), corpora allata (CA) and gnathal ganglion (GNG) in all
CC animals (at protein level). Allatostatin-A-5: Expressed in antennal
CC lobe (AL), corpora cardiaca (CC), corpora allata (CA) and gnathal
CC ganglion (GNG) in all animals (at protein level). Allatostatin-A-6:
CC Expressed in antennal lobe (AL) and gnathal ganglion (GNG) (at protein
CC level). Expression in AL detected in some animals, in GNG in few
CC animals (at protein level). Not expressed in corpora cardiaca (CC) and
CC corpora allata (CA) (at protein level). Allatostatin-A-7: Expressed in
CC antennal lobe (AL), corpora cardiaca (CC), corpora allata (CA) and
CC gnathal ganglion (GNG) (at protein level). Expression in AL detected in
CC all animals, in GNG, CC and CA in most animals (at protein level).
CC Allatostatin-A-8: Expressed in antennal lobe (AL), corpora cardiaca
CC (CC), corpora allata (CA) and gnathal ganglion (GNG) (at protein
CC level). Expression in AL detected in all animals, in GNG, CC and CA in
CC most animals (at protein level). Allatostatin-A-9: Expressed in
CC antennal lobe (AL), corpora cardiaca (CC), corpora allata (CA) and
CC gnathal ganglion (GNG) (at protein level). Expression in AL detected in
CC all animals, in GNG in most animals and in CC and CA in some animals
CC (at protein level).
CC -!- MASS SPECTROMETRY: [Allatostatin-A-1]: Mass=934.44; Mass_error=0.01;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Allatostatin-A-3]: Mass=925.51; Mass_error=0.01;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Allatostatin-A-4]: Mass=909.49; Mass_error=0.01;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Allatostatin-A-5]: Mass=911.47; Mass_error=0.01;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Allatostatin-A-6]: Mass=935.54; Mass_error=0.01;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Allatostatin-A-7]: Mass=926.48; Mass_error=0.01;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Allatostatin-A-8]: Mass=995.57; Mass_error=0.01;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Allatostatin-A-9]: Mass=1393.68; Mass_error=0.01;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:29466015};
CC -!- SIMILARITY: Belongs to the allatostatin family. {ECO:0000305}.
CC -!- CAUTION: Further mature peptides might exist. {ECO:0000305}.
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DR AlphaFoldDB; C0HKR2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR010276; Allatostatin.
DR Pfam; PF05953; Allatostatin; 9.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..48
FT /evidence="ECO:0000305"
FT /id="PRO_0000444176"
FT PEPTIDE 51..58
FT /note="Allatostatin-A-1"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444177"
FT PROPEP 62..80
FT /evidence="ECO:0000305"
FT /id="PRO_0000444178"
FT PEPTIDE 83..90
FT /note="Allatostatin-A-3"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444179"
FT PROPEP 94..130
FT /evidence="ECO:0000305"
FT /id="PRO_0000444180"
FT PEPTIDE 133..140
FT /note="Allatostatin-A-4"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444181"
FT PROPEP 144..152
FT /evidence="ECO:0000305"
FT /id="PRO_0000444182"
FT PEPTIDE 155..162
FT /note="Allatostatin-A-5"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444183"
FT PEPTIDE 166..173
FT /note="Allatostatin-A-6"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444184"
FT PEPTIDE 177..184
FT /note="Allatostatin-A-7"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444185"
FT PEPTIDE 188..196
FT /note="Allatostatin-A-8"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444186"
FT PEPTIDE 200..210
FT /note="Allatostatin-A-9"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444187"
FT PROPEP 214..229
FT /evidence="ECO:0000305"
FT /id="PRO_0000444188"
FT REGION 23..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 90
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 140
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 162
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 173
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 184
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 196
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 210
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
SQ SEQUENCE 229 AA; 25912 MW; 40FF425C3CB80716 CRC64;
MLSTSLPVCF LVIGAALCAP ERMQNDPDPH DSTAQGSDNH SDHIAPLAKR SPHYDFGLGK
RAYSYVSEYK RLPVYNFGLG KRSRPYSFGL GKRSVDEDQT NDDQQQIMNN DLDQAALAEF
FDQYDDAGYE KRARPYSFGL GKRFADDDTS EEKRARAYDF GLGKRLPLYN FGLGKRARSY
NFGLGKRLAS KFNFGLGKRE RDMHRFSFGL GKRSADDAST EDSDNYFDV
