ID   PCSK5_MOUSE             Reviewed;        1877 AA.
AC   Q04592; E9QPB7; Q62040;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=Proprotein convertase subtilisin/kexin type 5;
DE            EC=3.4.21.-;
DE   AltName: Full=Proprotein convertase 5;
DE            Short=PC5;
DE   AltName: Full=Proprotein convertase 6;
DE            Short=PC6;
DE   AltName: Full=Subtilisin-like proprotein convertase 6;
DE            Short=SPC6;
DE   AltName: Full=Subtilisin/kexin-like protease PC5;
DE   Flags: Precursor;
GN   Name=Pcsk5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 330-1877 (ISOFORM PC5B).
RC   STRAIN=ICR; TISSUE=Intestine;
RX   PubMed=8335106; DOI=10.1016/0014-5793(93)80163-o;
RA   Nakagawa T., Murakami K., Nakayama K.;
RT   "Identification of an isoform with an extremely large Cys-rich region of
RT   PC6, a Kex2-like processing endoprotease.";
RL   FEBS Lett. 327:165-171(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PC5A).
RC   TISSUE=Brain, and Intestine;
RX   PubMed=8468318; DOI=10.1093/oxfordjournals.jbchem.a124015;
RA   Nakagawa T., Hosaka M., Torii S., Watanabe T., Murakami K., Nakayama K.;
RT   "Identification and functional expression of a new member of the mammalian
RT   Kex2-like processing endoprotease family: its striking structural
RT   similarity to PACE4.";
RL   J. Biochem. 113:132-135(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PC5A).
RC   TISSUE=Adrenal cortex;
RX   PubMed=8341687; DOI=10.1073/pnas.90.14.6691;
RA   Lusson J., Vieau D., Hamelin J., Day R., Chretien M., Seidah N.G.;
RT   "cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate
RT   proprotein convertase expressed in endocrine and nonendocrine cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6691-6695(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RX   PubMed=8947550; DOI=10.1083/jcb.135.5.1261;
RA   De Bie I., Marcinkiewicz M., Malide D., Lazure C., Nakayama K.,
RA   Bendayan M., Seidah N.G.;
RT   "The isoforms of proprotein convertase PC5 are sorted to different
RT   subcellular compartments.";
RL   J. Cell Biol. 135:1261-1275(1996).
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=8698813; DOI=10.1083/jcb.134.1.181;
RA   Constam D.B., Calfon M., Robertson E.J.;
RT   "SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone
RT   morphogenetic proteins at distinct sites during embryogenesis.";
RL   J. Cell Biol. 134:181-191(1996).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=9291583;
RX   DOI=10.1002/(sici)1520-6408(1997)21:1<75::aid-dvg9>3.0.co;2-5;
RA   Rancourt S.L., Rancourt D.E.;
RT   "Murine subtilisin-like proteinase SPC6 is expressed during embryonic
RT   implantation, somitogenesis, and skeletal formation.";
RL   Dev. Genet. 21:75-81(1997).
CC   -!- FUNCTION: Serine endoprotease that processes various proproteins by
CC       cleavage at paired basic amino acids, recognizing the RXXX[KR]R
CC       consensus motif. Likely functions in the constitutive and regulated
CC       secretory pathways. Plays an essential role in pregnancy establishment
CC       by proteolytic activation of a number of important factors such as
CC       BMP2, CALD1 and alpha-integrins. May be responsible for the maturation
CC       of gastrointestinal peptides. May be involved in the cellular
CC       proliferation of adrenal cortex via the activation of growth factors.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform PC5A]: Secreted. Note=Secreted through
CC       the regulated secretory pathway.
CC   -!- SUBCELLULAR LOCATION: [Isoform PC5B]: Endomembrane system; Single-pass
CC       type I membrane protein. Note=Type I membrane protein localized to a
CC       paranuclear post-Golgi network compartment in communication with early
CC       endosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=PC5B; Synonyms=Long;
CC         IsoId=Q04592-1; Sequence=Displayed;
CC       Name=PC5A; Synonyms=Short;
CC         IsoId=Q04592-2; Sequence=VSP_005438, VSP_005439;
CC   -!- TISSUE SPECIFICITY: PC5A is expressed in most tissues but is most
CC       abundant in the intestine and adrenals. PC5B is expressed in the
CC       intestine, adrenals and lung but not in the brain.
