Full text data of PZP
PZP
(CPAMD6)
[Confidence: low (only semi-automatic identification from reviews)]
Pregnancy zone protein (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 6; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Pregnancy zone protein (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 6; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P20742
ID PZP_HUMAN Reviewed; 1482 AA.
AC P20742; A6ND27; Q15273; Q2NKL2; Q7M4N7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-DEC-2009, sequence version 4.
DT 22-JAN-2014, entry version 128.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT full-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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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
RP 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
RT project: 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;
RP 1056-1061; 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
RT human 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;
RA Sottrup-Jensen L., Sand O., Kristensen L., Fey G.H.;
RT "The alpha-macroglobulin bait region. Sequence diversity and
RT localization of cleavage sites for proteinases in five mammalian
RT alpha-macroglobulins.";
RL J. Biol. Chem. 264:15781-15789(1989).
RN [7]
RP PROTEIN SEQUENCE OF 974-983.
RX PubMed=2415522;
RA Sand O., Folkersen J., Westergaard J.G., Sottrup-Jensen L.;
RT "Characterization of human pregnancy zone protein. Comparison with
RT human 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.,
RA Cassiman J.-J., 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
RT alpha 2M 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.
RT Interactions 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, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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, AND MASS
RP SPECTROMETRY.
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
RT multiple 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.,
RA Buerckstuemmer T., 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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT 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,
CC called the 'bait region' which contains specific cleavage sites
CC for different proteinases. When a proteinase cleaves the bait
CC region, a conformational change is induced in the protein which
CC traps the proteinase. The entrapped enzyme remains active against
CC low molecular weight substrates (activity against high molecular
CC weight substrates is greatly reduced). Following cleavage in the
CC bait region a thioester bond is hydrolyzed and mediates the
CC covalent binding of the protein to the proteinase.
CC -!- SUBUNIT: Homotetramer, which consists of two pairs of disulfide-
CC linked 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Plasma. Prominent constituent of late-
CC pregnancy sera.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family.
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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 PIR; S13495; S13495.
DR PIR; S29738; S29738.
DR UniGene; Hs.707491; -.
DR ProteinModelPortal; P20742; -.
DR SMR; P20742; 126-226, 1346-1474.
DR STRING; 9606.ENSP00000261336; -.
DR MEROPS; I39.003; -.
DR PhosphoSite; P20742; -.
DR DMDM; 281185515; -.
DR PaxDb; P20742; -.
DR PRIDE; P20742; -.
DR Ensembl; ENST00000261336; ENSP00000261336; ENSG00000126838.
DR Ensembl; ENST00000381997; ENSP00000371427; ENSG00000126838.
DR UCSC; uc001qvl.3; human.
DR GeneCards; GC12M009301; -.
DR H-InvDB; HIX0036869; -.
DR HGNC; HGNC:9750; PZP.
DR HPA; HPA041403; -.
DR HPA; HPA041471; -.
DR MIM; 176420; gene.
DR neXtProt; NX_P20742; -.
DR eggNOG; COG2373; -.
DR HOGENOM; HOG000220939; -.
DR HOVERGEN; HBG000039; -.
DR InParanoid; P20742; -.
DR OMA; WIWELVA; -.
DR OrthoDB; EOG7DJSKB; -.
DR PhylomeDB; P20742; -.
DR PRO; PR:P20742; -.
DR ArrayExpress; P20742; -.
DR Bgee; P20742; -.
DR Genevestigator; P20742; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007565; P:female pregnancy; TAS:UniProtKB.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR011626; A2M_comp.
DR InterPro; IPR002890; A2M_N.
DR InterPro; IPR011625; A2M_N_2.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR010916; TonB_box_CS.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07678; A2M_comp; 1.
DR Pfam; PF01835; A2M_N; 1.
DR Pfam; PF07703; A2M_N_2; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF10569; Thiol-ester_cl; 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; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Polymorphism;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1 25
FT CHAIN 26 1482 Pregnancy zone protein.
FT /FTId=PRO_0000000063.
FT REGION 685 735 Bait region.
FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 69 69 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 246 246 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 392 392 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 406 406 N-linked (GlcNAc...).
