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Carboxypeptidase D (EC 3.4.17.22) (Metallocarboxypeptidase D) (Protein silver)

 CBPD_DROME              Reviewed;        1406 AA.
P42787; A2RVE4; B7Z112; C7LAH0; D0Z763; O46058; Q24094; Q24095;
Q9W5F3; Q9W5F4; Q9W5F5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
12-SEP-2018, entry version 177.
RecName: Full=Carboxypeptidase D;
EC=3.4.17.22;
AltName: Full=Metallocarboxypeptidase D;
AltName: Full=Protein silver;
Flags: Precursor;
Name=svr; Synonyms=CPD, CpepE; ORFNames=CG4122;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 5; 6 AND 7), AND FUNCTION.
TISSUE=Embryo;
PubMed=12393882; DOI=10.1074/jbc.M209652200;
Sidyelyeva G., Fricker L.D.;
"Characterization of Drosophila carboxypeptidase D.";
J. Biol. Chem. 277:49613-49620(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R;
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Booth B., Frise E., Kapadia B., Park S.,
Wan K.H., Yu C., Celniker S.E.;
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1152 (ISOFORMS 1/5), NUCLEOTIDE
SEQUENCE [MRNA] OF 93-152 (ISOFORMS 3/4/6), AND FUNCTION.
TISSUE=Embryo;
PubMed=7568156; DOI=10.1073/pnas.92.21.9470;
Settle S.H. Jr., Green M.M., Burtis K.C.;
"The silver gene of Drosophila melanogaster encodes multiple
carboxypeptidases similar to mammalian prohormone-processing
enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 92:9470-9474(1995).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 425-696, FUNCTION, AND
DEVELOPMENTAL STAGE.
STRAIN=Canton-S;
PubMed=8000074; DOI=10.1002/arch.940270303;
Bernasconi P.;
"Molecular cloning of a Drosophila melanogaster gene coding for an
homologue of human carboxypeptidase E.";
Arch. Insect Biochem. Physiol. 27:169-178(1994).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1251, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=Oregon-R; TISSUE=Head;
PubMed=17893096; DOI=10.1093/glycob/cwm097;
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
Panin V.;
"Identification of N-glycosylated proteins from the central nervous
system of Drosophila melanogaster.";
Glycobiology 17:1388-1403(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1380, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Required for the proper melanization and sclerotization
of the cuticle. {ECO:0000269|PubMed:12393882,
ECO:0000269|PubMed:7568156, ECO:0000269|PubMed:8000074}.
-!- CATALYTIC ACTIVITY: Releases C-terminal Arg and Lys from
polypeptides.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P00730};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.0 for carboxypeptidase domain 1, and 5.0-6.0 for
domain 2.;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1; Synonyms=B, 1B long tail-1;
IsoId=P42787-1; Sequence=Displayed;
Name=2; Synonyms=C;
IsoId=P42787-2; Sequence=VSP_037495;
Name=3; Synonyms=1A long tail-1, D;
IsoId=P42787-3; Sequence=VSP_000773;
Name=4; Synonyms=H;
IsoId=P42787-4; Sequence=VSP_000773, VSP_000779;
Note=No experimental confirmation available.;
Name=5; Synonyms=1B long tail-2, G;
IsoId=P42787-5; Sequence=VSP_000779;
Name=6; Synonyms=1A short, E;
IsoId=P42787-6; Sequence=VSP_000773, VSP_000775, VSP_000776;
Name=7; Synonyms=1B short, F;
IsoId=P42787-7; Sequence=VSP_000775, VSP_000776;
Name=8; Synonyms=G, I;
IsoId=P42787-8; Sequence=VSP_037495, VSP_000779;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Embryonic and adult stages.
{ECO:0000269|PubMed:8000074}.
-!- DOMAIN: There are 3 carboxypeptidase-like domains. Only the first
two domains seem to have kept a catalytic activity.
-!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA91650.1; Type=Frameshift; Positions=1106; Evidence={ECO:0000305};
Sequence=AAC46486.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AF545816; AAN73045.1; -; mRNA.
EMBL; AF545817; AAN73046.1; -; mRNA.
EMBL; AF545818; AAN73047.1; -; mRNA.
EMBL; AF545819; AAN73048.1; -; mRNA.
