ID B3MLY2_DROAN Unreviewed; 772 AA.
AC B3MLY2;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Larval serum protein 1 gamma chain {ECO:0008006|Google:ProtNLM};
GN Name=Dana\GF14363 {ECO:0000313|EMBL:EDV31810.1};
GN Synonyms=dana_GLEANR_15125 {ECO:0000313|EMBL:EDV31810.1};
GN ORFNames=GF14363 {ECO:0000313|EMBL:EDV31810.1};
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:EDV31810.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV31810.1, 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; CH902620; EDV31810.1; -; Genomic_DNA.
DR RefSeq; XP_001962589.1; XM_001962553.2.
DR AlphaFoldDB; B3MLY2; -.
DR SMR; B3MLY2; -.
DR STRING; 7217.B3MLY2; -.
DR EnsemblMetazoa; FBtr0119063; FBpp0117555; FBgn0091390.
DR GeneID; 6497190; -.
DR KEGG; dan:6497190; -.
DR eggNOG; ENOG502QR98; Eukaryota.
DR HOGENOM; CLU_012213_1_0_1; -.
DR InParanoid; B3MLY2; -.
DR OMA; EWIKMGQ; -.
DR OrthoDB; 5406463at2759; -.
DR PhylomeDB; B3MLY2; -.
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..772
FT /note="Larval serum protein 1 gamma chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002790932"
FT DOMAIN 31..153
FT /note="Hemocyanin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03722"
FT DOMAIN 159..490
FT /note="Hemocyanin/hexamerin middle"
FT /evidence="ECO:0000259|Pfam:PF00372"
FT DOMAIN 499..748
FT /note="Hemocyanin C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03723"
SQ SEQUENCE 772 AA; 93514 MW; 9EF91A77BAA99B83 CRC64;
MKLTLVLLAL VGCVAAFSVP TPKVKIADKN FLEKQKFLLE ITYRIEDPLM FEEWIKFGTK
FIYDKSFYSE YDYYMEKFYE SYKLGALLPK GEFFGALVKT HMKQAYGLFN FFYYAKDWET
FVSNVAWARI HVNEGMFIYA LTLAVIHKPE FQGLILPQIY EIFPQYFFNS KFVYEAEKFD
YEVFSKLTMY EKEYKDILYK DYSKFTGNFY FYTKDWKTFQ WYKMMGLDQE WYVEDKYFLR
ENYASFVNDP KYADVMKGLK SFYYPVDYTR DIEFFNDQSK LSYFTEDLGW NAYWYYLNMD
YAFFLDGKKF GLDKDRRGEW WIYNVQQILA RYYQERLANG FGEIPEFFWY KQIEYGYDPQ
LIYYNGVGYS YRKNYYDFYT YGNFEMFSKI QNFFGKVYKF LETGYYKTAD GQVIDFHKPE
SVKFIGNYLQ GNADTYDKYF FNFYYMYSHM YFADVDYNDM DVFPNVFLNY ETMLRDPFFY
TFYKKFTDVF YQFKYFLGPY TQKDLFYEGV TIKDVTVSKL VTYYDIVDFD VTNLLNDKMT
FVDGQFVWDK ALLARQARLN HKPFEFEFTI ESTQAQKGVV RVFLGPKFDE YGQVIPLNYN
RKNFVQIDSF VYPFVAGVNT FKRSSKEFSW TSEDRITYTE LYKYVMLASE GKYDFPLDIS
EPHNAFPDRL VLPKGWEQGM PMQFYYFVSP YAEEYEQFST FDYTYASGVG SGTRFVDSKP
FGYPFDRQID EYDFFVPNGF FQDVKIYYVD TFAKYFEKKY PKFGTFDYSI EY
//
