P20742 (PZP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pregnancy zone protein

Alternative name(s):
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 6

Gene names

Name:	PZP
Synonyms:	CPAMD6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1482 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.
Subunit structure	Homotetramer, which consists of two pairs of disulfide-linked chains.
Subcellular location	Secreted.
Tissue specificity	Plasma. Prominent constituent of late-pregnancy sera.
Sequence similarities	Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. [View classification]

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Bait region Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond Glycoprotein Thioester bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	female pregnancy Traceable author statement Ref.9. Source: UniProtKB
Cellular_component	extracellular space Inferred from electronic annotation. Source: InterPro extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB
Molecular_function	endopeptidase inhibitor activity Traceable author statement Ref.6. Source: UniProtKB serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P20742-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P20742-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.
     132-142: TDKPMYKPGQT → MSESYRRTTFP
     830-912: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Ref.4
	Chain	26 – 1482	1457	Pregnancy zone protein		PRO_0000000063
Regions
	Region	685 – 735	51	Bait region
Amino acid modifications
	Glycosylation	24	1	N-linked (GlcNAc...) Potential
	Glycosylation	54	1	N-linked (GlcNAc...) Potential
	Glycosylation	69	1	N-linked (GlcNAc...) Potential
	Glycosylation	246	1	N-linked (GlcNAc...) Potential
	Glycosylation	392	1	N-linked (GlcNAc...) Potential
	Glycosylation	406	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	753	1	N-linked (GlcNAc...) Potential
	Glycosylation	875	1	N-linked (GlcNAc...) Potential
	Glycosylation	932	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	997	1	N-linked (GlcNAc...) Ref.10 Ref.11
	Glycosylation	1430	1	N-linked (GlcNAc...) Ref.10
	Cross-link	978 ↔ 981		Isoglutamyl cysteine thioester (Cys-Gln)
Natural variations
	Alternative sequence	1 – 131	131	Missing in isoform 2.		VSP_030862
	Alternative sequence	132 – 142	11	TDKPMYKPGQT → MSESYRRTTFP in isoform 2.		VSP_030863
	Alternative sequence	830 – 912	83	Missing in isoform 2.		VSP_030864
	Natural variant	379	1	L → V. Corresponds to variant rs12230214 [ dbSNP | Ensembl ].		VAR_034429
	Natural variant	691	1	V → M. Ref.5 Corresponds to variant rs3213832 [ dbSNP | Ensembl ].		VAR_021845
	Natural variant	813	1	V → A. Corresponds to variant rs2277413 [ dbSNP | Ensembl ].		VAR_020005
	Natural variant	857	1	N → S. Ref.1 Corresponds to variant rs3213831 [ dbSNP | Ensembl ].		VAR_060733
	Natural variant	1003	1	T → M. Corresponds to variant rs57006764 [ dbSNP | Ensembl ].		VAR_060982
	Natural variant	1128	1	R → H in a colorectal cancer sample; somatic mutation. Ref.13		VAR_036235
	Natural variant	1205	1	T → P. Ref.3 Corresponds to variant rs2377741 [ dbSNP | Ensembl ].		VAR_060734
