GenomeNet

Database: UniProt
Entry: B4HLB0_DROSE
LinkDB: B4HLB0_DROSE
Original site: B4HLB0_DROSE 
ID   B4HLB0_DROSE            Unreviewed;       137 AA.
AC   B4HLB0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=GM25186 {ECO:0000313|EMBL:EDW40929.1};
DE   SubName: Full=Preproinsulin-like peptide 2 {ECO:0000313|EMBL:ARM20269.1};
GN   Name=Dsec\GM25186 {ECO:0000313|EMBL:EDW40929.1};
GN   Synonyms=ILP2 {ECO:0000313|EMBL:ARM20269.1};
GN   ORFNames=Dsec_GM25186 {ECO:0000313|EMBL:EDW40929.1};
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN   [1] {ECO:0000313|EMBL:EDW40929.1, ECO:0000313|Proteomes:UP000001292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c {ECO:0000313|EMBL:EDW40929.1}, and Rob3c / Tucson
RC   14021-0248.25 {ECO:0000313|Proteomes:UP000001292};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [2] {ECO:0000313|EMBL:EDW40929.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Rob3c {ECO:0000313|EMBL:EDW40929.1};
RG   FlyBase;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ARM20269.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Park I., Park J.;
RT   "BCMB452 Independent Research.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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; KY711381; ARM20269.1; -; mRNA.
DR   EMBL; CH480815; EDW40929.1; -; Genomic_DNA.
DR   RefSeq; XP_002029943.1; XM_002029907.1.
DR   AlphaFoldDB; B4HLB0; -.
DR   STRING; 7238.B4HLB0; -.
DR   EnsemblMetazoa; FBtr0208171; FBpp0206663; FBgn0180046.
DR   GeneID; 6605102; -.
DR   KEGG; dse:6605102; -.
DR   HOGENOM; CLU_125164_0_1_1; -.
DR   OMA; CKEFNSV; -.
DR   OrthoDB; 3564703at2759; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:EnsemblMetazoa.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0005158; F:insulin receptor binding; IEA:EnsemblMetazoa.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEA:EnsemblMetazoa.
DR   GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR   GO; GO:0060180; P:female mating behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IEA:EnsemblMetazoa.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0030536; P:larval feeding behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0045475; P:locomotor rhythm; IEA:EnsemblMetazoa.
DR   GO; GO:0061964; P:negative regulation of entry into reproductive diapause; IEA:EnsemblMetazoa.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IEA:EnsemblMetazoa.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:EnsemblMetazoa.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:EnsemblMetazoa.
DR   GO; GO:0045793; P:positive regulation of cell size; IEA:EnsemblMetazoa.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:EnsemblMetazoa.
DR   GO; GO:0046622; P:positive regulation of organ growth; IEA:EnsemblMetazoa.
DR   GO; GO:0040009; P:regulation of growth rate; IEA:EnsemblMetazoa.
DR   GO; GO:1990928; P:response to amino acid starvation; IEA:EnsemblMetazoa.
DR   GO; GO:0032094; P:response to food; IEA:EnsemblMetazoa.
DR   GO; GO:0030431; P:sleep; IEA:EnsemblMetazoa.
DR   GO; GO:0070328; P:triglyceride homeostasis; IEA:EnsemblMetazoa.
DR   CDD; cd04366; IlGF_insulin_bombyxin_like; 1.
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; INSULIN-LIKE PEPTIDE 2-RELATED; 1.
DR   PANTHER; PTHR13647:SF6; 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   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001292};
KW   Secreted {ECO:0000256|RuleBase:RU000406};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..137
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014298672"
FT   DOMAIN          26..132
FT                   /note="Insulin-like"
FT                   /evidence="ECO:0000259|SMART:SM00078"
SQ   SEQUENCE   137 AA;  15240 MW;  FD0BAAA5CBB156CD CRC64;
     MSKPVSFISM VAVILLASST VKLAQGTLCS EKLNEVLSMV CEEYNPVIPH KRAMPGADSD
     LDPLNPLQFV QEFEEEDNSI SEPLRSALFP GSYLGGVLSS LAEVRRRTRQ RQGIVERCCK
     KSCDMKALRE YCSVVRN
//
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