GenomeNet

Database: UniProt
Entry: B3MKW8_DROAN
LinkDB: B3MKW8_DROAN
Original site: B3MKW8_DROAN 
ID   B3MKW8_DROAN            Unreviewed;      3589 AA.
AC   B3MKW8;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDV30626.1};
DE   SubName: Full=Uncharacterized protein, isoform C {ECO:0000313|EMBL:KPU72961.1};
GN   Name=Dana\GF14947 {ECO:0000313|EMBL:EDV30626.1};
GN   Synonyms=dana_GLEANR_15713 {ECO:0000313|EMBL:EDV30626.1};
GN   ORFNames=GF14947 {ECO:0000313|EMBL:EDV30626.1};
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:EDV30626.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV30626.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV30626.1}, and Tucson
RC   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).
RN   [2] {ECO:0000313|EMBL:EDV30626.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV30626.1};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
RN   [3] {ECO:0000313|EMBL:EDV30626.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV30626.1};
RG   FlyBase;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; CH902620; EDV30626.1; -; Genomic_DNA.
DR   EMBL; CH902620; KPU72961.1; -; Genomic_DNA.
DR   RefSeq; XP_001961405.1; XM_001961369.2.
DR   RefSeq; XP_014761810.1; XM_014906324.1.
DR   SMR; B3MKW8; -.
DR   STRING; 7217.B3MKW8; -.
DR   EnsemblMetazoa; FBtr0119647; FBpp0118139; FBgn0091972.
DR   EnsemblMetazoa; FBtr0386802; FBpp0346640; FBgn0091972.
DR   GeneID; 6497762; -.
DR   KEGG; dan:6497762; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   HOGENOM; CLU_000125_0_0_1; -.
DR   OMA; CMKLEIM; -.
DR   OrthoDB; 5474074at2759; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0031901; C:early endosome membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005112; F:Notch binding; IEA:EnsemblMetazoa.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProt.
DR   GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IEA:EnsemblMetazoa.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:EnsemblMetazoa.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0035152; P:regulation of tube architecture, open tracheal system; IEA:EnsemblMetazoa.
DR   GO; GO:0016360; P:sensory organ precursor cell fate determination; IEA:EnsemblMetazoa.
DR   CDD; cd00033; CCP; 3.
DR   CDD; cd00037; CLECT; 1.
DR   CDD; cd00041; CUB; 3.
DR   CDD; cd00054; EGF_CA; 12.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 5.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.10.25.10; Laminin; 17.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 3.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 4.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000859; CUB_dom.
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; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR003410; HYR_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
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; PF00431; CUB; 3.
DR   Pfam; PF00008; EGF; 9.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF07699; Ephrin_rec_like; 7.
DR   Pfam; PF00754; F5_F8_type_C; 2.
DR   Pfam; PF12661; hEGF; 3.
DR   Pfam; PF02494; HYR; 3.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF00084; Sushi; 4.
DR   SMART; SM00032; CCP; 8.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00042; CUB; 3.
DR   SMART; SM00181; EGF; 21.
DR   SMART; SM00179; EGF_CA; 15.
DR   SMART; SM01411; Ephrin_rec_like; 7.
DR   SMART; SM00231; FA58C; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00208; TNFR; 3.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 6.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 12.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 10.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01180; CUB; 3.
DR   PROSITE; PS00022; EGF_1; 15.
DR   PROSITE; PS01186; EGF_2; 12.
DR   PROSITE; PS50026; EGF_3; 16.
DR   PROSITE; PS01187; EGF_CA; 6.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS50022; FA58C_3; 2.
DR   PROSITE; PS50825; HYR; 3.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS50923; SUSHI; 5.
