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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
 
 
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