EMBL; AF545820; AAN73049.1; -; mRNA.
EMBL; AE014298; AAF45514.2; -; Genomic_DNA.
EMBL; AE014298; AAF45515.4; -; Genomic_DNA.
EMBL; AE014298; AAO41630.2; -; Genomic_DNA.
EMBL; AE014298; AAS65237.1; -; Genomic_DNA.
EMBL; AE014298; AAS65238.1; -; Genomic_DNA.
EMBL; AE014298; AAS65239.1; -; Genomic_DNA.
EMBL; AE014298; AAS65240.1; -; Genomic_DNA.
EMBL; AE014298; ACL82874.1; -; Genomic_DNA.
EMBL; AL009147; CAA15634.1; -; Genomic_DNA.
EMBL; AL009147; CAA15635.1; -; Genomic_DNA.
EMBL; BT029935; ABM92809.1; -; mRNA.
EMBL; BT099720; ACV53084.1; -; mRNA.
EMBL; BT100310; ACZ52622.1; -; mRNA.
EMBL; U29591; AAA91650.1; ALT_FRAME; mRNA.
EMBL; U29592; AAA91651.1; -; mRNA.
EMBL; U03883; AAC46486.1; ALT_SEQ; Genomic_DNA.
PIR; T13284; T13284.
PIR; T13420; T13420.
PIR; T13421; T13421.
RefSeq; NP_001138141.1; NM_001144669.2. [P42787-8]
RefSeq; NP_001284742.1; NM_001297813.1. [P42787-6]
RefSeq; NP_001284743.1; NM_001297814.1. [P42787-7]
RefSeq; NP_001284744.1; NM_001297815.1. [P42787-5]
RefSeq; NP_525032.2; NM_080293.4. [P42787-1]
RefSeq; NP_726675.3; NM_166846.5. [P42787-4]
RefSeq; NP_788852.2; NM_176679.3. [P42787-1]
RefSeq; NP_996319.1; NM_206596.2. [P42787-5]
RefSeq; NP_996320.1; NM_206597.2. [P42787-7]
RefSeq; NP_996321.1; NM_206598.3. [P42787-6]
RefSeq; NP_996322.1; NM_206599.2. [P42787-3]
UniGene; Dm.42; -.
ProteinModelPortal; P42787; -.
SMR; P42787; -.
BioGrid; 57568; 3.
IntAct; P42787; 2.
STRING; 7227.FBpp0089126; -.
MEROPS; M14.037; -.
iPTMnet; P42787; -.
PaxDb; P42787; -.
PRIDE; P42787; -.
EnsemblMetazoa; FBtr0070081; FBpp0070080; FBgn0004648. [P42787-1]
EnsemblMetazoa; FBtr0070084; FBpp0089123; FBgn0004648. [P42787-3]
EnsemblMetazoa; FBtr0070085; FBpp0089124; FBgn0004648. [P42787-6]
EnsemblMetazoa; FBtr0070086; FBpp0089125; FBgn0004648. [P42787-7]
EnsemblMetazoa; FBtr0070087; FBpp0089126; FBgn0004648. [P42787-5]
EnsemblMetazoa; FBtr0290016; FBpp0288455; FBgn0004648. [P42787-4]
EnsemblMetazoa; FBtr0290017; FBpp0288456; FBgn0004648. [P42787-8]
EnsemblMetazoa; FBtr0340146; FBpp0309132; FBgn0004648. [P42787-6]
EnsemblMetazoa; FBtr0344737; FBpp0311069; FBgn0004648. [P42787-7]
EnsemblMetazoa; FBtr0344738; FBpp0311070; FBgn0004648. [P42787-1]
EnsemblMetazoa; FBtr0344739; FBpp0311071; FBgn0004648. [P42787-5]
GeneID; 30998; -.
KEGG; dme:Dmel_CG4122; -.
CTD; 30998; -.
FlyBase; FBgn0004648; svr.
eggNOG; KOG2649; Eukaryota.
eggNOG; ENOG410XX0H; LUCA.
GeneTree; ENSGT00760000119124; -.
InParanoid; P42787; -.
KO; K07752; -.
OMA; GNHERIA; -.
OrthoDB; EOG091G06A9; -.
PhylomeDB; P42787; -.
BRENDA; 3.4.17.22; 1994.
Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
ChiTaRS; svr; fly.
GenomeRNAi; 30998; -.
PRO; PR:P42787; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0004648; Expressed in 24 organ(s), highest expression level in head.
ExpressionAtlas; P42787; baseline and differential.
Genevisible; P42787; DM.
GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
GO; GO:0005576; C:extracellular region; HDA:FlyBase.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
GO; GO:0004180; F:carboxypeptidase activity; IDA:FlyBase.
GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:FlyBase.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0007616; P:long-term memory; IMP:FlyBase.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:0016485; P:protein processing; IBA:GO_Central.
CDD; cd03868; M14_CPD_I; 1.
InterPro; IPR008969; CarboxyPept-like_regulatory.
InterPro; IPR034241; M14_CPD_I.
InterPro; IPR000834; Peptidase_M14.
Pfam; PF00246; Peptidase_M14; 2.
PRINTS; PR00765; CRBOXYPTASEA.
SMART; SM00631; Zn_pept; 2.
SUPFAM; SSF49464; SSF49464; 4.
PROSITE; PS00132; CARBOXYPEPT_ZN_1; 2.
PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2.
1: Evidence at protein level;
Alternative splicing; Carboxypeptidase; Complete proteome; Cuticle;
Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Phosphoprotein; Protease; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1406 Carboxypeptidase D.
/FTId=PRO_0000004405.
TOPO_DOM 26 1312 Extracellular. {ECO:0000255}.
TRANSMEM 1313 1333 Helical. {ECO:0000255}.
TOPO_DOM 1334 1406 Cytoplasmic. {ECO:0000255}.
REGION 26 446 Domain 1.
REGION 447 865 Domain 2.
REGION 866 1313 Domain 3.
MOTIF 1343 1345 Cell attachment site. {ECO:0000255}.
ACT_SITE 305 305 Proton donor/acceptor 1.
{ECO:0000250|UniProtKB:Q90240}.
ACT_SITE 730 730 Proton donor/acceptor 2.
{ECO:0000250|UniProtKB:Q90240}.
METAL 101 101 Zinc 1; catalytic. {ECO:0000250}.
METAL 104 104 Zinc 1; catalytic. {ECO:0000250}.
METAL 217 217 Zinc 1; catalytic. {ECO:0000250}.
METAL 517 517 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 520 520 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 626 626 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:P00730}.
MOD_RES 1380 1380 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 549 549 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 612 612 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 652 652 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 787 787 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 808 808 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 981 981 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1152 1152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1251 1251 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096}.
VAR_SEQ 1 152 MPTLGLLFASIGIAVLAMGVPHCRGYTIKEDESFLQQPHYA
SQEQLEDLFAGLEKAYPNQAKVHFLGRSLEGRNLLALQISR
NTRSRNLLTPPVKYIANMHGDETVGRQLLVYMAQYLLGNHE
RISDLGQLVNSTDIYLVPTMNPDGYALSQ -> MLFFCLAL
IIGCAVGEYSEVRVIQEEDNFLESPHYLKNEEIGDLFSQLA
KDYPDLAQTYTIGKSLEDRPIYALALSAPTGESKNGDLLRP
MVKLVANIQGDEAVGRQMVLYMAEYLATHYDGDPKVQALLN
LTEIHFLPTCNPDGFAKAK (in isoform 3,
isoform 4 and isoform 6).
{ECO:0000303|PubMed:12393882}.
/FTId=VSP_000773.
VAR_SEQ 2 152 PTLGLLFASIGIAVLAMGVPHCRGYTIKEDESFLQQPHYAS
QEQLEDLFAGLEKAYPNQAKVHFLGRSLEGRNLLALQISRN
TRSRNLLTPPVKYIANMHGDETVGRQLLVYMAQYLLGNHER
ISDLGQLVNSTDIYLVPTMNPDGYALSQ -> NTCL (in
isoform 2 and isoform 8).
{ECO:0000303|Ref.5}.
/FTId=VSP_037495.
VAR_SEQ 426 435 NFRKVKVERS -> ISSFYSPYYF (in isoform 6
and isoform 7).
{ECO:0000303|PubMed:12393882}.
/FTId=VSP_000775.
VAR_SEQ 436 1406 Missing (in isoform 6 and isoform 7).
