PCSK5_MOUSE
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 03-AUG-2022, entry version 193.
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 GlyGen; Q04592; 13 sites.
DR iPTMnet; Q04592; -.
DR PhosphoSitePlus; Q04592; -.
DR MaxQB; Q04592; -.
DR PaxDb; Q04592; -.
DR PeptideAtlas; Q04592; -.
DR PRIDE; Q04592; -.
DR ProteomicsDB; 294032; -. [Q04592-1]
DR ProteomicsDB; 294033; -. [Q04592-2]
DR Antibodypedia; 27199; 205 antibodies from 26 providers.
DR DNASU; 18552; -.
DR Ensembl; ENSMUST00000025618; ENSMUSP00000025618; ENSMUSG00000024713. [Q04592-1]
DR Ensembl; ENSMUST00000050715; ENSMUSP00000050272; ENSMUSG00000024713. [Q04592-2]
DR GeneID; 18552; -.
DR KEGG; mmu:18552; -.
DR UCSC; uc008gxp.2; mouse. [Q04592-1]
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; 518530at2759; -.
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 73 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 252 other tissues.
DR ExpressionAtlas; Q04592; baseline and differential.
DR Genevisible; Q04592; MM.
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:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; 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; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 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 Pfam; PF14843; GF_recep_IV; 2.
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; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR SUPFAM; SSF57184; SSF57184; 8.
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.
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
