ID B3MIJ5_DROAN Unreviewed; 3643 AA.
AC B3MIJ5;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Protocadherin-like wing polarity protein stan {ECO:0008006|Google:ProtNLM};
GN Name=Dana\GF13772 {ECO:0000313|EMBL:EDV38071.2};
GN Synonyms=dana_GLEANR_13779 {ECO:0000313|EMBL:EDV38071.2};
GN ORFNames=GF13772 {ECO:0000313|EMBL:EDV38071.2};
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:EDV38071.2, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV38071.2, 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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; CH902619; EDV38071.2; -; Genomic_DNA.
DR RefSeq; XP_001961249.2; XM_001961213.2.
DR STRING; 7217.B3MIJ5; -.
DR EnsemblMetazoa; FBtr0118472; FBpp0116964; FBgn0090799.
DR GeneID; 6496608; -.
DR KEGG; dan:6496608; -.
DR eggNOG; KOG4289; Eukaryota.
DR HOGENOM; CLU_000158_1_0_1; -.
DR InParanoid; B3MIJ5; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:UniProt.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:UniProt.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd15441; 7tmB2_CELSR_Adhesion_IV; 1.
DR CDD; cd11304; Cadherin_repeat; 8.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 9.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR PANTHER; PTHR24026:SF51; PROTOCADHERIN-LIKE WING POLARITY PROTEIN STAN; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..3643
FT /note="Protocadherin-like wing polarity protein stan"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006454770"
FT TRANSMEM 2814..2834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2846..2865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2885..2905
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2917..2937
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2957..2977
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2998..3020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3026..3049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 359..463
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 464..580
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 581..688
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 689..793
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 794..896
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 897..1006
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1007..1112
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1113..1219
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1481..1517
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1555..1752
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1755..1791
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1795..1962
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1964..1999
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2094..2141
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2114..2200
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2809..3050
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 2550..2680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3106..3236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3265..3308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3339..3378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3462..3643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2561..2581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2624..2646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2649..2676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3106..3161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3162..3183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3191..3206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3207..3236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3265..3280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3287..3308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3462..3477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3478..3503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3541..3558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3586..3623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3627..3643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1507..1516
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1781..1790
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1968..1978
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1989..1998
