PCSK5_RAT
ID PCSK5_RAT Reviewed; 1809 AA.
AC P41413; D3ZVZ3; Q62914;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 03-AUG-2022, entry version 174.
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/kexin-like protease PC5;
DE Short=rPC5;
DE Flags: Precursor;
GN Name=Pcsk5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PC5A), AND TISSUE SPECIFICITY.
RC TISSUE=Adrenal gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1608-1809 (ISOFORM PC5B).
RC TISSUE=Adrenal gland;
RA De Bie I., Marcinkiewicz M., Nakayama K., Lazure C., Seidah N.G.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10749928; DOI=10.1091/mbc.11.4.1257;
RA Xiang Y., Molloy S.S., Thomas L., Thomas G.;
RT "The PC6B cytoplasmic domain contains two acidic clusters that direct
RT sorting to distinct trans-Golgi network/endosomal compartments.";
RL Mol. Biol. Cell 11:1257-1273(2000).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=9013936; DOI=10.1006/dbio.1996.8402;
RA Zheng M., Seidah N.G., Pintar J.E.;
RT "The developmental expression in the rat CNS and peripheral tissues of
RT proteases PC5 and PACE4 mRNAs: comparison with other proprotein processing
RT enzymes.";
RL Dev. Biol. 181:268-283(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 {ECO:0000250}.
CC Note=Secreted through the regulated secretory pathway. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform PC5B]: Endomembrane system
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Note=Type I membrane protein localized to a paranuclear post-Golgi
CC network compartment in communication with early endosomes.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=PC5B; Synonyms=Long;
CC IsoId=P41413-1; Sequence=Displayed;
CC Name=PC5A; Synonyms=Short;
CC IsoId=P41413-2; Sequence=VSP_005440, VSP_005441;
CC -!- TISSUE SPECIFICITY: Expressed in the intestine, brain, adrenal gland,
CC anterior pituitary, thyroid, ovaries, testis and lung. Highest levels
CC are found in the gut, duodenum, jejunum and ileum. Expression is higher
CC in female than in male reproductive organs.
CC {ECO:0000269|PubMed:8341687}.
CC -!- DEVELOPMENTAL STAGE: First detected at E9 in highly restricted regions
CC of the neural tube, in caudal myotomes, and at the materno-embryonic
CC junction of the uterus. At E10, restricted expression is detected in
CC the optic and otic vesicles, the roof of midbrain, and trunk myotomes.
CC By midgestation (E13-E16), expression in the developing nervous system
CC has expanded to multiple regions including hippocampus, thalamus,
CC hypothalamus, brain stem, and spinal cord. Expression is also detected
CC in several peripheral organ systems, including gut, lung, adrenal and
CC kydney primordia. {ECO:0000269|PubMed:9013936}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L14933; AAA99906.2; -; mRNA.
DR EMBL; U47014; AAA87888.1; -; mRNA.
DR PIR; B48225; B48225.
DR RefSeq; NP_446275.1; NM_053823.1. [P41413-2]
DR AlphaFoldDB; P41413; -.
DR SMR; P41413; -.
DR IntAct; P41413; 1.
DR STRING; 10116.ENSRNOP00000016164; -.
DR MEROPS; S08.076; -.
DR GlyGen; P41413; 8 sites.
DR jPOST; P41413; -.
DR PaxDb; P41413; -.
DR PRIDE; P41413; -.
DR Ensembl; ENSRNOT00000016164; ENSRNOP00000016164; ENSRNOG00000012036. [P41413-2]
DR GeneID; 116548; -.
DR KEGG; rno:116548; -.
DR UCSC; RGD:620326; rat. [P41413-1]
DR CTD; 5125; -.
DR RGD; 620326; Pcsk5.
DR VEuPathDB; HostDB:ENSRNOG00000012036; -.
DR eggNOG; KOG3525; Eukaryota.
DR GeneTree; ENSGT00940000155770; -.
DR HOGENOM; CLU_002976_3_0_1; -.
DR InParanoid; P41413; -.
DR OMA; NTHHIDI; -.
DR OrthoDB; 473018at2759; -.
DR BRENDA; 3.4.21.B26; 5301.
DR Reactome; R-RNO-167060; NGF processing.
DR Reactome; R-RNO-8963889; Assembly of active LPL and LIPC lipase complexes.
DR PRO; PR:P41413; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012036; Expressed in esophagus and 17 other tissues.
DR Genevisible; P41413; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:1990635; C:proximal dendrite; IDA:RGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0042277; F:peptide binding; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR GO; GO:0003279; P:cardiac septum development; ISO:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR GO; GO:0140447; P:cytokine precursor processing; ISO:RGD.
DR GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
DR GO; GO:0007566; P:embryo implantation; ISO:RGD.
DR GO; GO:0048566; P:embryonic digestive tract development; ISO:RGD.
DR GO; GO:0048706; P:embryonic skeletal system development; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0035108; P:limb morphogenesis; ISO:RGD.
DR GO; GO:0043043; P:peptide biosynthetic process; ISO:RGD.
DR GO; GO:0016486; P:peptide hormone processing; ISO:RGD.
DR GO; GO:0033625; P:positive regulation of integrin activation; IMP:RGD.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IMP:RGD.
DR GO; GO:1905609; P:positive regulation of smooth muscle cell-matrix adhesion; IMP:RGD.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IMP:RGD.
DR GO; GO:0016485; P:protein processing; ISO:RGD.
DR GO; GO:0002001; P:renin secretion into blood stream; ISO:RGD.
DR GO; GO:0030323; P:respiratory tube development; ISO:RGD.
DR GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
DR GO; GO:0034699; P:response to luteinizing hormone; IEP:RGD.
DR GO; GO:0006465; P:signal peptide processing; ISO:RGD.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEP:RGD.
