ID B3M149_DROAN Unreviewed; 791 AA.
AC B3M149;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Larval serum protein 1 beta chain {ECO:0008006|Google:ProtNLM};
GN Name=Dana\GF16081 {ECO:0000313|EMBL:EDV44319.1};
GN Synonyms=dana_GLEANR_17356 {ECO:0000313|EMBL:EDV44319.1};
GN ORFNames=GF16081 {ECO:0000313|EMBL:EDV44319.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV44319.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV44319.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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).
CC -!- SIMILARITY: Belongs to the hemocyanin family.
CC {ECO:0000256|ARBA:ARBA00038082}.
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DR EMBL; CH902617; EDV44319.1; -; Genomic_DNA.
DR RefSeq; XP_001955758.1; XM_001955722.2.
DR AlphaFoldDB; B3M149; -.
DR STRING; 7217.B3M149; -.
DR EnsemblMetazoa; FBtr0120781; FBpp0119273; FBgn0093103.
DR GeneID; 6498878; -.
DR KEGG; dan:6498878; -.
DR eggNOG; ENOG502QR98; Eukaryota.
DR HOGENOM; CLU_012213_1_0_1; -.
DR InParanoid; B3M149; -.
DR OMA; HISDYER; -.
DR OrthoDB; 5406463at2759; -.
DR PhylomeDB; B3M149; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 2.60.40.1520; Hemocyanin, C-terminal domain; 1.
DR Gene3D; 1.20.1370.10; Hemocyanin, N-terminal domain; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR013788; Hemocyanin/hexamerin.
DR InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR InterPro; IPR005203; Hemocyanin_C.
DR InterPro; IPR037020; Hemocyanin_C_sf.
DR InterPro; IPR005204; Hemocyanin_N.
DR InterPro; IPR036697; Hemocyanin_N_sf.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11511:SF5; FAT-BODY PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR11511; LARVAL STORAGE PROTEIN/PHENOLOXIDASE; 1.
DR Pfam; PF03723; Hemocyanin_C; 1.
DR Pfam; PF00372; Hemocyanin_M; 1.
DR Pfam; PF03722; Hemocyanin_N; 1.
DR PRINTS; PR00187; HAEMOCYANIN.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48050; Hemocyanin, N-terminal domain; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Storage protein {ECO:0000256|ARBA:ARBA00022761}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..791
FT /note="Larval serum protein 1 beta chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002791702"
FT DOMAIN 32..153
FT /note="Hemocyanin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03722"
FT DOMAIN 160..498
FT /note="Hemocyanin/hexamerin middle"
FT /evidence="ECO:0000259|Pfam:PF00372"
FT DOMAIN 507..757
FT /note="Hemocyanin C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03723"
SQ SEQUENCE 791 AA; 96500 MW; AC3361E1AC8A891E CRC64;
MKVAIVLLAC LGLVAATSVY KKHEVKIADK TFLEKQKFLF EIVYRLEDPL MFEDYIKMGS
SLFIEKSYYT TFDKYMEIFY DAYKVGALLP KGEFFGALVK THAKQARGLF NFFYYAKDWE
TFMHNVAWAR MHVNEGMFVY ALTLAVIHRE DFHGLMLPSI YEIFPQFFFN SKFVYEAEKF
DYEMWMKMTM YEKEYMDVYY KNHAHGYGYG NMYQSGDYMY MKDFKMWQWW KLMGLGEHWY
SEDKYILREN IYEFNQDSKW LSMMKDVKVW WMPVDYTRDL NMYNEESKLS YFTEDLGWNS
YWYYLNMDYS FFLDGTTFDL KNDRRGEWWL YNVHQLLSRY YMERLSHGFG AIPEFSWYHQ
IEMGYDPQMI YYNGIGYSYR KNYYEMETYG NFEMLDKITS FMKRIQTIVD MGYYKTMDGH
MIDLRKPESI EYIGNMMQGN VDAMDKMFFQ FWYMLAHMYF ADVDFHQMEV YPNVMLNFET
MMRDPMYYMF YKSIVQVYFQ FMHYLPKYTK EQLLMPGVSM KHVEVSELTT YFDLVDFDVT
NMLNDKMVFH DGKFVWDKSL YARQMRLNHK PFTYTYTIES DKVEKVVVRA FLGPKFDEFG
KMISLTENRM NFMEIDEFFY ELKAGTNMIK RNSNEFYWTV KDRTTYTELY YYLMMAFDGK
YDFPLDISEP HCGFPDRLVL PMGWKKGMPM QMFFMVMPYS APTHEQFSTF DYTYSCGIGS
GARFVDNMPF GYPFDREIDE YEFFVPNMYF KDVKIYHADT MEPYYKYKGY SNYGHFDYTF
FSDYYTKYFK Y
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