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   27-MAR-2024, entry version 197.
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; 9.
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   GlyCosmos; P20742; 10 sites, 4 glycans.
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; 9606-ENSP00000261336; -.
DR   PeptideAtlas; P20742; -.
DR   PRIDE; P20742; -.
DR   ProteomicsDB; 53781; -. [P20742-1]
DR   ProteomicsDB; 53782; -. [P20742-2]
DR   Antibodypedia; 42093; 171 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   AGR; HGNC:9750; -.
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; CVKGVPV; -.
DR   OrthoDB; 2970602at2759; -.
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 129 other cell types or tissues.
DR   ExpressionAtlas; P20742; baseline and differential.
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:0005615; C:extracellular space; IBA:GO_Central.
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; 1.50.10.20; -; 1.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.60.120.1540; -; 1.
DR   Gene3D; 2.60.40.1930; -; 2.
DR   Gene3D; 2.60.40.1940; -; 1.
DR   Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR047565; Alpha-macroglob_thiol-ester_cl.
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   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR   PANTHER; PTHR11412:SF92; PREGNANCY ZONE PROTEIN; 1.
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   SMART; SM01419; Thiol-ester_cl; 1.
DR   SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR   Genevisible; P20742; HS.
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
//