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   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..3589
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014298541"
FT   TRANSMEM        3447..3473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          43..168
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          210..322
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          326..438
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          439..551
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          550..611
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          612..672
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          673..733
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          734..792
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          792..830
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          829..977
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          1049..1108
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          1298..1444
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          1463..1549
FT                   /note="HYR"
FT                   /evidence="ECO:0000259|PROSITE:PS50825"
FT   DOMAIN          1550..1633
FT                   /note="HYR"
FT                   /evidence="ECO:0000259|PROSITE:PS50825"
FT   DOMAIN          2021..2057
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2059..2095
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2097..2135
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2137..2176
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2178..2214
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2216..2251
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2253..2289
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2291..2327
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2329..2367
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2369..2405
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2407..2444
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2446..2482
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2484..2520
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2522..2558
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2799..2881
FT                   /note="HYR"
FT                   /evidence="ECO:0000259|PROSITE:PS50825"
FT   DOMAIN          3407..3442
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        172..184
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        179..197
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        191..206
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        439..466
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT   DISULFID        552..595
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        675..718
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        704..731
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        1079..1106
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        2047..2056
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2085..2094
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2106..2123
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2125..2134
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2166..2175
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2204..2213
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2220..2230
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2241..2250
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2279..2288
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2317..2326
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2338..2355
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2357..2366
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2395..2404
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2434..2443
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2472..2481
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2510..2519
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2548..2557
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3410..3420
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3432..3441
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   3589 AA;  391215 MW;  6213FA6D176F68EE CRC64;