FT CARBOHYD 753 753 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 875 875 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 932 932 N-linked (GlcNAc...).
FT CARBOHYD 997 997 N-linked (GlcNAc...).
FT CARBOHYD 1430 1430 N-linked (GlcNAc...).
FT CROSSLNK 978 981 Isoglutamyl cysteine thioester (Cys-Gln).
FT VAR_SEQ 1 131 Missing (in isoform 2).
FT /FTId=VSP_030862.
FT VAR_SEQ 132 142 TDKPMYKPGQT -> MSESYRRTTFP (in isoform
FT 2).
FT /FTId=VSP_030863.
FT VAR_SEQ 830 912 Missing (in isoform 2).
FT /FTId=VSP_030864.
FT VARIANT 379 379 L -> V (in dbSNP:rs12230214).
FT /FTId=VAR_034429.
FT VARIANT 691 691 V -> M (in dbSNP:rs3213832).
FT /FTId=VAR_021845.
FT VARIANT 813 813 V -> A (in dbSNP:rs2277413).
FT /FTId=VAR_020005.
FT VARIANT 857 857 N -> S (in dbSNP:rs3213831).
FT /FTId=VAR_060733.
FT VARIANT 1003 1003 T -> M (in dbSNP:rs57006764).
FT /FTId=VAR_060982.
FT VARIANT 1128 1128 R -> H (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036235.
FT VARIANT 1205 1205 T -> P (in dbSNP:rs2377741).
FT /FTId=VAR_060734.
FT VARIANT 1443 1443 I -> N (in dbSNP:rs10842971).
FT /FTId=VAR_024358.
FT CONFLICT 753 753 N -> Q (in Ref. 6; AA sequence).
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
//
ID PZP_HUMAN Reviewed; 1482 AA.
AC P20742; A6ND27; Q15273; Q2NKL2; Q7M4N7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-DEC-2009, sequence version 4.
DT 22-JAN-2014, entry version 128.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT full-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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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
RP 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
RT project: 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;
RP 1056-1061; 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
RT human 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;
RA Sottrup-Jensen L., Sand O., Kristensen L., Fey G.H.;
RT "The alpha-macroglobulin bait region. Sequence diversity and
RT localization of cleavage sites for proteinases in five mammalian
RT alpha-macroglobulins.";
RL J. Biol. Chem. 264:15781-15789(1989).
RN [7]
RP PROTEIN SEQUENCE OF 974-983.
RX PubMed=2415522;
RA Sand O., Folkersen J., Westergaard J.G., Sottrup-Jensen L.;
RT "Characterization of human pregnancy zone protein. Comparison with
RT human 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.,
RA Cassiman J.-J., 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
RT alpha 2M 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.
RT Interactions 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, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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, AND MASS
RP SPECTROMETRY.
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
RT multiple 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.,
RA Buerckstuemmer T., 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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT 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,
CC called the 'bait region' which contains specific cleavage sites
CC for different proteinases. When a proteinase cleaves the bait
CC region, a conformational change is induced in the protein which
CC traps the proteinase. The entrapped enzyme remains active against
CC low molecular weight substrates (activity against high molecular
CC weight substrates is greatly reduced). Following cleavage in the
CC bait region a thioester bond is hydrolyzed and mediates the
CC covalent binding of the protein to the proteinase.
CC -!- SUBUNIT: Homotetramer, which consists of two pairs of disulfide-
CC linked 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Plasma. Prominent constituent of late-
CC pregnancy sera.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family.
CC -----------------------------------------------------------------------
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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 PIR; S13495; S13495.
DR PIR; S29738; S29738.
DR UniGene; Hs.707491; -.
DR ProteinModelPortal; P20742; -.
DR SMR; P20742; 126-226, 1346-1474.
DR STRING; 9606.ENSP00000261336; -.
DR MEROPS; I39.003; -.
DR PhosphoSite; P20742; -.
DR DMDM; 281185515; -.
DR PaxDb; P20742; -.
DR PRIDE; P20742; -.
DR Ensembl; ENST00000261336; ENSP00000261336; ENSG00000126838.
DR Ensembl; ENST00000381997; ENSP00000371427; ENSG00000126838.
