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Database: UniProt
Entry: B4J1Y6_DROGR
LinkDB: B4J1Y6_DROGR
Original site: B4J1Y6_DROGR 
ID   B4J1Y6_DROGR            Unreviewed;      1050 AA.
AC   B4J1Y6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=GH15511 {ECO:0000313|EMBL:EDV95911.1};
GN   Name=Dgri\GH15511 {ECO:0000313|EMBL:EDV95911.1};
GN   ORFNames=Dgri_GH15511 {ECO:0000313|EMBL:EDV95911.1};
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070};
RN   [1] {ECO:0000313|EMBL:EDV95911.1, ECO:0000313|Proteomes:UP000001070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070};
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; CH916366; EDV95911.1; -; Genomic_DNA.
DR   RefSeq; XP_001983563.1; XM_001983527.1.
DR   AlphaFoldDB; B4J1Y6; -.
DR   SMR; B4J1Y6; -.
DR   STRING; 7222.B4J1Y6; -.
DR   eggNOG; KOG1218; Eukaryota.
DR   HOGENOM; CLU_008281_2_0_1; -.
DR   InParanoid; B4J1Y6; -.
DR   OMA; PACNINC; -.
DR   PhylomeDB; B4J1Y6; -.
DR   Proteomes; UP000001070; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   Gene3D; 2.10.25.140; -; 1.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 5.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR011489; EMI_domain.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR042635; MEGF10/SREC1/2-like.
DR   PANTHER; PTHR24043:SF8; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR   Pfam; PF12661; hEGF; 5.
DR   Pfam; PF00053; Laminin_EGF; 4.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 15.
DR   SMART; SM00180; EGF_Lam; 12.
DR   PROSITE; PS00022; EGF_1; 11.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS51041; EMI; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001070};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1050
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002811477"
FT   TRANSMEM        804..825
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..105
FT                   /note="EMI"
FT                   /evidence="ECO:0000259|PROSITE:PS51041"
FT   DOMAIN          185..220
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          228..263
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          271..306
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          402..437
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          488..523
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          664..699
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          997..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1050
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        210..219
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        253..262
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        296..305
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        427..436
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        513..522
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        689..698
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1050 AA;  115219 MW;  7486BDE05ECC42DD CRC64;
     MLRLSWIGLG LLALLANAQD EITAIEGPEG PNVCKKRENY NVEVVITELQ SFQERGSTWC
     LSIPPSCPTY RIRHRVVNKT QSLTKARIVR DCCDGYVRSG SECIPHCSEA CQHGRCIAPE
     KCKCTEGYGG PACNINCSPG LYGIDCKLKC DCLNNASCEP FTGECECAKG YAGERCAEIC
     PPGQYGEKCA ELCRCENGGS CDHISGKCSC APGYTGPLCD MRCPDGKHGA QCEEDCRCQN
     DGKCDPHNGA CECTAGWTGD VCANKCPTGS HGLNCELSCE CYNDAPCHHI TGRCECPPGY
     MGEVCMDECP LNTYGRNCTE RCHCENDAAC SPTGKCECAL GWRGERCEER ICEPNKYGAD
     CSKTCECDME HTDRCQPETG RCDCSIGWSS AQCTRPCAFL KYGLNCEQNC DCRNGAKCSP
     TNGTCICAPG FQGDKCEQSC PTGTYGQGCA FQCDCENGAK CAPETGQCLC APGWRNNKCD
     RSCDLNMYGD GCRHICECEN NASCNPINGN CTCAAGWTGK RCSQKCEPNS FGNDCSQQCQ
     CDKYNTIACE ATTGRCICKQ GWRGVHCETN CPSGYYGENC DKVCRCLNNS SCDSESGDCI
     CAPGWTGEDC SEPCSDGFYG MECKERCPES LHGNATCDHI TGEVLCRPGY LGRTCEHACK
     PGMYGPNCQL KCSCEHAGEC NHENGHCICL PGWTGANCNQ SCPQDTYGQG CTQRCRCQHH
     RTCRKNDGHC ICLPGWMGDQ CNYICPEGFY GEYCMNPCAC PSSNFQCHAA EGCVCRSGYT
     GANCDELIAM QRIAEHVESN NASVAWSMAL LTLCAAIICA VFLYYRRRVS NLKTEIAHVH
     YTHDTNGTTA WPPANHNFDN PVYGMQAETR LLSNHLRPKM NNFNQNGSVC TEYGDDSNAS
     SRVGSYSINY NHELLNKNMN ADLTNPNVYN AIGDPLKEEH VYDEIKQKEG YKDPVKIYSK
     ILFPEDEYDH LDYSRPSTSQ KPHYHRMNDT MLNINHDEEK PSNVKNSMTV LLDKKPAPPT
     EPEPQHESFD NTNLDNASTV SPSSSPELRK
//
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