GenomeNet

Database: UniProt
Entry: B4LSV4_DROVI
LinkDB: B4LSV4_DROVI
Original site: B4LSV4_DROVI 
ID   B4LSV4_DROVI            Unreviewed;      3129 AA.
AC   B4LSV4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=Uncharacterized protein, isoform B {ECO:0000313|EMBL:EDW64865.2};
GN   Name=Dvir\GJ20220 {ECO:0000313|EMBL:EDW64865.2};
GN   ORFNames=Dvir_GJ20220 {ECO:0000313|EMBL:EDW64865.2};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW64865.2, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:EDW64865.2, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
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   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC       {ECO:0000256|RuleBase:RU004357}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU003318};
CC       Single-pass type I membrane protein {ECO:0000256|RuleBase:RU003318}.
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; CH940649; EDW64865.2; -; Genomic_DNA.
DR   RefSeq; XP_002052710.2; XM_002052674.2.
DR   SMR; B4LSV4; -.
DR   EnsemblMetazoa; FBtr0437602; FBpp0394416; FBgn0207360.
DR   eggNOG; KOG3594; Eukaryota.
DR   HOGENOM; CLU_000347_1_0_1; -.
DR   Proteomes; UP000008792; 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:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
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   CDD; cd11304; Cadherin_repeat; 15.
DR   CDD; cd00053; EGF; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00110; LamG; 2.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.60.40.60; Cadherins; 17.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF422; NEURAL-CADHERIN 2-RELATED; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 14.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 16.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF49313; Cadherin-like; 18.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00232; CADHERIN_1; 6.
DR   PROSITE; PS50268; CADHERIN_2; 16.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00043}; Cell adhesion {ECO:0000256|RuleBase:RU003318};
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003318};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2947..2970
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          212..337
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          464..575
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          578..683
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          684..788
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          790..890
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          891..1000
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1002..1110
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1111..1215
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1225..1331
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1331..1446
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1447..1546
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1547..1662
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1663..1774
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1788..1893
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1894..1998
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1998..2117
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          2374..2410
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2411..2617
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2620..2660
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2663..2854
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2897..2935
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        2400..2409
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2650..2659
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2906..2923
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2925..2934