CC   -!- DEVELOPMENTAL STAGE: Weakly expressed throughout the embryo, except in
CC       the developing nervous system, the ribs and the liver, but markedly up-
CC       regulated at discrete sites during development. At 6.5 dpc, prominent
CC       expression observed in differentiated decidua. At 7.5 dpc, intense
CC       expression in extraembryonic endoderm, amnion and nascent mesoderm. At
CC       8.5 dpc, abundant expression in somites and yolk sac followed by a
CC       confinement to dermamyotome compartment. Between 9.5 dpc and 11.5 dpc,
CC       abundant expression in AER (thickened ectodermal cells of limb buds).
CC       At 12.5 dpc, expression in the limbs is confined to the condensing
CC       mesenchyme surrounding the cartilage. At this stage, strong expression
CC       also detected in vertebral and facial cartilage primordia and in the
CC       muscle of the tongue. At 16.5 dpc, abundant expression in epithelial
CC       cells of the intestinal villi. Isoform A is most abundant at all stages
CC       but significant levels of isoform B occur at 12.5 dpc.
CC       {ECO:0000269|PubMed:8698813, ECO:0000269|PubMed:9291583}.
CC   -!- DOMAIN: The propeptide domain acts as an intramolecular chaperone
CC       assisting the folding of the zymogen within the endoplasmic reticulum.
CC   -!- DOMAIN: AC 1 and AC 2 (clusters of acidic amino acids) contain sorting
CC       information. AC 1 directs TGN localization and interacts with the TGN
CC       sorting protein PACS-1.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; D17583; BAA04507.1; -; mRNA.
DR   EMBL; D12619; BAA02143.1; -; mRNA.
DR   EMBL; L14932; AAA74636.1; -; mRNA.
DR   EMBL; AC125203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC133509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC147369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS50401.1; -. [Q04592-1]
DR   CCDS; CCDS50402.1; -. [Q04592-2]
DR   PIR; A48225; A48225.
DR   PIR; S34583; S34583.
DR   RefSeq; NP_001177412.1; NM_001190483.2. [Q04592-1]
DR   AlphaFoldDB; Q04592; -.
DR   SMR; Q04592; -.
DR   BioGRID; 202061; 4.
DR   IntAct; Q04592; 1.
DR   MINT; Q04592; -.
DR   STRING; 10090.ENSMUSP00000025618; -.
DR   GlyCosmos; Q04592; 13 sites, No reported glycans.
DR   GlyGen; Q04592; 13 sites.
DR   iPTMnet; Q04592; -.
DR   PhosphoSitePlus; Q04592; -.
DR   MaxQB; Q04592; -.
DR   PaxDb; 10090-ENSMUSP00000025618; -.
DR   PeptideAtlas; Q04592; -.
DR   ProteomicsDB; 294032; -. [Q04592-1]
DR   ProteomicsDB; 294033; -. [Q04592-2]
DR   Antibodypedia; 27199; 220 antibodies from 26 providers.
DR   DNASU; 18552; -.
DR   Ensembl; ENSMUST00000025618.16; ENSMUSP00000025618.9; ENSMUSG00000024713.17. [Q04592-1]
DR   Ensembl; ENSMUST00000050715.10; ENSMUSP00000050272.9; ENSMUSG00000024713.17. [Q04592-2]
DR   GeneID; 18552; -.
DR   KEGG; mmu:18552; -.
DR   UCSC; uc008gxp.2; mouse. [Q04592-1]
DR   AGR; MGI:97515; -.
DR   CTD; 5125; -.
DR   MGI; MGI:97515; Pcsk5.
DR   VEuPathDB; HostDB:ENSMUSG00000024713; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   GeneTree; ENSGT00940000155770; -.
DR   HOGENOM; CLU_003159_0_0_1; -.
DR   InParanoid; Q04592; -.
DR   OMA; TWYNDTW; -.
DR   OrthoDB; 5474719at2759; -.
DR   PhylomeDB; Q04592; -.
DR   TreeFam; TF314277; -.
DR   BRENDA; 3.4.21.B26; 3474.
DR   Reactome; R-MMU-167060; NGF processing.
DR   Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
DR   BioGRID-ORCS; 18552; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Pcsk5; mouse.
DR   PRO; PR:Q04592; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q04592; Protein.
DR   Bgee; ENSMUSG00000024713; Expressed in external carotid artery and 253 other cell types or tissues.
DR   ExpressionAtlas; Q04592; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:1990635; C:proximal dendrite; ISO:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR   GO; GO:0042277; F:peptide binding; IDA:BHF-UCL.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:BHF-UCL.
DR   GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR   GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR   GO; GO:0140447; P:cytokine precursor processing; IDA:BHF-UCL.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0007566; P:embryo implantation; IMP:BHF-UCL.
DR   GO; GO:0048566; P:embryonic digestive tract development; IMP:BHF-UCL.
