PTTH_CAMFO
ID PTTH_CAMFO Reviewed; 180 AA.
AC E1ZVK1;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Prothoracicotropic hormone {ECO:0000303|PubMed:25641051};
DE Short=PTTH {ECO:0000303|PubMed:25641051};
DE Flags: Precursor;
GN ORFNames=EAG_10178 {ECO:0000312|EMBL:EFN74770.1};
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 67-81, AND IDENTIFICATION BY MASS SPECTROMETRY.
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: PTTH is a brain secretory polypeptide of insects which
CC stimulates the prothoracic glands to produce and release ecdysone, the
CC steroid essential to insect development.
CC {ECO:0000250|UniProtKB:P17219}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P17219}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25641051}.
CC -!- CAUTION: It is unclear whether the detected peptide spanning residues
CC 67-81 is active on its own or just constitutes the N-terminus of the
CC predicted sequence of prothoracicotropic hormone.
CC {ECO:0000305|PubMed:25641051}.
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DR EMBL; GL434548; EFN74770.1; -; Genomic_DNA.
DR RefSeq; XP_011250847.2; XM_011252545.2.
DR AlphaFoldDB; E1ZVK1; -.
DR GeneID; 105248016; -.
DR KEGG; cfo:105248016; -.
DR InParanoid; E1ZVK1; -.
DR OMA; FNSCRLL; -.
DR OrthoDB; 1231726at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR SUPFAM; SSF57501; SSF57501; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hormone; Neuropeptide; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..64
FT /evidence="ECO:0000305|PubMed:25641051"
FT /id="PRO_0000434255"
FT PEPTIDE 67..180
FT /note="Prothoracicotropic hormone"
FT /evidence="ECO:0000303|PubMed:25641051"
FT /id="PRO_0000434256"
FT DISULFID 86
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P17219"
FT DISULFID 88..123
FT /evidence="ECO:0000250|UniProtKB:P17219"
FT DISULFID 111..175
FT /evidence="ECO:0000250|UniProtKB:P17219"
SQ SEQUENCE 180 AA; 20616 MW; EFBAD6CBE65298CD CRC64;
MKLLILCVMV HGLLAEGPGQ VLWKEQVVAP EFLLDDREDI ASNRNAFFYE DKRSFRPEGL
GEQVKRIAGA EDVGLQPRLV TRSLQCTCET EYEYRNLGEG HYPRYLTTSH CKPKACQNKF
NSCRLLYYKV HILSQRDLNG LSDDRYSDDS ETETPLPEAL RHKWQLKPMK IPVACVPATG