CORIN_RAT
ID CORIN_RAT Reviewed; 1111 AA.
AC Q80YN4; D3ZN44; F1LS60;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Atrial natriuretic peptide-converting enzyme;
DE EC=3.4.21.-;
DE AltName: Full=Corin;
DE AltName: Full=Pro-ANP-converting enzyme;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, N-terminal propeptide;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, activated protease fragment;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment;
GN Name=Corin;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=15155264; DOI=10.1152/ajpheart.00947.2003;
RA Langenickel T.H., Pagel I., Buttgereit J., Tenner K., Lindner M., Dietz R.,
RA Willenbrock R., Bader M.;
RT "Rat corin gene: molecular cloning and reduced expression in experimental
RT heart failure.";
RL Am. J. Physiol. 287:H1516-H1521(2004).
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 FUNCTION, ACTIVATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ARG-866;
RP ASN-968 AND ASN-1087, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=17660514; DOI=10.1074/jbc.m703687200;
RA Liao X., Wang W., Chen S., Wu Q.;
RT "Role of glycosylation in corin zymogen activation.";
RL J. Biol. Chem. 282:27728-27735(2007).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20613715; DOI=10.1038/ki.2010.197;
RA Polzin D., Kaminski H.J., Kastner C., Wang W., Kramer S., Gambaryan S.,
RA Russwurm M., Peters H., Wu Q., Vandewalle A., Bachmann S., Theilig F.;
RT "Decreased renal corin expression contributes to sodium retention in
RT proteinuric kidney diseases.";
RL Kidney Int. 78:650-659(2010).
CC -!- FUNCTION: Serine-type endopeptidase involved in atrial natriuretic
CC peptide (NPPA) processing (PubMed:17660514). Converts through
CC proteolytic cleavage the non-functional propeptide NPPA into the active
CC hormone, thereby regulating blood pressure in heart and promoting
CC natriuresis, diuresis and vasodilation (By similarity). Proteolytic
CC cleavage of pro-NPPA also plays a role in female pregnancy by promoting
CC trophoblast invasion and spiral artery remodeling in uterus (By
CC similarity). Also acts as a regulator of sodium reabsorption in kidney
CC (PubMed:20613715). May also process pro-NPPB the B-type natriuretic
CC peptide (By similarity). {ECO:0000250|UniProtKB:Q9Y5Q5,
CC ECO:0000250|UniProtKB:Q9Z319, ECO:0000269|PubMed:17660514,
CC ECO:0000269|PubMed:20613715}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein. Cytoplasmic vesicle.
CC -!- SUBCELLULAR LOCATION: [Atrial natriuretic peptide-converting enzyme,
CC 180 kDa soluble fragment]: Secreted {ECO:0000250}. Note=Soluble form
CC produced following cleavage by ADAM10. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in heart. Also detected in
CC kidney, aorta, brain and testis. In kidney, present in epithelial
CC cells, with segmental expression in the proximal tubule, thick
CC ascending limb, connecting tubule, and throughout the collecting duct
CC (at protein level). {ECO:0000269|PubMed:15155264}.
CC -!- INDUCTION: Down-regulated upon experimental heart failure.
CC {ECO:0000269|PubMed:15155264}.
CC -!- PTM: N-glycosylated; required for processing and activation.
CC {ECO:0000269|PubMed:17660514}.
CC -!- PTM: Activated through proteolytic processing by a trypsin-like
CC protease; cleaved into a N-terminal propeptide and an activated corin
CC protease fragment. Atrial natriuretic peptide-converting enzyme, 180
CC kDa soluble fragment is produced by cleavage by ADAM10. Cleavage by
CC ADAM10 to produce soluble 180 kDa soluble fragment takes place after
CC the transmembrane region and before FZ 1 (Probable).
CC {ECO:0000305|PubMed:17660514}.
CC -!- PTM: A disulfide bond links the activated corin protease fragment and
CC the N-terminal propeptide. The disulfide bond also links the activated
CC corin protease fragment with Atrial natriuretic peptide-converting
CC enzyme, 180 kDa soluble fragment (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AY251285; AAO86772.1; -; mRNA.
DR EMBL; AC121481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_872279.1; NM_182473.1.
DR AlphaFoldDB; Q80YN4; -.
DR SMR; Q80YN4; -.
DR STRING; 10116.ENSRNOP00000061602; -.
