PZP_HUMAN
ID PZP_HUMAN Reviewed; 1482 AA.
AC P20742; A6ND27; Q15273; Q2NKL2; Q7M4N7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 4.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Pregnancy zone protein;
DE AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 6;
DE Flags: Precursor;
GN Name=PZP; Synonyms=CPAMD6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-857.
RX PubMed=1989698; DOI=10.1016/0167-4781(91)90157-h;
RA Devriendt K., van den Berghe H., Cassiman J.-J., Marynen P.;
RT "Primary structure of pregnancy zone protein. Molecular cloning of a full-
RT length PZP cDNA clone by the polymerase chain reaction.";
RL Biochim. Biophys. Acta 1088:95-103(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-1205.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 26-37; 222-230; 720-733; 896-902; 1003-1008; 1056-1061;
RP 1184-1193; 1197-1224; 1277-1286 AND 1336-1344 (ISOFORM 1).
RX PubMed=7678727; DOI=10.1006/abbi.1993.1045;
RA Thomsen N.K., Sottrup-Jensen L.;
RT "Alpha-macroglobulin domain structure studied by specific limited
RT proteolysis.";
RL Arch. Biochem. Biophys. 300:327-334(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 668-753, AND VARIANT MET-691.
RC TISSUE=Placenta;
RX PubMed=1692292; DOI=10.1016/0014-5793(90)80226-9;
RA Marynen P., Devriendt K., van den Berghe H., Cassiman J.-J.;
RT "A genetic polymorphism in a functional domain of human pregnancy zone
RT protein: the bait region. Genomic structure of the bait domains of human
RT pregnancy zone protein and alpha 2 macroglobulin.";
RL FEBS Lett. 262:349-352(1990).
RN [6]
RP PROTEIN SEQUENCE OF 670-759.
RX PubMed=2476433; DOI=10.1016/s0021-9258(18)71545-7;
RA Sottrup-Jensen L., Sand O., Kristensen L., Fey G.H.;
RT "The alpha-macroglobulin bait region. Sequence diversity and localization
RT of cleavage sites for proteinases in five mammalian alpha-macroglobulins.";
RL J. Biol. Chem. 264:15781-15789(1989).
RN [7]
RP PROTEIN SEQUENCE OF 974-983.
RX PubMed=2415522; DOI=10.1016/s0021-9258(17)36319-6;
RA Sand O., Folkersen J., Westergaard J.G., Sottrup-Jensen L.;
RT "Characterization of human pregnancy zone protein. Comparison with human
RT alpha 2-macroglobulin.";
RL J. Biol. Chem. 260:15723-15735(1985).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1259-1461.
RX PubMed=2478422; DOI=10.1016/0378-1119(89)90193-5;
RA Devriendt K., Zhang J., van Leuven F., van den Berghe H., Cassiman J.-J.,
RA Marynen P.;
RT "A cluster of alpha 2-macroglobulin-related genes (alpha 2 M) on human
RT chromosome 12p: cloning of the pregnancy-zone protein gene and an alpha 2M
RT pseudogene.";
RL Gene 81:325-334(1989).
RN [9]
RP INTERACTION WITH PROTEINASES AND METHYLAMINE.
RX PubMed=2692707; DOI=10.1021/bi00450a012;
RA Christensen U., Simonsen M., Harrit N., Sottrup-Jensen L.;
RT "Pregnancy zone protein, a proteinase-binding macroglobulin. Interactions
RT with proteinases and methylamine.";
RL Biochemistry 28:9324-9331(1989).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406; ASN-932; ASN-997 AND
RP ASN-1430.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-997.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-1128.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a
CC unique 'trapping' mechanism. This protein has a peptide stretch, called
CC the 'bait region' which contains specific cleavage sites for different
CC proteinases. When a proteinase cleaves the bait region, a
CC conformational change is induced in the protein which traps the
CC proteinase. The entrapped enzyme remains active against low molecular
CC weight substrates (activity against high molecular weight substrates is
CC greatly reduced). Following cleavage in the bait region a thioester
CC bond is hydrolyzed and mediates the covalent binding of the protein to
CC the proteinase.