DR UCSC; uc001qvl.3; human.
DR GeneCards; GC12M009301; -.
DR H-InvDB; HIX0036869; -.
DR HGNC; HGNC:9750; PZP.
DR HPA; HPA041403; -.
DR HPA; HPA041471; -.
DR MIM; 176420; gene.
DR neXtProt; NX_P20742; -.
DR eggNOG; COG2373; -.
DR HOGENOM; HOG000220939; -.
DR HOVERGEN; HBG000039; -.
DR InParanoid; P20742; -.
DR OMA; WIWELVA; -.
DR OrthoDB; EOG7DJSKB; -.
DR PhylomeDB; P20742; -.
DR PRO; PR:P20742; -.
DR ArrayExpress; P20742; -.
DR Bgee; P20742; -.
DR Genevestigator; P20742; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007565; P:female pregnancy; TAS:UniProtKB.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR011626; A2M_comp.
DR InterPro; IPR002890; A2M_N.
DR InterPro; IPR011625; A2M_N_2.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR010916; TonB_box_CS.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07678; A2M_comp; 1.
DR Pfam; PF01835; A2M_N; 1.
DR Pfam; PF07703; A2M_N_2; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF10569; Thiol-ester_cl; 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; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Polymorphism;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1 25
FT CHAIN 26 1482 Pregnancy zone protein.
FT /FTId=PRO_0000000063.
FT REGION 685 735 Bait region.
FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 69 69 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 246 246 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 392 392 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 406 406 N-linked (GlcNAc...).
FT CARBOHYD 753 753 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 875 875 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 932 932 N-linked (GlcNAc...).
FT CARBOHYD 997 997 N-linked (GlcNAc...).
FT CARBOHYD 1430 1430 N-linked (GlcNAc...).
FT CROSSLNK 978 981 Isoglutamyl cysteine thioester (Cys-Gln).
FT VAR_SEQ 1 131 Missing (in isoform 2).
FT /FTId=VSP_030862.
FT VAR_SEQ 132 142 TDKPMYKPGQT -> MSESYRRTTFP (in isoform
FT 2).
FT /FTId=VSP_030863.
FT VAR_SEQ 830 912 Missing (in isoform 2).
FT /FTId=VSP_030864.
FT VARIANT 379 379 L -> V (in dbSNP:rs12230214).
FT /FTId=VAR_034429.
FT VARIANT 691 691 V -> M (in dbSNP:rs3213832).
FT /FTId=VAR_021845.
FT VARIANT 813 813 V -> A (in dbSNP:rs2277413).
FT /FTId=VAR_020005.
FT VARIANT 857 857 N -> S (in dbSNP:rs3213831).
FT /FTId=VAR_060733.
FT VARIANT 1003 1003 T -> M (in dbSNP:rs57006764).
FT /FTId=VAR_060982.
FT VARIANT 1128 1128 R -> H (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036235.
FT VARIANT 1205 1205 T -> P (in dbSNP:rs2377741).
FT /FTId=VAR_060734.
FT VARIANT 1443 1443 I -> N (in dbSNP:rs10842971).
FT /FTId=VAR_024358.
FT CONFLICT 753 753 N -> Q (in Ref. 6; AA sequence).
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
//
MIM
176420
*RECORD*
*FIELD* NO
176420
*FIELD* TI
*176420 PREGNANCY ZONE PROTEIN; PZP
;;COMPLEMENT COMPONENT 3- AND PREGNANCY ZONE PROTEIN-LIKE ALPHA-2-MACROGLOBULIN
read moreDOMAIN-CONTAINING PROTEIN 6; CPAMD6;;
C3- AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PROTEIN 6
*FIELD* TX
GENE FUNCTION
Pregnancy zone protein (PZP), one of the major pregnancy-associated
plasma proteins (see 260100 for another example), was described by
Smithies (1959), who used zone-electrophoresis in starch gels. PZP is a
prominent constituent of late-pregnancy sera. In healthy, nonpregnant
females and in males, PZP is present in trace amounts only: females,
10-30 mg/l; males, less than 10 mg/l. During pregnancy, PZP levels may
reach 1000-1400 mg/l just before term.
