ID   PROH4_CAMFO             Reviewed;         201 AA.
AC   E2AX35;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=IDLSRF-like peptide {ECO:0000305|PubMed:25641051};
DE   Flags: Precursor;
GN   ORFNames=EAG_01737 {ECO:0000312|EMBL:EFN61985.1};
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 29-40, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP   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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25641051}.
CC   -!- TISSUE SPECIFICITY: Expressed in central brain, antennal and optical
CC       lobes, in gnathal, thoracic and abdominal ganglia and in the
CC       retrocerebral complex (at protein level).
CC       {ECO:0000269|PubMed:25641051}.
CC   -!- MASS SPECTROMETRY: Mass=1435.73; Method=MALDI; Note=IDLSRF-like
CC       peptide.; Evidence={ECO:0000269|PubMed:25641051};
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DR   EMBL; GL443520; EFN61985.1; -; Genomic_DNA.
DR   RefSeq; XP_011265599.1; XM_011267297.2.
DR   AlphaFoldDB; E2AX35; -.
DR   STRING; 104421.E2AX35; -.
DR   GeneID; 105256978; -.
DR   KEGG; cfo:105256978; -.
DR   InParanoid; E2AX35; -.
DR   OMA; GICISIQ; -.
DR   OrthoDB; 1489754at2759; -.
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   CDD; cd00112; LDLa; 1.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   SMART; SM00192; LDLa; 1.
DR   SUPFAM; SSF57424; SSF57424; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Neuropeptide; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         29..40
FT                   /note="IDLSRF-like peptide"
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT                   /id="PRO_0000434253"
FT   PROPEP          43..201
FT                   /evidence="ECO:0000305|PubMed:25641051"
FT                   /id="PRO_0000434254"
FT   DOMAIN          45..85
FT                   /note="LDL-receptor class A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        46..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        54..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        67..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   201 AA;  21937 MW;  55DC10F7B89BC3D5 CRC64;
     MVRRFCNGAV ALGIALTACA AFPRAIMAID LSRFYGHINT KRSDACHPYE PFKCPGDGLC
     ISIQYLCDGA PDCQDGYDED SRLCTAAKRP PVEETATFLQ SLLASHGPNY LEKLFGNKAR
     DTLKPLGGVE KVAIALSESQ TIEDFGAALH LMRSDLEHLR SVFMAVENGD LGMLKSIGIK
     DSELGDVKFF LEKLVKTGFL D