PTSP_AGRIP
ID PTSP_AGRIP Reviewed; 251 AA.
AC C0HKW7; C0HKW8; C0HKW9; C0HKX0; C0HKX1; C0HKX2;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=Prothoracicostatic peptides {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Prothoracicostatic peptide 5 {ECO:0000303|PubMed:29466015};
DE Short=PTSP-5 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Prothoracicostatic peptide 6 {ECO:0000303|PubMed:29466015};
DE Short=PTSP-6 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Prothoracicostatic peptide 7 {ECO:0000303|PubMed:29466015};
DE Short=PTSP-7 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Prothoracicostatic peptide precursor-related peptide 2 {ECO:0000303|PubMed:29466015};
DE Short=PTSP-PP-2 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Prothoracicostatic peptide 8 {ECO:0000303|PubMed:29466015};
DE Short=PTSP-8 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Prothoracicostatic peptide precursor-related peptide 3 {ECO:0000303|PubMed:29466015};
DE Short=PTSP-PP-3 {ECO:0000303|PubMed:29466015};
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 190-198; 202-215; 218-228
RP AND 232-251, TISSUE SPECIFICITY, MASS SPECTROMETRY, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND AMIDATION AT TRP-89; TRP-152; TRP-198 AND TRP-228.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Prothoracicostatic peptide 5: Expressed in antennal
CC lobe (AL), corpora cardiaca (CC), corpora allata (CA) and gnathal
CC ganglion (GNG) (at protein level). Expression in AL detected in all
CC animals, in CC, CA and GNG in most (at protein level).
CC Prothoracicostatic peptide 6: Expressed in antennal lobe (AL), corpora
CC cardiaca (CC), corpora allata (CA) and gnathal ganglion (GNG) (at
CC protein level). Expression in AL detected in all animals, expression in
CC GNG in most animals, in CA and CC detected in some animals (at protein
CC level). Prothoracicostatic peptide 7: Expressed in antennal lobe (AL),
CC corpora cardiaca (CC), corpora allata (CA) and gnathal ganglion (GNG)
CC (at protein level). Expression in AL, CA and CC detected in most
CC animals, expression in GNG in some animals (at protein level).
CC Prothoracicostatic peptide precursor-related peptide 2: Expressed in
CC antennal lobe (AL), corpora cardiaca (CC) and corpora allata (CA) with
CC expression detected in few animals (at protein level). Not expressed in
CC gnathal ganglion (GNG) (at protein level). Prothoracicostatic peptide
CC 8: Expressed in antennal lobe (AL), corpora cardiaca (CC), corpora
CC allata (CA) and gnathal ganglion (GNG) (at protein level). Expression
CC in AL detected in all animals, expression in GNG in most animals, in CA
CC and CC detected in some animals (at protein level). Prothoracicostatic
CC peptide precursor-related peptide 3: Expressed in antennal lobe (AL) in
CC few animals (at protein level). Not expressed in corpora cardiaca (CC),
CC corpora allata (CA) and gnathal ganglion (GNG) (at protein level).
CC {ECO:0000269|PubMed:29466015}.
CC -!- MASS SPECTROMETRY: [Prothoracicostatic peptide 5]: Mass=1262.58;
CC Method=MALDI; Note=Prothoracicostatic peptide 5.;
CC Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Prothoracicostatic peptide 6]: Mass=1414.66;
CC Method=MALDI; Note=Prothoracicostatic peptide 6.;
CC Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Prothoracicostatic peptide 7]: Mass=997.47;
CC Method=MALDI; Note=Prothoracicostatic peptide 7.;
CC Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Prothoracicostatic peptide precursor-related
CC peptide 2]: Mass=1690.78; Method=MALDI; Note=Prothoracicostatic
CC peptide-PP 2.; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Prothoracicostatic peptide 8]: Mass=1359.67;
CC Method=MALDI; Note=Prothoracicostatic peptide 8.;
CC Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Prothoracicostatic peptide precursor-related
CC peptide 3]: Mass=2072.80; Method=MALDI; Note=Prothoracicostatic
CC peptide-PP 3.; Evidence={ECO:0000269|PubMed:29466015};
CC -!- CAUTION: Further mature peptides might exist. {ECO:0000305}.
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DR AlphaFoldDB; C0HKW7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Secreted.
FT PROPEP 1..77
FT /evidence="ECO:0000305"
FT /id="PRO_0000444265"
FT PEPTIDE 80..89
FT /note="Prothoracicostatic peptide 5"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444266"
FT PROPEP 93..138
FT /evidence="ECO:0000305"
FT /id="PRO_0000444267"
FT PEPTIDE 141..152
FT /note="Prothoracicostatic peptide 6"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444268"
FT PROPEP 156..187
FT /evidence="ECO:0000305"
FT /id="PRO_0000444269"
FT PEPTIDE 190..198
FT /note="Prothoracicostatic peptide 7"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444270"
FT PEPTIDE 202..215
FT /note="Prothoracicostatic peptide precursor-related peptide
FT 2"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444271"
FT PEPTIDE 218..228
FT /note="Prothoracicostatic peptide 8"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444272"
FT PEPTIDE 232..251
FT /note="Prothoracicostatic peptide precursor-related peptide
FT 3"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444273"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 152
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 198
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 228
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:29466015"
SQ SEQUENCE 251 AA; 28633 MW; F9B2C38ABD9AF02B CRC64;
MRKSARGQVC TEAGAGASGD WQDMSSAWGK RAWQDLNSAW GKRGWNDMSS AWGKRAWQDL
NSAWGKRGWQ DLNSAWGKRA WRDMSQSPWG KRGWNDMSSA WGKRGWNDMS SAWGKRGWND
MSSAWGKRGW NDMSSAWGKR GPEKWANFHG SWGKRAAEPD YEEIDAAIEQ LIPIQQLSDN
ERMEVPEKKA WSALHGAWGK RPVKQAQYNS GSYYWKREPA WTNLRGMWGK RSAPDADAVD
DDHESSARDE A