GenomeNet

Database: UniProt
Entry: E1JJ98_DROME
LinkDB: E1JJ98_DROME
Original site: E1JJ98_DROME 
ID   E1JJ98_DROME            Unreviewed;      1593 AA.
AC   E1JJ98;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=FI20257p1 {ECO:0000313|EMBL:AFH78571.1};
DE   SubName: Full=Small optic lobes, isoform E {ECO:0000313|EMBL:ACZ95346.1};
GN   Name=sol {ECO:0000313|EMBL:ACZ95346.1,
GN   ECO:0000313|FlyBase:FBgn0003464};
GN   Synonyms=CalpD {ECO:0000313|EMBL:ACZ95346.1}, calpD
GN   {ECO:0000313|EMBL:ACZ95346.1}, Dmel\CG1391
GN   {ECO:0000313|EMBL:ACZ95346.1}, DmSol {ECO:0000313|EMBL:ACZ95346.1},
GN   nofE {ECO:0000313|EMBL:ACZ95346.1}, PC79
GN   {ECO:0000313|EMBL:ACZ95346.1}, SOL {ECO:0000313|EMBL:ACZ95346.1}, Sol
GN   {ECO:0000313|EMBL:ACZ95346.1}, sol-RE {ECO:0000313|EMBL:AFH78571.1},
GN   w5000 {ECO:0000313|EMBL:ACZ95346.1};
GN   ORFNames=CG1391 {ECO:0000313|EMBL:ACZ95346.1,
GN   ECO:0000313|FlyBase:FBgn0003464}, Dmel_CG1391
GN   {ECO:0000313|EMBL:ACZ95346.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:ACZ95346.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:ACZ95346.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA   An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:ACZ95346.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:ACZ95346.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000313|EMBL:ACZ95346.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:ACZ95346.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:ACZ95346.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:ACZ95346.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA   Svirskas R., Rubin G.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:ACZ95346.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [9] {ECO:0000313|EMBL:ACZ95346.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
RN   [10] {ECO:0000313|EMBL:AFH78571.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [11] {ECO:0000313|EMBL:ACZ95346.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109357; DOI=.1534/g3.115.018929;
RG   FlyBase Consortium;
RA   Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA   Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA   Gelbart W.M., null;
RT   "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT   Throughput Data.";
RL   G3 (Bethesda) 5:1721-1736(2015).
RN   [12] {ECO:0000313|EMBL:ACZ95346.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109356; DOI=.1534/g3.115.018937;
RG   FlyBase Consortium;
RA   Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA   Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA   null;
RT   "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL   G3 (Bethesda) 5:1737-1749(2015).
RN   [13] {ECO:0000313|EMBL:ACZ95346.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25589440;
RA   Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA   Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA   Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA   de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA   Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA   Karpen G.H., Celniker S.E.;
RT   "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL   Genome Res. 25:445-458(2015).
RN   [14] {ECO:0000313|EMBL:ACZ95346.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Berkeley Drosophila Genome Project;
RA   Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA   Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA   Rubin G.;
RT   "Drosophila melanogaster release 4 sequence.";
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [15] {ECO:0000313|EMBL:ACZ95346.1}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC       {ECO:0000256|ARBA:ARBA00007623}.
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DR   EMBL; AE014298; ACZ95346.1; -; Genomic_DNA.
DR   EMBL; BT133439; AFH78571.1; -; mRNA.
DR   RefSeq; NP_001162813.1; NM_001169342.2.
DR   SMR; E1JJ98; -.
DR   MEROPS; C02.010; -.
DR   DNASU; 44014; -.
DR   EnsemblMetazoa; FBtr0301583; FBpp0290798; FBgn0003464.
DR   GeneID; 44014; -.
DR   AGR; FB:FBgn0003464; -.
DR   CTD; 44014; -.
DR   FlyBase; FBgn0003464; sol.
DR   VEuPathDB; VectorBase:FBgn0003464; -.
DR   OrthoDB; 142935at2759; -.
DR   BioGRID-ORCS; 44014; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 44014; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0003464; Expressed in secondary oocyte and 23 other cell types or tissues.
DR   ExpressionAtlas; E1JJ98; baseline and differential.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00044; CysPc; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 3.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR10183; CALPAIN; 1.
DR   PANTHER; PTHR10183:SF382; CALPAIN-15; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   Pfam; PF00641; zf-RanBP; 6.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00230; CysPc; 1.
