ID B4HY15_DROSE Unreviewed; 1274 AA.
AC B4HY15;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=GM13662 {ECO:0000313|EMBL:EDW51945.1};
GN Name=Dsec\GM13662 {ECO:0000313|EMBL:EDW51945.1};
GN ORFNames=Dsec_GM13662 {ECO:0000313|EMBL:EDW51945.1};
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:EDW51945.1, ECO:0000313|Proteomes:UP000001292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25
RC {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).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; CH480818; EDW51945.1; -; Genomic_DNA.
DR RefSeq; XP_002036022.1; XM_002035986.1.
DR AlphaFoldDB; B4HY15; -.
DR SMR; B4HY15; -.
DR STRING; 7238.B4HY15; -.
DR EnsemblMetazoa; FBtr0196647; FBpp0195139; FBgn0168593.
DR HOGENOM; CLU_003950_0_0_1; -.
DR OMA; SRECLCE; -.
DR PhylomeDB; B4HY15; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 6.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 10.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR12916; CYTOCHROME C OXIDASE POLYPEPTIDE VIC-2; 1.
DR PANTHER; PTHR12916:SF4; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1-RELATED; 1.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07699; Ephrin_rec_like; 4.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF02494; HYR; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR01983; NOTCH.
DR SMART; SM00181; EGF; 12.
DR SMART; SM00179; EGF_CA; 8.
DR SMART; SM01411; Ephrin_rec_like; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 7.
DR PROSITE; PS00022; EGF_1; 9.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50825; HYR; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001292};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1170..1195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..44
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 46..82
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 84..122
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 124..160
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 162..199
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 201..237
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 239..275
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 277..313
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 554..636
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 1130..1165
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 34..43
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 72..81
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 93..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 112..121
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 150..159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 189..198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 227..236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 265..274
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 303..312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1133..1143
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1155..1164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1274 AA; 137654 MW; 9958757D7B4DB1DC CRC64;
MGSACDINID DCENRPCANE GTCVDLVDGY SCNCEPGYTG KNCQHTIDDC ASNPCQHGAT
CVDQLDGFSC KCRPGYVGLS CEAEIDECLS DPCNPVGTER CLDLDNKFEC VCRDGFKGPL
CATDIDDCEA QPCLNNGVCR DRVGGFECGC EPGWSGMRCE QQVTTCGAQA PCQNDASCID
LFQDYFCVCP SGTDGKNCET APERCIGDPC MHGGKCQDFG SGLNCSCPAD YSGIGCQYEY
DACEEHVCQN GATCVDNGAG YSCQCPPGFT GRNCEQDIVD CKDNSCPPGA SCVDLTNGFY
CQCPFNMTGD DCRKAIQVDY DLYFSDPSRS TAAQVVPFPT GEANSLTVAM WVQFAQKDDR
GIFFTLYGVQ SARMTQQRRM LLQAHSSGVQ VSLFEDQPDA FLSFGEYTSV NDGQWHHVAV
VWDGISGQLQ LITEGLIASK MEYGPGGSLP GYLWAVLGLP QPYGLSNELA YSDSGFQGTI
TKAQVWARAL DITSEIQKQV RDCRSEPVLY PGLILNWAGY EVTAGGVERN VPSLCGQRKC
PVGYTGANCQ QLVVDKEPPV VEHCPGDLWV IAKNGSAVVT WDEPHFSDNI GVTKIYERNG
HRSGTTLLWG TYDITYIASD AAGNTASCSF KVSLLTDFCP ALADPVGGSQ VCKDWGAGGQ
FKVCEIACNT GLRFSEQVPE FYTCGAEGFW RPTREPSMPL VYPSCSPSKP AQRVFRIKML
FPSDVLCNKA GQAVLRQKVT NSVNGLNRDW NFCSYAIEGT RECKDIRIDV KCDHYRGAQN
NRVRRQSKDG GVYVMEAELP VVNDPVVHTS TGERSSVKQL LEKLILEDDQ FAVQEILPNT
VPDPASLELG SEYACPVGQV VMIPDCVPCA IGTFYDSANK TCIACSRGTY QSEAGQLQCS
KCPVIAGRPG VTAGPGARSA ADCKERCPAG KYFDAETGLC RSCGHGFYQP NEGSFSCELC
GLGQTTRSTE ATSRKECRDE CSSGQQLGAD GRCEPCPRGT YRLQGVQPSC AACPLGRTTP
KVGASSVEEC TLPVCSAGTY LNATQNMCIE CRKGYYQSES QQTACLQCPP NHSTKITGAT
SKSECTNPCE HIAEGKPHCD VNAYCIMVPE TSDFKCECKP GFNGTGMVCT DVCDGFCENS
GACVKDLKGT PSCRCVGSFT GPHCAERSEF AYIAGGIAGA VIFIIIIVLL IRMICVRSTK
RRDPKKSLHG GKMSTLARSN ASLYGTKEDL YDRLKRHAYT GKKGTITSYP SIASSILKYY
LLFSEKSDSD SEVQ
//