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   3129 AA;  349919 MW;  A5F2B483FC56BC74 CRC64;
     MAARRCPLAP PMRGLQPQRQ RMTSIPLPAT RCITHMLLLS MLLLHLSNIG LATATGEQQA
     ASYAGLSAEN AARMLAGSPG EAEANAQHGG NGHSEMSLVL PHDTYPGFSI KKFKTRPLQQ
     PNGTAAHHRG AGGAGAAAYH MLDSDYSKYF TVLDDGVVMT TADISPLVNR PVQLVVVEQT
     PNATNTHNLQ LFVMHRKDML RFSGSLLDAS GEVRENHPAG TRVRGVPLMQ AFSGSILDEE
     LAQPKKVRYT IIDGNVDDAF ALQERRANQN VQLNAKSLVI EGDDESGVWL VTNRPLDREE
     RSHYDLSVEA SDVDGLDKTV SKIQITVLDE NDNRPVFKSQ DYKFAIAGKK SLNSDSNNSV
     SWQRFAILGR VEATDADGDK IAYRLKSPSN VVIIVPQTGE LMLAGEPTTN ELLLEVIAHD
     LRYPSLLSAQ PAKVLLEFLA PEPVSFIMQH LEHDAVNEHS HHREKRRVTR AVRPTKRIEF
     TEADGDTEGK SVFQLEKETD KETFKIRDDN PWVTVETNGA VRVKKKWDFE ELGPDKTIDF
     WVIITNMGHN AGIKYTDNQR VIILVKDVND EPPYFINRPL PMQAVVQLNA PPNTPVFTLQ
     ARDPDTDHNI HYFIVRDRTG GRFEVDERSG VVRTRGTDLF QLDMEYVLYV KAEDQNGKVD
     DRRFQSTPEE RLSIVGGKRA PQFYMPGYEA EIPENQKKDS DIISVKAKSF ADREIRYTLK
     AQGQGAGTFN IGPSSGIVKL AKELDFEDLR QPHVYTLIVT ATEDSGGFST SVELTIRVTD
     VNDNAPKFEL PDYQAHNVDE DIPLGTSILR VKAMDADSGA NAEIEYLVSD DHFAVDSNGI
     IVNNKQLDAD NNNAYYEFIV TAKDKGEPAK SGTATVRVYT KNKNDEEPKF SQQVYTPNVD
     ENAGPNTLVT TVVASDKDGD NVRFGFVGGG TSSGQFVIED ITGVIRLHNK AISLDRDKYE
     LNVTAMDDGS CCVNGDQTIH TSTAVVVVFI TDVNDNKPVF KDCGTYYPKV EEGAPNGSPV
     IKVVATDEDK GVNGQVKYSI VQQPNQKGTK FTVDEETGEV STNKVFDREG DDGKFVSVTV
     KATDQGDPSL EGVCSFTVEI TDVNDNPPLF DRQKYVENVK QDASIGTNIL RVSASDEDAD
     NNGAIVYSLS APFNPNDLEY FDIQAESGWI VLKKPLDRET YKLEAMAQDK GYPPLSRTVE
     VQIDVVDRAN NPPVWDHTVY GPIYVKENMP VGGKVVSIKA SSGIEGNPTV FYRLMPGSTA
     QTNKFHTFYL QQRPDNGDTW ADIKVNHPLD YESIKEYNLT IRVENNGAQQ LASEATVYIM
     LEDVNDEIPL FTEREQETVL EGEPIGTKVT QVNAIDKDGT FPNNQVYYYI VDSPRNEGKE
     FFEINLQSGE IFTKTVFDRE KKGAYALEVE ARDGAPSARP NSNGPNSVTK FIRIGIADKN
     DNPPYFDKSL YEAEVDENED IQHTVLTVTA KDHDESSRIR YEITSGNIGG AFAVKNMTGA
     IYVAGALDYE TRRRYELRLA ASDNLKENYT TVIIHVKDVN DNPPVFERPT YRTQITEEDD
     RNLPKRVLQV TATDGDKDRP QNIVYFLTGQ GIDPDNPANS KFDINRTTGE IFVLKPLDRD
     QPNGRPQWRF TVFAQDEGGE GLVGYADVQV NLKDINDNAP IFPQGVYFGN VTENGTAGMV
     VMTMTAVDYD DPNEGSNARL VYSIEKNVIE EETGSPIFEI EPDTGVIKTA VCCLDRERTP
     DYSIQVVAMD GGGLKGTGTA SIRVKDINDM PPQFTKDEWF TEVDETDGTA LPEMPILTVT
     VHDEDETNKF QYKVIDNSGY GADKFTMVRN NDGTGSLKIV QPLDYEDQLQ SNGFRFRIQV
     NDKGEDNDND KYHVAYSWVV VKLRDINDNK PHFERANVEV SVFEDTKVGT ELEKFKATDP
     DQGGKSKVSY SIDRSSDRQR QFAINQNGSV TIQRSLDREV VPRHQVKILA IDDGSPPKTA
     TATLTVIVQD INDNAPKFLK DYRPVLPEHV PPRKVVEILA TDDDDRSKSN GPPFQFRLDP
     SADDIIRASF KVEQDQKGAN GDGMAVISSL RSFDREQQKE YMIPIVIKDH GSPAMTGTST
     LTVIIGDVND NKMQPGSKDI FVYNYQGQSP DTPIGRVYVY DLDDWDLPDK KFYWEAQEHP
     RFKLDEDSGM VTMRAGTREG RYHLRFKVYD RKHTQTDVPA NVTVMVREIP HEAVINSGSV
     RLSGISDEDF IRVWNYRTQS LSRSKLDRFR DKLADLLNTE RENVDIFSVQ LKRRNPPLTD
     VRFSAHGSPY YKPVRLNGIV LMHREEIEKD VGINITMVGI DECLYENQMC EGSCTNALEI
     SPLPYMVNAN KTALVGVRVD TLADCTCGAR NFTKPESCRT TPCHNGGRCV DTRFGPHCSC
     PAGYTGPRCQ QTTRSFRGNG WAWYPPLEMC DESHLSLEFI TRKPDGLIIY NGPIVPPERD
     EMLISDFVAL ELERGYPRLL IDFGSGTLEL RVKTKKTLDD GEWHRIDLFW DTESVRMVVD
     FCKSAEISEM EDGTPPEFDD TSCQARGQIP PFNEYLNVNA PLQVGGLYRE QFEQSLYFWH
     YMPTAKGFDG CIRNLVHNSK LYDLAHPGLS RNSVAGCPQT EEVCAQTEAT ARCWEHGNCV
     GSLSEARCHC RPGWTGPACN IPTVPTTFKA QSYVKYALSF EPDRFSTQVQ LRFRTREEHG
     ELFRVSDQHN REYGILEIKD ARLHFRYNLN SLRTEEKDLW LNSVAVNDGQ WHVVRINRYG
     SAATLELDGG EGRRYNETFE FVGHQWLLVD KQEGVYAGGK AEYTGVRTFE VYADYQKSCL
     DDIRLEGKHL PLPPAMNGTQ WGQATMARNL EKGCPSNKPC SNVICPDPFE CVDLWNVYEC
     TCGEGRIMSP DSKGCMDRNE CLDMPCMNGA TCINLEPRLR YRCICPDGFW GESCELVQEG
     QTLKLSMGAL AAILVCLLII LILVLVFVVY NRRREAHIKY PGPDDDVREN IINYDDEGGG
     EDDMTAFDIT PLQIPIGGPM PPELAPMKMP IMYPVMTLMP GQEPNVGMFI EEHKKRADGD
     PNAPPFDDLR NYAYEGGGST AGSLSSLASG TDDEQQEYDY LGAWGPRFDK LANMYGPEAP
     NPHNTELEL
//
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