	Natural variant	1443	1	I → N. Corresponds to variant rs10842971 [ dbSNP | Ensembl ].		VAR_024358
Experimental info
	Sequence conflict	753	1	N → Q AA sequence Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 15, 2009. Version 4. Checksum: FA89A47458C4A18B	FASTA	1,482	163,863
	10 20 30 40 50 60 MRKDRLLHLC LVLLLILLSA SDSNSTEPQY MVLVPSLLHT EAPKKGCVLL SHLNETVTVS 70 80 90 100 110 120 ASLESGRENR SLFTDLVAEK DLFHCVSFTL PRISASSEVA FLSIQIKGPT QDFRKRNTVL 130 140 150 160 170 180 VLNTQSLVFV QTDKPMYKPG QTVRFRVVSV DENFRPRNEL IPLIYLENPR RNRIAQWQSL 190 200 210 220 230 240 KLEAGINQLS FPLSSEPIQG SYRVVVQTES GGRIQHPFTV EEFVLPKFEV KVQVPKIISI 250 260 270 280 290 300 MDEKVNITVC GEYTYGKPVP GLATVSLCRK LSRVLNCDKQ EVCEEFSQQL NSNGCITQQV 310 320 330 340 350 360 HTKMLQITNT GFEMKLRVEA RIREEGTDLE VTANRISEIT NIVSKLKFVK VDSHFRQGIP 370 380 390 400 410 420 FFAQVLLVDG KGVPIPNKLF FISVNDANYY SNATTNEQGL AQFSINTTSI SVNKLFVRVF 430 440 450 460 470 480 TVHPNLCFHY SWVAEDHQGA QHTANRVFSL SGSYIHLEPV AGTLPCGHTE TITAHYTLNR 490 500 510 520 530 540 QAMGELSELS FHYLIMAKGV IVRSGTHTLP VESGDMKGSF ALSFPVESDV APIARMFIFA 550 560 570 580 590 600 ILPDGEVVGD SEKFEIENCL ANKVDLSFSP AQSPPASHAH LQVAAAPQSL CALRAVDQSV 610 620 630 640 650 660 LLMKPEAELS VSSVYNLLTV KDLTNFPDNV DQQEEEQGHC PRPFFIHNGA IYVPLSSNEA 670 680 690 700 710 720 DIYSFLKGMG LKVFTNSKIR KPKSCSVIPS VSAGAVGQGY YGAGLGVVER PYVPQLGTYN 730 740 750 760 770 780 VIPLNNEQSS GPVPETVRSY FPETWIWELV AVNSSGVAEV GVTVPDTITE WKAGAFCLSE 790 800 810 820 830 840 DAGLGISSTA SLRAFQPFFV ELTMPYSVIR GEVFTLKATV LNYLPKCIRV SVQLKASPAF 850 860 870 880 890 900 LASQNTKGEE SYCICGNERQ TLSWTVTPKT LGNVNFSVSA EAMQSLELCG NEVVEVPEIK 910 920 930 940 950 960 RKDTVIKTLL VEAEGIEQEK TFSSMTCASG ANVSEQLSLK LPSNVVKESA RASFSVLGDI 970 980 990 1000 1010 1020 LGSAMQNIQN LLQMPYGCGE QNMVLFAPNI YVLNYLNETQ QLTQEIKAKA VGYLITGYQR 1030 1040 1050 1060 1070 1080 QLNYKHQDGS YSTFGERYGR NQGNTWLTAF VLKTFAQARS YIFIDEAHIT QSLTWLSQMQ 1090 1100 1110 1120 1130 1140 KDNGCFRSSG SLLNNAIKGG VEDEATLSAY VTIALLEIPL PVTNPIVRNA LFCLESAWNV 1150 1160 1170 1180 1190 1200 AKEGTHGSHV YTKALLAYAF SLLGKQNQNR EILNSLDKEA VKEDNLVHWE RPQRPKAPVG 1210 1220 1230 1240 1250 1260 HLYQTQAPSA EVEMTSYVLL AYLTAQPAPT SGDLTSATNI VKWIMKQQNA QGGFSSTQDT 1270 1280 1290 1300 1310 1320 VVALHALSRY GAATFTRTEK TAQVTVQDSQ TFSTNFQVDN NNLLLLQQIS LPELPGEYVI 1330 1340 1350 1360 1370 1380 TVTGERCVYL QTSMKYNILP EKEDSPFALK VQTVPQTCDG HKAHTSFQIS LTISYTGNRP 1390 1400 1410 1420 1430 1440 ASNMVIVDVK MVSGFIPLKP TVKMLERSSS VSRTEVSNNH VLIYVEQVTN QTLSFSFMVL 1450 1460 1470 1480 QDIPVGDLKP AIVKVYDYYE TDESVVAEYI APCSTDTEHG NV
	Isoform 2 [UniParc]. Checksum: 8D3255FD5698667E	FASTA	1,268	140,368