{ECO:0000303|PubMed:12393882}.
/FTId=VSP_000776.
VAR_SEQ 1385 1406 ELSQRAHLVNNQTNYSFIIQAA -> GMTIQPYFDEEQLER
ILHTDDDDDDGPHMEPELDVADDSEDDIVMLHNNGNKRRH
(in isoform 4, isoform 5 and isoform 8).
{ECO:0000303|PubMed:12393882,
ECO:0000303|Ref.5}.
/FTId=VSP_000779.
CONFLICT 733 733 C -> Y (in Ref. 6; AAA91650).
{ECO:0000305}.
CONFLICT 1041 1041 V -> E (in Ref. 5; ABM92809 and 6;
AAA91650). {ECO:0000305}.
SEQUENCE 1406 AA; 158789 MW; E7CF31AEC21363BD CRC64;
MPTLGLLFAS IGIAVLAMGV PHCRGYTIKE DESFLQQPHY ASQEQLEDLF AGLEKAYPNQ
AKVHFLGRSL EGRNLLALQI SRNTRSRNLL TPPVKYIANM HGDETVGRQL LVYMAQYLLG
NHERISDLGQ LVNSTDIYLV PTMNPDGYAL SQEGNCESLP NYVGRGNAAN IDLNRDFPDR
LEQSHVHQLR AQSRQPETAA LVNWIVSKPF VLSANFHGGA VVASYPYDNS LAHNECCEES
LTPDDRVFKQ LAHTYSDNHP IMRKGNNCND SFSGGITNGA HWYELSGGMQ DFNYAFSNCF
ELTIELSCCK YPAASTLPQE WQRNKASLLQ LLRQAHIGIK GLVTDASGFP IADANVYVAG
LEEKPMRTSK RGEYWRLLTP GLYSVHASAF GYQTSAPQQV RVTNDNQEAL RLDFKLAPVE
TNFDGNFRKV KVERSEPPQK LKKQFNGFLT PTKYEHHNFT AMESYLRAIS SSYPSLTRLY
SIGKSVQGRD LWVLEIFATP GSHVPGVPEF KYVANMHGNE VVGKELLLIL TKYMLERYGN
DDRITKLVNG TRMHFLYSMN PDGYEISIEG DRTGGVGRAN AHGIDLNRNF PDQYGTDRFN
KVTEPEVAAV MNWTLSLPFV LSANLHGGSL VANYPFDDNE NDFNDPFMRL RNSSINGRKP
NPTEDNALFK HLAGIYSNAH PTMYLGQPCE LFQNEFFPDG ITNGAQWYSV TGGMQDWNYV
RAGCLELTIE MGCDKFPKAA ELSRYWEDHR EPLLQFIEQV HCGIHGFVHS TIGTPIAGAV
VRLDGANHST YSQVFGDYWK LALPGRHNLT VLGDNYAPLR MEVEVPDVHP FEMRMDITLM
PDDPQHWASA NDFRIIENVV NTRYHTNPQV RARLAELENQ NGQIASFGYA DSEFGTIFNY
LKMTSDIGEP EEHKYKLLVV SSLYDTTAPL GREILLNLIR HLVEGFKLQD TSVVELLKRS
VIYFLPQTSK FQNVFDMYNS NTSICDPVLG DELAERILGP ETDQAKDVFL QFLRSERFDL
MLTFGAGNSD LNYPKGDSVL VKFAHRMQRT EFNYSPLQCP PSATRQLHRE TTERLTNMMY
RIYNLPVYTL GISCCRMPHQ KKIASVWRKN IDKIKNFLAL VKTGVSGLVQ NDKGQPLREA
YVRLLEHDRI INVTKNVARF QLMLPHGLYG LEVTAPNYES QMIKVDVEDG RVTELGIIRM
HPFTLIRGVV LELPNNDNRA TTSIAGVVLD ESNHPVRNAK VSVVGQTQLR NFTGSMGQYR
ISAVPLGTIT LKVEAPRHLE ATRQMHLIQG GLATENVVFH LKVNEHVFGL PRFLFILCAS
VLIIVGVIVC VLCAQFWFYR RHRGDKPYYN FSLLPQRGKE QFGLEDDDGG DDGETELFRS
PIKRELSQRA HLVNNQTNYS FIIQAA


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