DR GO; GO:0019058; P:viral life cycle; ISO:RGD.
DR CDD; cd00064; FU; 18.
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; IPR043601; Rspo_Fu-CRD_dom.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR Pfam; PF15913; Furin-like_2; 1.
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; 16.
DR SMART; SM00261; FU; 21.
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 2: Evidence at transcript level;
KW Alternative splicing; Cleavage on pair of basic residues; Glycoprotein;
KW Hydrolase; Membrane; Pregnancy; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Transmembrane; Transmembrane helix;
KW Zymogen.
FT SIGNAL 1..34
FT /evidence="ECO:0000250"
FT PROPEP 35..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000027106"
FT CHAIN 117..1809
FT /note="Proprotein convertase subtilisin/kexin type 5"
FT /id="PRO_0000027107"
FT TOPO_DOM 117..1700
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1701..1721
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1722..1809
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..964
FT /note="FU 7"
FT REPEAT 965..1010
FT /note="FU 8"
FT REPEAT 1012..1054
FT /note="FU 9"
FT REPEAT 1058..1099
FT /note="FU 10"
FT REPEAT 1137..1179
FT /note="FU 11"
FT REPEAT 1183..1230
FT /note="FU 12"
FT REPEAT 1232..1276
FT /note="FU 13"
FT REPEAT 1278..1321
FT /note="FU 14"
FT REPEAT 1323..1369
FT /note="FU 15"
FT REPEAT 1373..1418
FT /note="FU 16"
FT REPEAT 1422..1467
FT /note="FU 17"
FT REPEAT 1471..1516
FT /note="FU 18"
FT REPEAT 1520..1567
FT /note="FU 19"
FT REPEAT 1571..1616
FT /note="FU 20"
FT REPEAT 1622..1669
FT /note="FU 21"
FT REGION 638..1685
FT /note="CRM (Cys-rich motif)"
FT REGION 1757..1776
FT /note="AC 1"
FT REGION 1788..1809
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 1642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 878..915
FT /note="GEYIDEQGHCQICDASCAKCWGPTQDDCISCPITRVFD -> ATEESWAEGG
FT FCMLVKKNNLCQRKVLQQLCCKTCTFQG (in isoform PC5A)"
FT /evidence="ECO:0000303|PubMed:8341687"
FT /id="VSP_005440"
FT VAR_SEQ 916..1809
FT /note="Missing (in isoform PC5A)"
FT /evidence="ECO:0000303|PubMed:8341687"
FT /id="VSP_005441"
SQ SEQUENCE 1809 AA; 201308 MW; 726855D09F929ADE CRC64;
MDWGWGSRCC RPGRRDLLCV LALLAGCLLP VCRTRVYTNH WAVKIAGGFA EADRIASKYG
FINVGQIGAL KDYYHFYHSR TIKRSVLSSR GTHSFISMEP KVEWIQQQVV KKRTKRDYDL
SRAQSTYFND 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 GPDHCTDCLH
YHYKLKNNTR ICVSSCPPGH FHADKKRCRK CAPNCESCFG SHADQCLSCK YGYFLNEETS
SCVAQCPEGS YQDIKKNICG KCSENCKTCT GFHNCTECKG GLSLQGSRCS VTCEDGQFFS
GHDCQPCHRF CATCAGAGAD GCINCTEGYV MEEGRCVQSC SVSYYLDHSL EGGYKSCKRC
DNSCLTCNGP GFKNCSSCPS GYLLDLGMCQ MGAICKDGEY IDEQGHCQIC DASCAKCWGP
TQDDCISCPI TRVFDDGRCV MNCPSWKFEL KKQCHPCHHT CQGCQGSGPS NCTSCKAGEF
QDSEYGECMP CEEGCVGCTV DDPGACTSCA TGYYMFERHC YKACPEKTFG EKWECKACGT
NCGSCDQHEC YWCEEGFFLS SGSCVQDCDP GFYGDQELGE CKPCHRACET CTGLGYNQCS
SCPEGLQLWH GTCIWPTWPH VEGKVWNEAV PTEKPSLVRS LPQDRRKWKV QIKRDATRQY
QPCHSSCKTC NGSLCTSCPA GTYLWLQACV PSCPQGTWLS VRSSSCEKCA EGCASCSGDD
LCQRCLSQPS NTLLLHEGRC YHSCPEGFYA KDGVCEHCSS PCKTCKGNAT SCHSCEGDFV
LDHGVCWETC PEKHVAVEGV CKHCPERCQD CIHEKTCKEC MPDFFLYNDM CHHSCPKNFY
PDMRQCVPCH KNCLGCNGPK EDDCKACADT SKVLHNGLCL DECPKGTYKD EVNDECRDCP
ESCLICSSAW TCLTCREGFT VVQDVCTAPK ECAAIEYWDV GSHRCQPCHR KCSRCSGPSE
NQCYTCPRET FLLNTTCVKE CPEGYHTDKD SHQCVPCHSS CRTCEGPHSM QCLSCRPGWF
QLGKECLLQC RDGYYGESTS GRCEKCDKSC KTCRGPQPTD CQSCDTFFFL LRSKGQCHLA
CPEHYYADQH AQTCERCHPT CDKCSGKEAW NCLSCVWSYH LLKGICTPEC IVGEYRDGKG
ENFNCKKCHE SCMECKGPGS KNCTGCSAGL LLQMDDSRCL RCCNASHPHR SQDCCDCQSS
TDECILPASD DTVFHEHTKT ALLVTSGAML LLLLGAAVVV WRKSRSQPVA KGRYEKLAEP
TVSYSSYRSS YLDEDQVIEY RDRDYDEDDE DDIVYMGQDG TVYRKFKYGL LDEAEDDELE
YDDESYSYQ