DR MEROPS; S01.019; -.
DR GlyGen; Q80YN4; 5 sites.
DR PaxDb; Q80YN4; -.
DR GeneID; 289596; -.
DR KEGG; rno:289596; -.
DR UCSC; RGD:727887; rat.
DR CTD; 10699; -.
DR RGD; 727887; Corin.
DR eggNOG; KOG3577; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q80YN4; -.
DR OrthoDB; 1314811at2759; -.
DR Reactome; R-RNO-5578768; Physiological factors.
DR PRO; PR:Q80YN4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; ISS:UniProtKB.
DR GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
DR GO; GO:0035813; P:regulation of renal sodium excretion; IMP:UniProtKB.
DR GO; GO:0003050; P:regulation of systemic arterial blood pressure by atrial natriuretic peptide; ISS:UniProtKB.
DR CDD; cd07445; CRD_corin_1; 1.
DR CDD; cd07888; CRD_corin_2; 1.
DR CDD; cd00112; LDLa; 7.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 1.10.2000.10; -; 2.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 4.10.400.10; -; 7.
DR InterPro; IPR017052; Corin.
DR InterPro; IPR041762; Corin_CRD_1.
DR InterPro; IPR041763; Corin_CRD_2.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF01392; Fz; 2.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036376; Corin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR SUPFAM; SSF57424; SSF57424; 7.
DR SUPFAM; SSF63501; SSF63501; 2.
DR PROSITE; PS50038; FZ; 2.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zymogen.
FT CHAIN 1..1111
FT /note="Atrial natriuretic peptide-converting enzyme"
FT /id="PRO_0000391762"
FT CHAIN 1..866
FT /note="Atrial natriuretic peptide-converting enzyme, N-
FT terminal propeptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000391763"
FT CHAIN ?..866
FT /note="Atrial natriuretic peptide-converting enzyme, 180
FT kDa soluble fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000417988"
FT CHAIN 867..1111
FT /note="Atrial natriuretic peptide-converting enzyme,
FT activated protease fragment"
FT /evidence="ECO:0000305"
FT /id="PRO_0000391764"
FT TOPO_DOM 1..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..1111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 199..325
FT /note="FZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 334..371
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 371..407
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 407..444
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 444..481
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 516..639
FT /note="FZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 645..681
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 681..719
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 720..756
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 756..851
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 867..1100
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOTIF 93..96
FT /note="DDNN motif"
FT ACT_SITE 908
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 957
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 1050
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT SITE 866..867
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 204..264
FT /evidence="ECO:0000250"
FT DISULFID 212..257
FT /evidence="ECO:0000250"
FT DISULFID 248..288
FT /evidence="ECO:0000250"
FT DISULFID 277..322
FT /evidence="ECO:0000250"
FT DISULFID 281..305
FT /evidence="ECO:0000250"
FT DISULFID 335..348
FT /evidence="ECO:0000250"
FT DISULFID 343..361
FT /evidence="ECO:0000250"
FT DISULFID 355..370
FT /evidence="ECO:0000250"
FT DISULFID 372..384
FT /evidence="ECO:0000250"
FT DISULFID 379..397
FT /evidence="ECO:0000250"
FT DISULFID 391..406
FT /evidence="ECO:0000250"
FT DISULFID 408..421
FT /evidence="ECO:0000250"
FT DISULFID 416..434
FT /evidence="ECO:0000250"
FT DISULFID 428..443
FT /evidence="ECO:0000250"
FT DISULFID 445..458
FT /evidence="ECO:0000250"
FT DISULFID 453..471
FT /evidence="ECO:0000250"
FT DISULFID 465..480
FT /evidence="ECO:0000250"
FT DISULFID 521..584
FT /evidence="ECO:0000250"
FT DISULFID 529..577
FT /evidence="ECO:0000250"
FT DISULFID 568..606
FT /evidence="ECO:0000250"
FT DISULFID 595..636
FT /evidence="ECO:0000250"
FT DISULFID 599..623
FT /evidence="ECO:0000250"
FT DISULFID 646..658
FT /evidence="ECO:0000250"
FT DISULFID 653..671
FT /evidence="ECO:0000250"
FT DISULFID 665..680
FT /evidence="ECO:0000250"
FT DISULFID 682..696
FT /evidence="ECO:0000250"
FT DISULFID 690..709
FT /evidence="ECO:0000250"
FT DISULFID 703..718
FT /evidence="ECO:0000250"
FT DISULFID 721..733
FT /evidence="ECO:0000250"
FT DISULFID 728..746
FT /evidence="ECO:0000250"
FT DISULFID 740..755
FT /evidence="ECO:0000250"
FT DISULFID 855..977
FT /note="Interchain (between N-terminal propeptide and
FT activated protease fragment chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000255|PROSITE-ProRule:PRU00124, ECO:0000255|PROSITE-
FT ProRule:PRU00196, ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 893..909
FT /evidence="ECO:0000250"
FT DISULFID 991..1056
FT /evidence="ECO:0000250"
FT DISULFID 1020..1035
FT /evidence="ECO:0000250"
FT MUTAGEN 866
FT /note="R->A: Impairs proteolytic processing and
FT activation."