     MNQPTAANSH WLAALLSSLL FFNLLHSIGA DEAFSCPNGW ELRGLNCYKY FNIKHSWEKS
     AELCRRYGAE LVAIDSFVEN NETLSIARAS DPNQRASDKY WLGLASLDDL RTNTLESASG
     ALISQYSGYW SLNQPNADSG ECVAAGFAGK SQSWDLGTCE SLLPFMCRAQ ACPQGALHCA
     NGKCINQAFK CDGSDDCGDG TDELDCPAQC HFHMQSGGDV IETPNYPHKY SALSKCKWTL
     EGPLGSNIIL QFQDFETEKT FDTVQILVGG RTEDKSVSLA TLSGKQDLTT QPFVSASNFM
     IVKFTTDGSV ERKGFRATWK TEAKNCGGTL KATLQRQILT SSNYPKQYPG GLECLYLIKA
     QPGRIISIEV DDLDVAEGRD YLLIRDGDSP MSRTIAKLTG KTAQNERIII STGNSLYLYF
     KSSLGEAGKG FSLRYIQGCK ATITARNGTV TSPAFGLADY PKNQECYFTI RNNARAPLSL
     KFDKFTVHKS DNVQVFDGSS TSGLRLHSGN GFTGTAAPKL TLTASSGEML IKFTSDALHN
     AAGWSATFSA DCPELQPGIG ALASSRDTAF GTLVSFTCPI GQEFATGKTR LVTECLRGGN
     WSVSYIPKCQ EVYCGPVPQI DNGFSIGSSN VTYRGIAMYQ CYAGFAFASG TPIEKISCLP
     DGRWERQPNC MASQCAPLPE VAHANVTLLN GGGRSYGTIV QYVCESGYER NGHPVLTCMS
     NGTWSGDVPR CSRKRCYEFP DIDNGFVVDS TREYLFGDEA RVQCYKGYKL IGSNIMRCSE
     AQKFEQPPIC EDINECSSSQ CDLTTTECQN TNGSFHCQCR AGFTATTECR PVADLGLGNG
     GIPDDSISSS VSEQGYSKTQ LRLNTNGWCG GSSEPGANWI LIDLKAPTIL RGFRTMSVQR
     PDGNVAFSSA VRLQYTNDLT DVFKDYANPD GTAVEFRILE PTLSILNLPL PIEARYIRFR
     IQDYVGAPCI RMELMGCTRL DCVDINECSK NNGGCDQKCI NSPGGYACGC NTGYQLYTSN
     GTAGFHLERS ESGERDGDTY QRNKTCVPVM CPELDAPENG QLLSDKNDYH FGDVVRFQCH
     FGYIMSGSST ALCLSSGQWN ASVPECNYAK CVSLPDDKLE GLTVARPDPE SVLVPFRDNV
     TITCGSAGRQ LRATASSGFR QCVYDPKPGL PDYWLSGMQP SCPRVDCYAP MPTPGAEYGQ
     FVDTRFQSSF FFGCQNTFKL AGQTGRNDNV VRCGADGIWD FGDLRCEGPV CEDPGRPADG
     RQIARSYEQS SEVYFGCNRP GYILINPRPI TCIREPECKV IRPLGLSSGR IPDSAINATS
     ERPNYEAKNI RLNSATGWCG KQEAFTYVSV DLGQIYRVKA ILVKGVVTND IVGRPTEIRF
     FYKQAESENY VVYFPNFNLT MRDPGNYGEL AMITLPKYVQ ARFVILGIVS YMDNACLKFE
     LMGCEEPKHE PLLGYDYGYS PCVDNEPPIF QNCPQQPIVV RRDENGGVLP VNFTEPTAVD
     NSGSIARLEI KPQNFRTPSY VFKDTVVKYV AFDYDGNVAI CEINITVPDV TPPLLQCPQS
     YVIELVDRQE SYDVNFNDTR KRIKTSDDTG EVRLQFSPER ATIKIGNFEN VTVTATDKFN
     NRASCHFQVS LKASPCVDWE LQPPANGAIN CLPGDRGIEC IATCKPGFRF TDGEPLKTFS
     CETSRLWRPT SVVPDCVSEN TEQAAYHVTA TITYRANGAV AQSCLGQYQD VLAQHYTGLN
     QLLSQRCSAV NVNMNVTFVK SVPMLLEENV VKMDFILSIL PAVRQPQLYD LCGSTLNLIF
     DLSVPYASAV IDDLLNIANI GNQCPPLRAL KSQISRGFSC NVGEVLNMDT SDVPRCLHCP
     AGTYVSEGQN SCTYCPRGYY QNRDRQGTCV RCPAGTYTKE EGSKAQADCI PVCGYGTYSP
     TGLVPCLECP RNSFSAEPPT GGFKDCQACP AQTFTYQPAA SNRDLCRAKC APGTYSATGL
     APCSLCPLHH YQGSAGSQSC NECPSNMRTD TAGSKGREQC KAVVCGEGAC QHGGLCVPMG
     HDIQCFCPAG FSGRRCEQDI DECASQPCYN GGQCKDLPQG YRCDCQPGYS GINCQEEASD
     CENDTCPTRA MCKNEPGFKN VTCLCRSGYT GDQCDVTIDP CTANGNPCGN GASCQALQQG
     RYKCECLPGW EGIHCELNIN DCSENPCLLG ANCTDLVNDF QCACPPGFTG KRCEQKIDLC
     LSEPCKHGTC VDRLFDHECV CHPGWTGAAC DVNIDDCEIR PCANEGTCVD LVDGYSCNCE
     PGYTGKNCQH TIDDCASNPC QHGATCVDQL DGFSCKCRPG YVGLSCEAEI DECLSDPCNP
     VGTERCLDKD NKFECVCRDG FKGQLCETDI DDCEAQPCLN NGLCRDRVGG FECGCEPGWS
     GMRCEQQVTT CNLQAPCQND AHCIDLFQDY FCVCPSGTDG KNCETAPERC IGDPCMHGGK
     CQDFGSGLNC SCPADYSGIG CQYEYDACEE KVCQNGATCV DNGAGYSCQC PPGFTGRNCE
     QDIVDCKDNS CPPGASCVDL TNGFYCQCPF NMTGDDCRKA IQVDYDLYFS DPSRSTAAQV
     VPFATGEANS LTVAMWVQFA QKDDPGIFFT LYGVESARMT QRRRMLLQAH SSGVQISLFE
     DQSDAFLSFG EYTSVNDGQW HHVAVVWDGI SGQLQLITEG LIASKMEYGA GGSLPGYLWA
     VLGRPQPYGL TNELAYSDAG FQGTITKAQV WARALDITSE IQKQVRDCRS EPVLYPGLIL
     NWAGYEVTSG GVERNVPSLC GQRKCPVGYT GPNCQQLVVD KEPPVVEHCP GDLWVIAKNG
     SAMVTWDEPH FSDNIGVTKI YERNGHRSGT TLLWGSYDIT YIASDAAGNT ASCSFKVSLL
     TDFCPSLADP VGGSQVCKDW GAGGQFKVCE IACNTGLRFS EPVPEFYTCG AEGFWRPTRE
     PSMPLVYPSC SPSKPAQRVF RIKMLFPSDV LCNKAGQAVL RQKVTNSVNG LNRDWNFCSY
     AVEGTRECKD IQIDVKCDHY RAAQNNRVRR QAKDGGVYVM EAELPVVNED DDDLTLTGRQ
     GRQQTGGDTY TLEIAFPAVN DPVIHTSTGE RSSVKQLLEK LILEDDQFAV QDILPNTVPD
     PASLELGSEY ACPVGQVVMI PDCVPCAIGT FYDSANKTCI PCARGTYQSE AGQQQCSKCP
     VIAGRPGVTA GPGARSAADC KERCPAGKYF DAETGLCRSC GHGFFQSNEG AFGCELCGLG
     QTTRSTEATS RKECRDECSS GQQLGADGRC EPCPRGTYRL QGVQPSCAAC PLGRTTPKVG
     ASSVEECTLP VCSPGTYLNA TLNMCIECRK GFYQSESQQT SCLQCPPNHS TKIAGATSKS
     ECTNPCEHIA EGKPHCDVNA YCIMVPETSD FKCECKPGFN GTGMACTDMC EGFCENSGTC
     VKDLKGTPSC RCVGSFTGPH CAERSEFAYI AGGIAGAVIF IIIIVLLIWM ICVRSTKRRD
     PKKMLTPAID QTGSQVNFYY GAHTPYAESI APSHHSTYAH YYDDEEDGWE MPNFYNETYM
     KDGLHGGKMS TLARSNASLY GTKEDLYDRL KRHAYTGKKE KSDSDSEVQ
//
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