CC -!- SUBUNIT: Homotetramer, which consists of two pairs of disulfide-linked
CC chains.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P20742-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P20742-2; Sequence=VSP_030862, VSP_030863, VSP_030864;
CC -!- TISSUE SPECIFICITY: Plasma. Prominent constituent of late-pregnancy
CC sera.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000305}.
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DR EMBL; X54380; CAA38255.1; -; mRNA.
DR EMBL; AC010175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111756; AAI11757.1; -; mRNA.
DR EMBL; X51541; CAA35919.1; -; Genomic_DNA.
DR EMBL; M24416; AAA60234.1; -; Genomic_DNA.
DR CCDS; CCDS8600.1; -. [P20742-1]
DR PIR; S13495; S13495.
DR PIR; S29738; S29738.
DR AlphaFoldDB; P20742; -.
DR SMR; P20742; -.
DR BioGRID; 111796; 11.
DR IntAct; P20742; 8.
DR STRING; 9606.ENSP00000261336; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR MEROPS; I39.003; -.
DR GlyConnect; 1623; 4 N-Linked glycans (2 sites).
DR GlyGen; P20742; 10 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; P20742; -.
DR PhosphoSitePlus; P20742; -.
DR BioMuta; PZP; -.
DR DMDM; 281185515; -.
DR CPTAC; non-CPTAC-2688; -.
DR CPTAC; non-CPTAC-2689; -.
DR EPD; P20742; -.
DR jPOST; P20742; -.
DR MassIVE; P20742; -.
DR MaxQB; P20742; -.
DR PaxDb; P20742; -.
DR PeptideAtlas; P20742; -.
DR PRIDE; P20742; -.
DR ProteomicsDB; 53781; -. [P20742-1]
DR ProteomicsDB; 53782; -. [P20742-2]
DR Antibodypedia; 42093; 155 antibodies from 22 providers.
DR Ensembl; ENST00000261336.7; ENSP00000261336.2; ENSG00000126838.10. [P20742-1]
DR MANE-Select; ENST00000261336.7; ENSP00000261336.2; NM_002864.3; NP_002855.2.
DR UCSC; uc001qvl.3; human. [P20742-1]
DR GeneCards; PZP; -.
DR HGNC; HGNC:9750; PZP.
DR HPA; ENSG00000126838; Tissue enriched (liver).
DR MIM; 176420; gene.
DR neXtProt; NX_P20742; -.
DR OpenTargets; ENSG00000126838; -.
DR VEuPathDB; HostDB:ENSG00000126838; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000163609; -.
DR HOGENOM; CLU_001634_0_1_1; -.
DR InParanoid; P20742; -.
DR OMA; ISVCGIY; -.
DR PhylomeDB; P20742; -.
DR TreeFam; TF313285; -.
DR PathwayCommons; P20742; -.
DR SignaLink; P20742; -.
DR SIGNOR; P20742; -.
DR Pharos; P20742; Tbio.
DR PRO; PR:P20742; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P20742; protein.
DR Bgee; ENSG00000126838; Expressed in bronchial epithelial cell and 127 other tissues.
DR ExpressionAtlas; P20742; baseline and differential.
