ID Q5R272_DROSE Unreviewed; 882 AA.
AC Q5R272;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=CG11055 {ECO:0000313|EMBL:BAD72919.1};
DE SubName: Full=GM22000 {ECO:0000313|EMBL:EDW48671.1};
GN Name=Dsec\GM22000 {ECO:0000313|EMBL:EDW48671.1};
GN ORFNames=Dsec_GM22000 {ECO:0000313|EMBL:EDW48671.1};
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|EMBL:BAD72919.1};
RN [1] {ECO:0000313|EMBL:BAD72919.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15729003; DOI=10.1266/ggs.79.351;
RA Kawahara Y., Matsuo T., Nozawa M., Shin-I T., Kohara Y., Aigaki T.;
RT "Comparative sequence analysis of a gene-dense region among closely related
RT species of Drosophila melanogaster.";
RL Genes Genet. Syst. 79:351-359(2004).
RN [2] {ECO:0000313|EMBL:EDW48671.1, ECO:0000313|Proteomes:UP000001292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c {ECO:0000313|EMBL:EDW48671.1}, 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 [3] {ECO:0000313|EMBL:EDW48671.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Rob3c {ECO:0000313|EMBL:EDW48671.1};
RG FlyBase;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AB162351; BAD72919.1; -; Genomic_DNA.
DR EMBL; CH480816; EDW48671.1; -; Genomic_DNA.
DR RefSeq; XP_002034658.1; XM_002034622.1.
DR AlphaFoldDB; Q5R272; -.
DR SMR; Q5R272; -.
DR STRING; 7238.Q5R272; -.
DR ESTHER; drose-q5r272; Hormone-sensitive_lipase_like.
DR EnsemblMetazoa; FBtr0204985; FBpp0203477; FBgn0082777.
DR GeneID; 6610042; -.
DR KEGG; dse:6610042; -.
DR HOGENOM; CLU_010288_1_0_1; -.
DR OMA; NACITHG; -.
DR OrthoDB; 2941058at2759; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR010468; HSL_N.
DR PANTHER; PTHR23025:SF3; HORMONE-SENSITIVE LIPASE; 1.
DR PANTHER; PTHR23025; TRIACYLGLYCEROL LIPASE; 1.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR Pfam; PF06350; HSL_N; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000001292}.
FT DOMAIN 51..375
FT /note="Hormone-sensitive lipase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06350"
FT DOMAIN 395..560
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 766..827
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 548..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 97443 MW; 1697EA2AC2423801 CRC64;
MIDAASAERG SPQFIALLND NLKLGHDDDG PQAVNGKDTH QYVPADLEAA YGTLYAACQD
HAAFFARDHT ELGQRLHAAH IAWQDFIVLA NRLVQQIAAF AHEYDFDEQT PGNGYRSFIY
VTNACIAHGI SICQQLTATR STIFFRKKFY MKEVEACSQL LSSLCTCLQY LLILRQWSAS
TGDLFACGNH TAEQLFELGD TINQYCFYGR CLGFQYGDSI RGVLRFLGIS MASYSESYYS
QEDDGPIVKT TRSLWTSGKY LMNPELRARR IVNISQNAKI DFCKSFWFLA ESEMMHKLPS
IVGSSIKVNR LIELPAEPLK LPRRKDFKAS ENLSSDVNQN QGDGDFVEIP VPTAHLGPGL
PVSVRLLSAK RRAGMLGEGR YRGWRKPIPP SPSILFHCHG GGFVAQSSKS HELYLRDWAV
ALDCPILSVD YSLAPEAPFP RALQEVYYAY CWLLNNTELL GTTAERIVCA GDSAGANLSI
GVALKCIEQG VRVPDGLFLA YCPTLVSFVP SPARLLCLMD PLLPFGFMMR CLRAYAAPAQ
ETLQQNAKQV EDAAQIRNAP KSNVGSLNSS RRTSMARSPL SPLEASMEPD DESSDTFASA
SASYHSQTVE RTDLPHTEGD NSSCVSFEDD SQPIVHYPIE ISADPPKDTA SAAYIDNFLD
KYLIDTATME VTEETAPEAA QAQANGHAKI SSDDDILVET GRDLVAIDTL QGRLQEAVNN
ITNTLTRCTQ SYEIHGSNVM GQQDVRNMDA LIARSPSEEF AFDVPKDPFL SPYWASDEWL
SKLPETKILT LNMDPCLDDC VMFAKKLKRL GRQVDLEILE GLPHGFLNFT MLSNEAMEGS
KKCIKSLQTL LQTDSKLKNI DKGNSMDDEE ESSSPSASLA AS
//