FT /evidence="ECO:0000269|PubMed:17660514"
FT MUTAGEN 968
FT /note="N->S: Prevents proteolytic processing and
FT activation; when associated with S-1087."
FT /evidence="ECO:0000269|PubMed:17660514"
FT MUTAGEN 1087
FT /note="N->S: Prevents proteolytic processing and
FT activation; when associated with S-968."
FT /evidence="ECO:0000269|PubMed:17660514"
FT CONFLICT 178
FT /note="P -> S (in Ref. 1; AAO86772)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="R -> T (in Ref. 1; AAO86772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1048
FT /note="I -> G (in Ref. 1; AAO86772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1111 AA; 122757 MW; 44A738ACA6E0AC16 CRC64;
MGRVSFNVRV SSVRRARCSC PGRCYLSCRV PPTTALHALN GFGRAGVLGE TAGGTVGLGP
SGTRGFLSGS KFQASGSLKD CFGAPPAPDV LRADSSVGEG CPQKLVTANL LRFLLLVLIP
CICALIVLLA ILLSFVGTLK KVYFKSNDSE PLVTDGEVRV PGVIHVNRYE NTGAPSMPPS
QSIPAWTPRA PSLEDQSHGN TSTCVNITHR QCQILPYHST LAPLLPIVKN MDTEKFLKFF
TYLHRLGCYQ HILLFGCSLA FPKCIVDGDD RHGLLPCRSF CEAAKEGCES VLGMVNSSWP
DSLRCSQFRY HTENNSDASR ICFSLQQEHG KQSLCGGGES FLCTSGLCIS KKLQCNGYND
CDDWSDEAHC NCSEDLFHCG TGKCLHHSLV CDGYDDCGDL SDEQNCDCNL TKEHRCGDGR
CIAAEWVCDG DHDCVDKSDE VNCSCPSQGL VECRSGQCIP STFQCDGDED CKDGSDEENC
SDRPTPCPGG DRGCLDSSCV ESCAGSSLCD SDSSLSNCSH CEPITLELCM NLPYNLTHYP
NYLGHRTQKE ASISWESALF PALVQTNCYK YLMFFACTIL VPKCDVNTGQ RVPPCRLLCE
HSKERCESVL GIVGLQWPED TDCSQFPEQS SDNQTCLLPN EDVEECSPSH FKCRSGRCVL
GSRRCDGQAD CDDDSDEENC GCKERDLWEC PLNKQCLKHT LICDGFPDCS DSMDEKNCSF
CQDDELECAN HECVPRDLWC DGWTDCSDSS DEWGCVTLSK NGNSSSFLTV HRSARDHHVC
ADGWQETLSQ LACRQMGLGE PSVTELVQGQ EGQQWLRLHS SWENLNGSTL QELLVHRRSC
PSGSEISLLC TKQDCGRRPA ARMNKRILGG RTSRPGRWPW QCSLQSEPSG HICGCVLIAK
KWVLTVAHCF EGREDADVWK VVFGINNLDH PSGFMQTRFV KTILLHPRYS RAVVDYDISV
VELSDDINET SYVRPVCLPS PREFLEPDTY CYITGWGHMG NKMPFKLQEG EVRIIPLEQC
QSYFDMKTIT NRMICAGYES GTVDSCMIDS GGPLVCERPG GQWTLFGLTS WGSVCFSKVL
GPGVYSNVSY FVDWIERQIY IQTFLQKKSQ G