DR Genevisible; P20742; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007565; P:female pregnancy; TAS:UniProtKB.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR041813; A2M_TED.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR010916; TonB_box_CS.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Bait region; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW Secreted; Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1..25
FT CHAIN 26..1482
FT /note="Pregnancy zone protein"
FT /id="PRO_0000000063"
FT REGION 685..735
FT /note="Bait region"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 997
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 1430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CROSSLNK 978..981
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT VAR_SEQ 1..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030862"
FT VAR_SEQ 132..142
FT /note="TDKPMYKPGQT -> MSESYRRTTFP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030863"
FT VAR_SEQ 830..912
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030864"
FT VARIANT 379
FT /note="L -> V (in dbSNP:rs12230214)"
FT /id="VAR_034429"
FT VARIANT 691
FT /note="V -> M (in dbSNP:rs3213832)"
FT /evidence="ECO:0000269|PubMed:1692292"
FT /id="VAR_021845"
FT VARIANT 813
FT /note="V -> A (in dbSNP:rs2277413)"
FT /id="VAR_020005"
FT VARIANT 857
FT /note="N -> S (in dbSNP:rs3213831)"
FT /evidence="ECO:0000269|PubMed:1989698"
FT /id="VAR_060733"
FT VARIANT 1003
FT /note="T -> M (in dbSNP:rs57006764)"
FT /id="VAR_060982"
FT VARIANT 1128
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs200477595)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036235"
FT VARIANT 1205
FT /note="T -> P (in dbSNP:rs2377741)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060734"
FT VARIANT 1443
FT /note="I -> N (in dbSNP:rs10842971)"
FT /id="VAR_024358"
FT CONFLICT 753
FT /note="N -> Q (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1482 AA; 163863 MW; FA89A47458C4A18B CRC64;
MRKDRLLHLC LVLLLILLSA SDSNSTEPQY MVLVPSLLHT EAPKKGCVLL SHLNETVTVS
ASLESGRENR SLFTDLVAEK DLFHCVSFTL PRISASSEVA FLSIQIKGPT QDFRKRNTVL
VLNTQSLVFV QTDKPMYKPG QTVRFRVVSV DENFRPRNEL IPLIYLENPR RNRIAQWQSL
KLEAGINQLS FPLSSEPIQG SYRVVVQTES GGRIQHPFTV EEFVLPKFEV KVQVPKIISI
MDEKVNITVC GEYTYGKPVP GLATVSLCRK LSRVLNCDKQ EVCEEFSQQL NSNGCITQQV
HTKMLQITNT GFEMKLRVEA RIREEGTDLE VTANRISEIT NIVSKLKFVK VDSHFRQGIP
FFAQVLLVDG KGVPIPNKLF FISVNDANYY SNATTNEQGL AQFSINTTSI SVNKLFVRVF
TVHPNLCFHY SWVAEDHQGA QHTANRVFSL SGSYIHLEPV AGTLPCGHTE TITAHYTLNR
QAMGELSELS FHYLIMAKGV IVRSGTHTLP VESGDMKGSF ALSFPVESDV APIARMFIFA
ILPDGEVVGD SEKFEIENCL ANKVDLSFSP AQSPPASHAH LQVAAAPQSL CALRAVDQSV
LLMKPEAELS VSSVYNLLTV KDLTNFPDNV DQQEEEQGHC PRPFFIHNGA IYVPLSSNEA
DIYSFLKGMG LKVFTNSKIR KPKSCSVIPS VSAGAVGQGY YGAGLGVVER PYVPQLGTYN
VIPLNNEQSS GPVPETVRSY FPETWIWELV AVNSSGVAEV GVTVPDTITE WKAGAFCLSE
DAGLGISSTA SLRAFQPFFV ELTMPYSVIR GEVFTLKATV LNYLPKCIRV SVQLKASPAF
LASQNTKGEE SYCICGNERQ TLSWTVTPKT LGNVNFSVSA EAMQSLELCG NEVVEVPEIK
RKDTVIKTLL VEAEGIEQEK TFSSMTCASG ANVSEQLSLK LPSNVVKESA RASFSVLGDI
LGSAMQNIQN LLQMPYGCGE QNMVLFAPNI YVLNYLNETQ QLTQEIKAKA VGYLITGYQR
QLNYKHQDGS YSTFGERYGR NQGNTWLTAF VLKTFAQARS YIFIDEAHIT QSLTWLSQMQ
KDNGCFRSSG SLLNNAIKGG VEDEATLSAY VTIALLEIPL PVTNPIVRNA LFCLESAWNV
AKEGTHGSHV YTKALLAYAF SLLGKQNQNR EILNSLDKEA VKEDNLVHWE RPQRPKAPVG
HLYQTQAPSA EVEMTSYVLL AYLTAQPAPT SGDLTSATNI VKWIMKQQNA QGGFSSTQDT
VVALHALSRY GAATFTRTEK TAQVTVQDSQ TFSTNFQVDN NNLLLLQQIS LPELPGEYVI
TVTGERCVYL QTSMKYNILP EKEDSPFALK VQTVPQTCDG HKAHTSFQIS LTISYTGNRP
ASNMVIVDVK MVSGFIPLKP TVKMLERSSS VSRTEVSNNH VLIYVEQVTN QTLSFSFMVL
QDIPVGDLKP AIVKVYDYYE TDESVVAEYI APCSTDTEHG NV