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2094..2106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2096..2113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2115..2124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3643 AA; 404640 MW; 56803A5D53375671 CRC64;
METRELPRRP LTLGLLLLLL QLCQLASGYL IVVHEDTPPG TVIFNASVYK LGSERHYKIN
AHKSANFVHH LVSVSHKDGQ IQLRKSLKCD GIYYPNLFTF YVDSTSNQLR SIDYYSLPVR
IFVSGHSCNE DRRLEQELHL HHYEEEDNTG YSKRRRRRST QEVIQLNGNQ LEEMFSRNST
EFRAGDLIFG DSFDNEMRHR ILNRKRRSLP SADPLHLQPV LHRRISDAKQ WISETYASYA
IHTTDKWNQI CLRKSQLVNS LNAFLPRSVC QHCRVSFLDV NDERFSIEHK NRDLVASRDV
CIPESMWKVS ITFSIRCDRR DIVDSDHRLK IVYHHQEFND TDIAKRVRRE LRNQSPYFEQ
ALYVASVLEE QPAGAAVTTV RARDPEDSPV VYSMVSLLDS RSQSLFKVDS RTGVVTTSAS
LDRELMDVHY FRVVATDDSF PPRSGTTTLQ VNVLDCNDHS PSFEAEQFEA SIREGATVGS
TVITLRATDQ DIGKNAEIEY GIEAVTDGGG LAQDQELPIF RIDSRSGVIS TRSSLDRETS
DSYHLLVTAA DMASAQSERR TATASVLVKV LDDNDNYPQF SERTYTVQVP EDQWGGSEDN
TVAHIRATDA DQGNNAAIRY AIIGGNTQSQ FSIDSMSGDV SLVKPLDYES VRSYRLVIRA
QDGGSPSRSN TTQLLVNVID ANDNAPRFYT SQFQESVLEN VPVGYNIIRV QAYDSDEGAN
AEITYSISER DDNFPLAVDP RTGWVQTIKP LDREEQARFA FQVVAKDGGV PPKSASSSVV
ITVQDVNDND PAFNPKYYEA NVGEDQPPGT PVTTVTATDP DEDSRLHYEI TTGNTRGRFA
ITSQNGRGLI TIAQSLDYKQ EKRFVLTVAA TDSGGRSDTA TVHINITDAN NFAPIFENAP
YSASVFEDAP VGTTVLVVSA TDSDVGVNAQ ITYSLNEESI NGLGSPDPFS INSQTGAIVT
SAPLDRETTS GYLLTVTAKD GGNPSLSDTT DVEIGVTDVN DNAPAFKSPL YQASILEDAL
VGTSVIQVAA SDPDVGLNGR IKYLLGDRDV EDGSFVIDPT SGTIRTNKGL DRESVAVYHL
TAIAVDKGSP PLSSTVEVQI RLEDVNDSPP TFPSDKITLY VPENSPVGSV VGEIHAHDPD
EGVNAVVHYS IIGGEDSNAF SLVTRPGSER AQLLTMTELD YESSRKRFEL VVRAASPPLR
NDAHIEILVT DVNDNAPVLR DFQVIFNNFR DHFPSGEIGR IPAFDADVSD KLHYRILSGN
NANLLRLNSS SGGLVLSPQL NTNVPKFATM EVSVSDGINE AKAIMQLSVR LITEDMLFNS
VTVRLNEMTE EAFLSPLLNF FLDGLAAIIP CPKENIFVFS IQDDTDVSSR ILNVSFSARR
PDVSHEEFYT PQYLQERVYL NRAILARLAT VEVLPFDDNL CVREPCLNFE ECLTVLKFGN
ASEFIHSDTV LFRPIYPVNT FACSCPEGFT GSKEHYLCDT EVDLCYSDPC QNGGSCVRRE
GGYTCVCPAT HTGSSCETEV GQLRPCPSDT CEGGLSCLSN FPSSQPPPYT ASCELRARSF
GRNSFLTFES LKQRHRFNLK LRFATVQENG LLLYNGRYNE LHDFVALEIL EGHVSFSFSL
GDHSERVSVI QDSKVSDGKW HEVEVVYLNR SVTLVLDNCD TAIALSGRLG DRWSCANRTT
LKLDKRCSLL TETCHRFLDL TGPLQVGGLP RIPAHFPVAN RDFVGCISDL RIDDRFVDLN
SYVADNGTLA GCPQKAPLCP SEPCFNGGTC REGWGTYSCE CPEGYAGNNC QDNIPAPWRF
SGDGSLSFNP LLRPIQLPWT TSFSLRTRQR EAFLLQIQIG QNSSAAVCLR QGVLYYIFDG
EPMFLAGAFL SDGEWHRVEI RWQQGSEIYF SVDYGQRTGS VPMSQKVQGL YVGKIVMGSP
DGSIGTVPEA SPFEGCMQDV RIGAGQSVLS RPTIRENVED GCESRAQCPD HCPVHSSCSS
TWDLASCECD SGYVGSECAP ICTVRPCASG VCRANVSLAR GYGCECNSSS RHGDYCEREL
QQPCPGGWWG ERVCGPCRCD LAQGYHPDCN KTTGQCYCKT NHYQPPNETA CLSCDCYSIG
SFSGACNPLT GQCECREGVI GRRCDSCSNP YAEVTLSGCE VVYDACPRSF AAGVWWPRTT
LGGVAIEGCP LPARGKGQRS CDAQTGSWSL PDMYNCTSEP FVELRRQLSQ LEKLELELNS
FVAIKMAEQL RKACETVDRR GSSKDSKAPG LGRPNRRYKM ESSFLLSNGE NVWSHELEMD
YLSDELKFSH DRLYGADLLV TEGLLQELIN YELMQSGLNL SHSQDKYFIK NLVDAASVIL
DRKYEAEWRR ATELIQRGPE DLVDAFNKYL VVLARSQHDT YTSPFEIVQP NMALGLDIVT
TESLFGYEPE QLSEYHRSKY LKPNAFTTES VILPDTSGFL QHSARQRPVI SFPKYNNYIL
DRRKFDQHTK VLIPLEMLGI TPPESDEVSQ SGRRGGSHDH RAIVAYAQYK DVGQLLPDLY
DDTITRRWGV DVELATPILS LQILVPSRDR EQETQRMEIP PRKISATSSS SSSTGSSEQQ
FVEVFDVPKA PTSSSEQQIE DIRITAHEIP PPPGNSGEQL EASSNEGEVR EPHIRLNLDD
IEFHGNSGEE SISPDSPEVL NPNYEGVSST GSDEQPKGEN EAVYRDRRLV KRQVEITYPS
DQTDQQEQVI YRSLGSPHLA QPIKLQMWLD VDAARFGPRS NPQCVRWNSF TNQWTRLGCQ
TEIPDFDGDF SPTAQQPILV NCSCTHISSY AVIVDVIDPE DIPEPSLLVQ ITSYSAFLVS
LPLLLGVLLA LALLRGQQTN SNTIHQNIVL CVFCAELLFF VGMQSRRQLL ESEFPCKLTA
ICLHYFWLAA FAWTTVDCVH LYRMLTEMRD INHGPMGFYF AMGYGAPAIV VGLSVGVRAH
EYGNSLFCWL SVYEPVVWWL VGPIAGMSVV NLLILFVSVK AAFTLKDHVL GFGNLRTLLW
LSVVSLPLMG VMWVLAVLAA SEHSQLLSLL LSGVVLLHAL FCLIGYCIIN KRVRENLQRT
CLRCMGRKVP LLDSSMVVSN SSHNVNGTTR PSNFLAGGYD TTTRRNIGIS ASSTTSRSTA
KTSSSPYSDG QLRQTSTSTS NYNSASDAPS FLRGFESSTT GRSRGGEEKP RRQRKDSDSG
SETDGRSLEL ASSHSSDDDE SRTARSSGTH RSTAVSSTPA YLPNITEHVQ ATTPPELNVV
QSPQLFPSVS KPVYAPRWSS QLPDAYLQSP PNIGRWSQDT GSDNEHVHGQ AKMTISPNPL
PNPDLTDTSY LQQHHNKINM PPSILENIRD ARDGYEDSLY GRRGEYPDKY GSYKPPSHYG
SEKDYPGGGS GSQTIGHMRS FHPDAAYLSD NIYDKQRTLG SGYLGAKSES PYLSKDRITP
DIYGSRDGHY SLKRQPAYAT DSLHSVHSLL KNDYQQQQQH LQQQQLQHQQ QQHQLQDRLS
EGSDKNGYHF PYTAEEDHLP ARKLSHTQPP SLHGSQLMQP PGLGMVNDVN NPGLLARHTL
NGGSRHSSRA NSPPSSMVAP MQPLGPLASI TDTERNIDDD ETTVXRQPQK QQQHLRLQQQ
KQKHQQQQQQ QRSKHQTQYF ATIRRKPQYR IKPEAETASK KLP
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