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Database: UniProt
Entry: A0A026WJK1_OOCBI
LinkDB: A0A026WJK1_OOCBI
Original site: A0A026WJK1_OOCBI 
ID   A0A026WJK1_OOCBI        Unreviewed;       135 AA.
AC   A0A026WJK1;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=LIRP {ECO:0000313|EMBL:EZA56175.1};
GN   ORFNames=X777_03507 {ECO:0000313|EMBL:EZA56175.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA56175.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA56175.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds. {ECO:0000256|ARBA:ARBA00011207}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU000406}.
CC   -!- SIMILARITY: Belongs to the insulin family.
CC       {ECO:0000256|ARBA:ARBA00009034, ECO:0000256|RuleBase:RU000406}.
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DR   EMBL; KK107168; EZA56175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026WJK1; -.
DR   STRING; 2015173.A0A026WJK1; -.
DR   EnsemblMetazoa; XM_011337675.3; XP_011335977.3; LOC105278524.
DR   OMA; MFKKSGQ; -.
DR   Proteomes; UP000053097; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   Gene3D; 1.10.100.10; Insulin-like; 1.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR040228; Insulin-relat-peptide_inver.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   PANTHER; PTHR13647:SF4; INSULIN-LIKE PEPTIDE 1-RELATED; 1.
DR   PANTHER; PTHR13647; INSULIN-LIKE PEPTIDE 2-RELATED; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; Insulin-like; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW   Secreted {ECO:0000256|RuleBase:RU000406};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..135
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001541175"
FT   DOMAIN          48..133
FT                   /note="Insulin-like"
FT                   /evidence="ECO:0000259|SMART:SM00078"
SQ   SEQUENCE   135 AA;  15075 MW;  DC59AACCC5E7BE5E CRC64;
     MYSMFANRLN VVVTLVFAIA FLVAESGNAQ VDGFPQFNTK RSSISAPQRY CGKKLSNALQ
     IVCDGVYNSM FKKSGQEMEL ADYPFPYESF PFVPPERANG MLDRTSARFR RSRGIHEECC
     VNACTISELS SYCGP
//
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