	10 20 30 40 50 60 MSESYRRTTF PVRFRVVSVD ENFRPRNELI PLIYLENPRR NRIAQWQSLK LEAGINQLSF 70 80 90 100 110 120 PLSSEPIQGS YRVVVQTESG GRIQHPFTVE EFVLPKFEVK VQVPKIISIM DEKVNITVCG 130 140 150 160 170 180 EYTYGKPVPG LATVSLCRKL SRVLNCDKQE VCEEFSQQLN SNGCITQQVH TKMLQITNTG 190 200 210 220 230 240 FEMKLRVEAR IREEGTDLEV TANRISEITN IVSKLKFVKV DSHFRQGIPF FAQVLLVDGK 250 260 270 280 290 300 GVPIPNKLFF ISVNDANYYS NATTNEQGLA QFSINTTSIS VNKLFVRVFT VHPNLCFHYS 310 320 330 340 350 360 WVAEDHQGAQ HTANRVFSLS GSYIHLEPVA GTLPCGHTET ITAHYTLNRQ AMGELSELSF 370 380 390 400 410 420 HYLIMAKGVI VRSGTHTLPV ESGDMKGSFA LSFPVESDVA PIARMFIFAI LPDGEVVGDS 430 440 450 460 470 480 EKFEIENCLA NKVDLSFSPA QSPPASHAHL QVAAAPQSLC ALRAVDQSVL LMKPEAELSV 490 500 510 520 530 540 SSVYNLLTVK DLTNFPDNVD QQEEEQGHCP RPFFIHNGAI YVPLSSNEAD IYSFLKGMGL 550 560 570 580 590 600 KVFTNSKIRK PKSCSVIPSV SAGAVGQGYY GAGLGVVERP YVPQLGTYNV IPLNNEQSSG 610 620 630 640 650 660 PVPETVRSYF PETWIWELVA VNSSGVAEVG VTVPDTITEW KAGAFCLSED AGLGISSTAS 670 680 690 700 710 720 LRAFQPFFVE LTMPYSVIRG EVFTLKATVL NYLPKCIRAE GIEQEKTFSS MTCASGANVS 730 740 750 760 770 780 EQLSLKLPSN VVKESARASF SVLGDILGSA MQNIQNLLQM PYGCGEQNMV LFAPNIYVLN 790 800 810 820 830 840 YLNETQQLTQ EIKAKAVGYL ITGYQRQLNY KHQDGSYSTF GERYGRNQGN TWLTAFVLKT 850 860 870 880 890 900 FAQARSYIFI DEAHITQSLT WLSQMQKDNG CFRSSGSLLN NAIKGGVEDE ATLSAYVTIA 910 920 930 940 950 960 LLEIPLPVTN PIVRNALFCL ESAWNVAKEG THGSHVYTKA LLAYAFSLLG KQNQNREILN 970 980 990 1000 1010 1020 SLDKEAVKED NLVHWERPQR PKAPVGHLYQ TQAPSAEVEM TSYVLLAYLT AQPAPTSGDL 1030 1040 1050 1060 1070 1080 TSATNIVKWI MKQQNAQGGF SSTQDTVVAL HALSRYGAAT FTRTEKTAQV TVQDSQTFST 1090 1100 1110 1120 1130 1140 NFQVDNNNLL LLQQISLPEL PGEYVITVTG ERCVYLQTSM KYNILPEKED SPFALKVQTV 1150 1160 1170 1180 1190 1200 PQTCDGHKAH TSFQISLTIS YTGNRPASNM VIVDVKMVSG FIPLKPTVKM LERSSSVSRT 1210 1220 1230 1240 1250 1260 EVSNNHVLIY VEQVTNQTLS FSFMVLQDIP VGDLKPAIVK VYDYYETDES VVAEYIAPCS TDTEHGNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of pregnancy zone protein. Molecular cloning of a full-length PZP cDNA clone by the polymerase chain reaction." Devriendt K., van den Berghe H., Cassiman J.-J., Marynen P. Biochim. Biophys. Acta 1088:95-103(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-857.
[2]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-1205.
[4]	"Alpha-macroglobulin domain structure studied by specific limited proteolysis." Thomsen N.K., Sottrup-Jensen L. Arch. Biochem. Biophys. 300:327-334(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-37; 222-230; 720-733; 896-902; 1003-1008; 1056-1061; 1184-1193; 1197-1224; 1277-1286 AND 1336-1344 (ISOFORM 1).
[5]	"A genetic polymorphism in a functional domain of human pregnancy zone protein: the bait region. Genomic structure of the bait domains of human pregnancy zone protein and alpha 2 macroglobulin." Marynen P., Devriendt K., van den Berghe H., Cassiman J.-J. FEBS Lett. 262:349-352(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 668-753, VARIANT MET-691. Tissue: Placenta.
[6]	"The alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulins." Sottrup-Jensen L., Sand O., Kristensen L., Fey G.H. J. Biol. Chem. 264:15781-15789(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 670-759.
[7]	"Characterization of human pregnancy zone protein. Comparison with human alpha 2-macroglobulin." Sand O., Folkersen J., Westergaard J.G., Sottrup-Jensen L. J. Biol. Chem. 260:15723-15735(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 974-983.