DR   GO; GO:0048706; P:embryonic skeletal system development; IMP:BHF-UCL.
DR   GO; GO:0007507; P:heart development; IMP:BHF-UCL.
DR   GO; GO:0001822; P:kidney development; IMP:BHF-UCL.
DR   GO; GO:0035108; P:limb morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
DR   GO; GO:0033625; P:positive regulation of integrin activation; ISO:MGI.
DR   GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; ISO:MGI.
DR   GO; GO:1905609; P:positive regulation of smooth muscle cell-matrix adhesion; ISO:MGI.
DR   GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR   GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
DR   GO; GO:0030323; P:respiratory tube development; IMP:BHF-UCL.
DR   GO; GO:0006465; P:signal peptide processing; ISO:MGI.
DR   GO; GO:0019058; P:viral life cycle; IDA:BHF-UCL.
DR   CDD; cd00064; FU; 17.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00181; EGF; 18.
DR   SMART; SM00261; FU; 22.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 8.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
DR   Genevisible; Q04592; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Pregnancy;
KW   Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW   Transmembrane; Transmembrane helix; Zymogen.
FT   SIGNAL          1..34
FT   PROPEP          35..116
FT                   /id="PRO_0000027104"
FT   CHAIN           117..1877
FT                   /note="Proprotein convertase subtilisin/kexin type 5"
FT                   /id="PRO_0000027105"
FT   TOPO_DOM        117..1768
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1769..1789
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1790..1877
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          136..455
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          463..603
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT   REPEAT          632..682
FT                   /note="FU 1"
FT   REPEAT          685..732
FT                   /note="FU 2"
FT   REPEAT          736..779
FT                   /note="FU 3"
FT   REPEAT          781..826
FT                   /note="FU 4"
FT   REPEAT          834..881
FT                   /note="FU 5"
FT   REPEAT          884..929
FT                   /note="FU 6"
FT   REPEAT          931..981
FT                   /note="FU 7"
FT   REPEAT          984..1030
FT                   /note="FU 8"
FT   REPEAT          1034..1079
FT                   /note="FU 9"
FT   REPEAT          1081..1123
FT                   /note="FU 10"
FT   REPEAT          1127..1168
FT                   /note="FU 11"
FT   REPEAT          1206..1248
FT                   /note="FU 12"
FT   REPEAT          1252..1299
FT                   /note="FU 13"
FT   REPEAT          1301..1345
FT                   /note="FU 14"
FT   REPEAT          1347..1390
FT                   /note="FU 15"
FT   REPEAT          1392..1438
FT                   /note="FU 16"
FT   REPEAT          1442..1487
FT                   /note="FU 17"
FT   REPEAT          1491..1536
FT                   /note="FU 18"
FT   REPEAT          1540..1585
FT                   /note="FU 19"
FT   REPEAT          1589..1636
FT                   /note="FU 20"
FT   REPEAT          1640..1685
FT                   /note="FU 21"
FT   REPEAT          1691..1738
FT                   /note="FU 22"
FT   REGION          638..1753
FT                   /note="CRM (Cys-rich motif)"
FT   REGION          1825..1844
FT                   /note="AC 1"
FT   REGION          1856..1877
FT                   /note="AC 2"
FT   MOTIF           521..523
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        173
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        214
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        388
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   SITE            116..117
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        383