Sottrup-Jensen et al. (1984) showed that PZP closely resembles
alpha-2-macroglobulin (103950) in structure. Both have a quaternary
structure of 2 covalently bound 180-kD subunits which are further
noncovalently assembled into a tetramer of 720 kD. Amino acid sequence
of the 2 proteins are extensively homologous.
MAPPING
Marynen et al. (1989) used in situ hybridization and somatic cell hybrid
DNA analysis to demonstrate that PZP, alpha-2-macroglobulin, and an
alpha-2-macroglobulin pseudogene mapped to human chromosome 12p13-p12.2.
*FIELD* RF
1. Marynen, P.; Zhang, J.; Devriendt, K.; Cassiman, J.-J.: Alpha-2-macroglobulin,
pregnancy zone protein and an alpha-2-macroglobulin pseudogene map
to chromosome 12p12.2-13. (Abstract) Cytogenet. Cell Genet. 51:
1040 only, 1989.
2. Smithies, O.: Zone electrophoresis in starch gels and its application
to studies of serum proteins. Adv. Protein Chem. 14: 65-113, 1959.
3. Sottrup-Jensen, L.; Folkersen, J.; Kristensen, T.; Tack, B. F.
: Partial primary structure of human pregnancy zone protein: extensive
sequence homology with human alpha-2-macroglobulin. Proc. Nat. Acad.
Sci. 81: 7353-7357, 1984.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
alopez: 09/14/2010
supermim: 3/16/1992
supermim: 3/20/1990
carol: 12/12/1989
ddp: 10/27/1989
root: 6/30/1989
root: 5/31/1989
*RECORD*
*FIELD* NO
176420
*FIELD* TI
*176420 PREGNANCY ZONE PROTEIN; PZP
;;COMPLEMENT COMPONENT 3- AND PREGNANCY ZONE PROTEIN-LIKE ALPHA-2-MACROGLOBULIN
read moreDOMAIN-CONTAINING PROTEIN 6; CPAMD6;;
C3- AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PROTEIN 6
*FIELD* TX
GENE FUNCTION
Pregnancy zone protein (PZP), one of the major pregnancy-associated
plasma proteins (see 260100 for another example), was described by
Smithies (1959), who used zone-electrophoresis in starch gels. PZP is a
prominent constituent of late-pregnancy sera. In healthy, nonpregnant
females and in males, PZP is present in trace amounts only: females,
10-30 mg/l; males, less than 10 mg/l. During pregnancy, PZP levels may
reach 1000-1400 mg/l just before term.
Sottrup-Jensen et al. (1984) showed that PZP closely resembles
alpha-2-macroglobulin (103950) in structure. Both have a quaternary
structure of 2 covalently bound 180-kD subunits which are further
noncovalently assembled into a tetramer of 720 kD. Amino acid sequence
of the 2 proteins are extensively homologous.
MAPPING
Marynen et al. (1989) used in situ hybridization and somatic cell hybrid
DNA analysis to demonstrate that PZP, alpha-2-macroglobulin, and an
alpha-2-macroglobulin pseudogene mapped to human chromosome 12p13-p12.2.
*FIELD* RF
1. Marynen, P.; Zhang, J.; Devriendt, K.; Cassiman, J.-J.: Alpha-2-macroglobulin,
pregnancy zone protein and an alpha-2-macroglobulin pseudogene map
to chromosome 12p12.2-13. (Abstract) Cytogenet. Cell Genet. 51:
1040 only, 1989.
2. Smithies, O.: Zone electrophoresis in starch gels and its application
to studies of serum proteins. Adv. Protein Chem. 14: 65-113, 1959.
3. Sottrup-Jensen, L.; Folkersen, J.; Kristensen, T.; Tack, B. F.
: Partial primary structure of human pregnancy zone protein: extensive
sequence homology with human alpha-2-macroglobulin. Proc. Nat. Acad.
Sci. 81: 7353-7357, 1984.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
alopez: 09/14/2010
supermim: 3/16/1992
supermim: 3/20/1990
carol: 12/12/1989
ddp: 10/27/1989
root: 6/30/1989
root: 5/31/1989