PPK_CAMFO
ID PPK_CAMFO Reviewed; 177 AA.
AC E2AFK9;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=PBAN-type neuropeptides {ECO:0000312|EMBL:EFN67760.1};
DE Contains:
DE RecName: Full=Pyrokinin 1 {ECO:0000303|PubMed:25641051};
DE Short=Pk 1 {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Pyrokinin 2 {ECO:0000303|PubMed:25641051};
DE Short=Pk 2 {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Pyrokinin 3 {ECO:0000303|PubMed:25641051};
DE Short=Pk 3 {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Pyrokinin 4 {ECO:0000303|PubMed:25641051};
DE Short=Pk 4 {ECO:0000303|PubMed:25641051};
DE Flags: Precursor;
GN ORFNames=EAG_02707 {ECO:0000312|EMBL:EFN67760.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 56-74; 116-124; 127-154 AND 158-166, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP AMIDATION AT LEU-74; LEU-124; LEU-154 AND LEU-166.
RX PubMed=25641051; DOI=10.1021/pr5011636;
RA Schmitt F., Vanselow J.T., Schlosser A., Kahnt J., Roessler W., Wegener C.;
RT "Neuropeptidomics of the carpenter ant Camponotus floridanus.";
RL J. Proteome Res. 14:1504-1514(2015).
CC -!- FUNCTION: Pyrokinins mediate visceral muscle contractile activity
CC (myotropic activity). {ECO:0000250|UniProtKB:P82617}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25641051}.
CC -!- TISSUE SPECIFICITY: Pyrokinins (PK) 1 to 4 are expressed in the
CC retrocerebral complex. PK 1 is expressed in central brain, anntennal
CC lobes and abominal ganglia. PK 2 is expressed in optical lobes and in
CC gnathal, thoracic and abdominal ganglia. PK 3 is expressed in optical
CC lobes and in thoracic and abdominal ganglia (at protein level).
CC {ECO:0000269|PubMed:25641051}.
CC -!- MASS SPECTROMETRY: [Pyrokinin 1]: Mass=2069.98; Method=Electrospray;
CC Note=Pyrokinin 1.; Evidence={ECO:0000269|PubMed:25641051};
CC -!- MASS SPECTROMETRY: [Pyrokinin 2]: Mass=1069.57; Method=Electrospray;
CC Note=Pyrokinin 2.; Evidence={ECO:0000269|PubMed:25641051};
CC -!- MASS SPECTROMETRY: [Pyrokinin 3]: Mass=3275.55; Method=Electrospray;
CC Note=Pyrokinin 3.; Evidence={ECO:0000269|PubMed:25641051};
CC -!- MASS SPECTROMETRY: [Pyrokinin 4]: Mass=1065.64; Method=Electrospray;
CC Note=Pyrokinin 4.; Evidence={ECO:0000269|PubMed:25641051};
CC -!- MISCELLANEOUS: The structural similarity of PK1 and PK2 to CAPA-PK
CC might compensate for the apparent absence of CAPA-PK in ants.
CC {ECO:0000303|PubMed:25641051}.
CC -!- SIMILARITY: Belongs to the pyrokinin family. {ECO:0000305}.
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DR EMBL; GL439118; EFN67760.1; -; Genomic_DNA.
DR RefSeq; XP_011257226.1; XM_011258924.2.
DR AlphaFoldDB; E2AFK9; -.
DR STRING; 104421.E2AFK9; -.
DR GeneID; 105251860; -.
DR KEGG; cfo:105251860; -.
DR InParanoid; E2AFK9; -.
DR OMA; ITSGMWF; -.
DR OrthoDB; 1434163at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR PROSITE; PS00539; PYROKININ; 3.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..54
FT /evidence="ECO:0000305|PubMed:25641051"
FT /id="PRO_0000434243"
FT PEPTIDE 56..74
FT /note="Pyrokinin 1"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434244"
FT PROPEP 78..113
FT /evidence="ECO:0000305|PubMed:25641051"
FT /id="PRO_0000434245"
FT PEPTIDE 116..124
FT /note="Pyrokinin 2"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434246"
FT PEPTIDE 127..154
FT /note="Pyrokinin 3"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434247"
FT PEPTIDE 158..166
FT /note="Pyrokinin 4"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434248"
FT PROPEP 169..177
FT /evidence="ECO:0000305|PubMed:25641051"
FT /id="PRO_0000434249"
FT REGION 28..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:25641051"
FT MOD_RES 124
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:25641051"
FT MOD_RES 154
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:25641051"
FT MOD_RES 166
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:25641051"
SQ SEQUENCE 177 AA; 19760 MW; EE2EC6F9D920109F CRC64;
MIVTGNPVCA IALLLCLVFR ASGEYELEMS SGGSNDGRSP SNDFGSCTDG KCTKRTTTTQ
ESGISSGMWF GPRLGKRHKS NEKQQINPEI EMLVNALDQP GMRWTVITIP ANEKRQPTQF
TPRLGRGSEE KFIYSDATDR NEIDEDDPLF TPRLGRRVPW IPSPRLGRQS RSVSRKI