[8]	"A cluster of alpha 2-macroglobulin-related genes (alpha 2 M) on human chromosome 12p: cloning of the pregnancy-zone protein gene and an alpha 2M pseudogene." Devriendt K., Zhang J., van Leuven F., van den Berghe H., Cassiman J.-J., Marynen P. Gene 81:325-334(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1259-1461.
[9]	"Pregnancy zone protein, a proteinase-binding macroglobulin. Interactions with proteinases and methylamine." Christensen U., Simonsen M., Harrit N., Sottrup-Jensen L. Biochemistry 28:9324-9331(1989) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PROTEINASES AND METHYLAMINE.
[10]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406; ASN-932; ASN-997 AND ASN-1430, MASS SPECTROMETRY. Tissue: Plasma.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-997, MASS SPECTROMETRY. Tissue: Liver.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-1128.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X54380 mRNA. Translation: CAA38255.1. AC010175 Genomic DNA. No translation available. BC111756 mRNA. Translation: AAI11757.1. X51541 Genomic DNA. Translation: CAA35919.1. M24416 Genomic DNA. Translation: AAA60234.1.
IPI	IPI00025426. IPI00884981.
PIR	S13495. S29738.
UniGene	Hs.707491.
3D structure databases
ProteinModelPortal	P20742.
SMR	P20742. Positions 126-226, 1346-1474.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000261336.
Protein family/group databases
MEROPS	I39.003.
PTM databases
PhosphoSite	P20742.
Polymorphism databases
DMDM	281185515.
Proteomic databases
PaxDb	P20742.
PRIDE	P20742.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261336; ENSP00000261336; ENSG00000126838. ENST00000381997; ENSP00000371427; ENSG00000126838.
UCSC	uc001qvl.3. human. uc009zgl.3. human.
Organism-specific databases
GeneCards	GC12M009301.
H-InvDB	HIX0036869.
HGNC	HGNC:9750. PZP.
HPA	HPA041403. HPA041471.
MIM	176420. gene.
neXtProt	NX_P20742.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2373.
HOGENOM	HOG000220939.
HOVERGEN	HBG000039.
InParanoid	P20742.
OMA	WIWELVA.
OrthoDB	EOG4H9XJN.
PhylomeDB	P20742.
Gene expression databases
ArrayExpress	P20742.
Bgee	P20742.
Genevestigator	P20742.
GermOnline	ENSG00000126838. Homo sapiens.
Family and domain databases
Gene3D	2.60.40.690. 1 hit.
InterPro	IPR009048. A-macroglobulin_rcpt-bd. IPR011626. A2M_comp. IPR002890. A2M_N. IPR011625. A2M_N_2. IPR001599. Macroglobln_a2. IPR019742. MacrogloblnA2_CS. IPR019565. MacrogloblnA2_thiol-ester-bond. IPR008930. Terpenoid_cyclase/PrenylTrfase. IPR010916. TonB_box_CS. [Graphical view]
Pfam	PF00207. A2M. 1 hit. PF07678. A2M_comp. 1 hit. PF01835. A2M_N. 1 hit. PF07703. A2M_N_2. 1 hit. PF07677. A2M_recep. 1 hit. PF10569. Thiol-ester_cl. 1 hit. [Graphical view]
SUPFAM	SSF49410. AM_receptor_bind. 1 hit. SSF48239. Terp_cyc_toroid. 1 hit.
PROSITE	PS00477. ALPHA_2_MACROGLOBULIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

PZP_HUMAN

Accession

Primary (citable) accession number: P20742
Secondary accession number(s): A6ND27 , Q15273, Q2NKL2, Q7M4N7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	December 15, 2009
Last modified:	April 3, 2013
This is version 124 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.