DR   SMART; SM00547; ZnF_RBZ; 6.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 5.
DR   PROSITE; PS50199; ZF_RANBP2_2; 4.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   DOMAIN          1..35
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          703..732
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          743..773
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          926..955
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          1013..1320
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   REGION          210..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          859..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          664..691
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        234..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..594
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..875
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1078
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        1244
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        1264
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   1593 AA;  174184 MW;  2B989757525814BD CRC64;
     MGTISSVLQW SCTKCNTINP TESLKCFNCG TVRKVFPQQQ QQQHRSSSIT ASWTADDALE
     QEQAEKGQER DKEKGRAAVA RSEYKHVYKS LLRGCLKRPQ RNSQNLPANC VDCEDTRKYI
     KSSIELYRHF SNPALNRRWV CHACGTDNSS VTWHCLICDT VSYLAPIYKD AIAADRGQDL
     AGSLGNRGEL LAADHSHPHH HHHYLHQELE EQHQHQLHSQ HLHKRHLKGR SASGSGSGPG
     SGSGLRRTQS LSTAIDKSAS GRSCHICYAN NQSKDIFNLP QIKPAPQLTG IPPVAACSNS
     RFAIANDTFC RRKQNNNNKN QNHKVVRESG AKRKYNFTIT TLSRSAAKDA GHGQMKPLRQ
     VVNLNLNLQQ EPQQKSPANP QQLQRKTQRE PAAVSMNPTQ FTIPRNGVFI AVNEWSEPMA
     SSSSVSSSSN HHHHHHSNSN SNSSGNSNII NNNSSSSSGS NKLYENECVA LAQQQLRAAA
     AQAAQAAATA VAIASSPSAK AMAEPAPTAT MPIYAQVNKQ HKLKKKQQIA SESQTNNNTG
     SGEIADAVSE SLTAGLGTST DGSGEASESE SQVEEHSIYA KVWKGPRKAT ESKIMHDPGS
     SSRLSGAASA AAGTASAGAI AAAVGAAAAS RHDNKTQLGN GSRSKMWICI KCSYAYNRLW
     LQTCEMCEAK AEQQQQQLQL QQQQQQQQQH HHHHLQQQQA APRDEPWTCK KCTLVNYSTA
     MACVVCGGSK LKSISSIEDM TLRKGEFWTC SHCTLKNSLH SPVCSACKSH RQPQLSMAME
     AVRERPDGQS YEEQDAAAVG GGGGSAHQSG ANEVKAPTAL NLPLTSVALP MPMLQLPTST
     AAGLRGSRSP SPRMQLLPSL QQQRNSSSSG AIPKRHSTGG SIVPRNISIA GLANYNLQQG
     QGVGSASVVS ASGAGSGAGA VGASTSTKKW QCPACTYDNC AASVVCDICS SPRGLASAVL
     GEALGRKSVR VALTPADIRQ ESKLMENLRQ LEETEALTKW QNIIQYCRDN SELFVDDSFP
     PAPKSLYYNP ASGAGEGNPV VQWRRPHEIN CDGGAYPPWA VFRTPLPSDI CQGVLGNCWL
     LSALAVLAER EDLVKEVLVT KEICGQGAYQ VRLCKDGKWT TVLVDDLLPC DKRGHLVYSQ
     AKRKQLWVPL IEKAVAKIHG CYEALVSGRA IEGLATLTGA PCESIPLQAS SLPMPSEDEL
     DKDLIWAQLL SSRCVRFLMG ASCGGGNMKV DEEEYQQKGL RPRHAYSVLD VKDIQGHRLL
     KLRNPWGHYS WRGDWSDDSS LWTDDLRDAL MPHGASEGVF WISFEDVLNY FDCIDICKVR
     SGWNEVRLQG TLQPLCSISC VLLTVLEPTE AEFTLFQEGQ RNSEKSQRSQ LDLCVVIFRT
     RSPAAPEIGR LVEHSKRQVR GFVGCHKMLE RDIYLLVCLA FNHWHTGIED PHQYPQCILA
     IHSSKRLLVE QISPSPHLLA DAIISLTLTK GQRHEGREGM TAYYLTKGWA GLVVMVENRH
     ENKWIHVKCD CQESYNVVST RGELKTVDSV PPLQRQVIIV LTQLEGSGGF SIAHRLTHRL
     ANSRGLHDWG PPGATHCPPI ENVHGLHAPR LIT
//
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