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        667
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        754
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        804
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        854
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        951
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1016
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1711
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1733
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         878..915
FT                   /note="GEYIDDQGHCQTCEASCAKCWGPTQEDCISCPVTRVLD -> ATEESWAEGG
FT                   FCMLVKKNNLCQRKVLQQLCCKTCTFQG (in isoform PC5A)"
FT                   /evidence="ECO:0000303|PubMed:8341687,
FT                   ECO:0000303|PubMed:8468318"
FT                   /id="VSP_005438"
FT   VAR_SEQ         916..1877
FT                   /note="Missing (in isoform PC5A)"
FT                   /evidence="ECO:0000303|PubMed:8341687,
FT                   ECO:0000303|PubMed:8468318"
FT                   /id="VSP_005439"
FT   CONFLICT        704
FT                   /note="N -> D (in Ref. 1; BAA04507, 2; BAA02143 and 3;
FT                   AAA74636)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        986
FT                   /note="A -> T (in Ref. 1; BAA04507)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1002
FT                   /note="V -> I (in Ref. 1; BAA04507)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1139
FT                   /note="N -> T (in Ref. 1; BAA04507)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1877 AA;  209257 MW;  68F7B768E063872B CRC64;
     MDWDWGNRCS RPGRRDLLCV LALLAGCLLP VCRTRVYTNH WAVKIAGGFA EADRIASKYG
     FINVGQIGAL KDYYHFYHSR TIKRSVLSSR GTHSFISMEP KVEWIQQQVV KKRTKRDYDL
     SHAQSTYFND PKWPSMWYMH CSDNTHPCQS DMNIEGAWKR GYTGKNIVVT ILDDGIERTH
     PDLMQNYDAL ASCDVNGNDL DPMPRYDASN ENKHGTRCAG EVAATANNSH CTVGIAFNAK
     IGGVRMLDGD VTDMVEAKSV SYNPQHVHIY SASWGPDDDG KTVDGPAPLT RQAFENGVRM
     GRRGLGSVFV WASGNGGRSK DHCSCDGYTN SIYTISISST AESGKKPWYL EECSSTLATT
     YSSGESYDKK IITTDLRQRC TDNHTGTSAS APMAAGIIAL ALEANPFLTW RDVQHVIVRT
     SRAGHLNAND WKTNAAGFKV SHLYGFGLMD AEAMVMEAEK WTTVPQQHVC VESTDRQIKT
     IRPNSAVRSI YKASGCSDNP NHHVNYLEHV VVRITITHPR RGDLAIYLTS PSGTRSQLLA
     NRLFDHSMEG FKNWEFMTIH CWGERAAGDW VLEVYDTPSQ LRNFKTPGKL KEWSLVLYGT
     SVQPYSPTNE FPKVERFRYS RVEDPTDDYG AEDYAGPCDP ECSEVGCDGP GPDHCSDCLH
     YYYKLKNNTR ICVSSCPPGH YHADKKRCRK CAPNCESCFG SHGNQCLSCK YGYFLNEETS
     SCVTQCPDGS YEDIKKNVCG KCSENCKACI GFHNCTECKG GLSLQGSRCS VTCEDGQFFN
     GHDCQPCHRF CATCSGAGAD GCINCTEGYV MEEGRCVQSC SVSYYLDHSS EGGYKSCKRC
     DNSCLTCNGP GFKNCSSCPS GYLLDLGTCQ MGAICKDGEY IDDQGHCQTC EASCAKCWGP
     TQEDCISCPV TRVLDDGRCV MNCPSWKFEF KKQCHPCHYT CQGCQGSGPS NCTSCRADKH
     GQERFLYHGE CLENCPVGHY PAKGHACLPC PDNCELCYNP HVCSRCMSGY VIIPPNHTCQ
     KLECRQGEFQ DSEYEECMPC EEGCLGCTED DPGACTSCAT GYYMFERHCY KACPEKTFGV
     KWECRACGTN CGSCDQHECY WCEEGFFLSG GSCVQDCGPG FHGDQELGEC KPCHRACENC
     TGSGYNQCSS CQEGLQLWHG TCLWSTWPQV EGKDWNEAVP TEKPSLVRSL LQDRRKWKVQ
     IKRDATSQNQ PCHSSCKTCN GSLCASCPTG MYLWLQACVP SCPQGTWPSV TSGSCEKCSE
     DCVSCSGADL CQQCLSQPDN TLLLHEGRCY HSCPEGFYAK DGVCEHCSSP CKTCEGNATS
     CNSCEGDFVL DHGVCWKTCP EKHVAVEGVC KHCPERCQDC IHEKTCKECM PDFFLYNDMC
     HRSCPKSFYP DMRQCVPCHK NCLECNGPKE DDCKVCADTS KALHNGLCLD ECPEGTYKEE
     ENDECRDCPE SCLICSSAWT CLACREGFTV VHDVCTAPKE CAAVEYWDEG SHRCQPCHKK
     CSRCSGPSED QCYTCPRETF LLNTTCVKEC PEGYHTDKDS QQCVLCHSSC RTCEGPHSMQ
     CLSCRPGWFQ LGKECLLQCR DGYYGESTSG RCEKCDKSCK SCRGPRPTDC QSCDTFFFLL
     RSKGQCHRAC PEHYYADQHA QTCERCHPTC DKCSGKEAWS CLSCVWSYHL LKGICIPECI
     VGEYREGKGE NFNCKKCHES CMECKGPGSK NCTGCSAGLL LDMDDNRCLH CCNASHSRRS
     QDCCDCQSST DECILPAREA EFYEHTKTAL LVTSGAMLLL LLGAAAVVWR KSRSRPVAKG
     RYEKLAEPTV SYSSYRSSYL DEDQVIEYRD RDYDEDDEDD IVYMGQDGTV YRKFKYGLLD
     ETEDDELEYD DESYSYQ
//