PZP_MOUSE
ID PZP_MOUSE Reviewed; 1495 AA.
AC Q61838; E9QPW0; Q60628; Q6PEM2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Pregnancy zone protein;
DE AltName: Full=Alpha-2-macroglobulin;
DE Short=Alpha-2-M;
DE Contains:
DE RecName: Full=Alpha-2-macroglobulin 165 kDa subunit;
DE Contains:
DE RecName: Full=Alpha-2-macroglobulin 35 kDa subunit;
DE Flags: Precursor;
GN Name=Pzp; Synonyms=A2m;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-44 AND 1240-1259.
RC TISSUE=Liver;
RX PubMed=1280217; DOI=10.1111/j.1432-1033.1992.tb17424.x;
RA van Leuven F., Torrekens S., Overbergh L., Lorent K., de Strooper B.,
RA van den Berghe H.;
RT "The primary sequence and the subunit structure of mouse alpha-2-
RT macroglobulin, deduced from protein sequencing of the isolated subunits and
RT from molecular cloning of the cDNA.";
RL Eur. J. Biochem. 210:319-327(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-161.
RC STRAIN=129/J;
RX PubMed=7528166; DOI=10.1006/geno.1994.1425;
RA Umans L., Serneels L., Hilliker C., Stas L., Overbergh L., de Strooper B.,
RA van Leuven F., van den Berghe H.;
RT "Molecular cloning of the mouse gene coding for alpha 2-macroglobulin and
RT targeting of the gene in embryonic stem cells.";
RL Genomics 22:519-529(1994).
RN [5]
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=15355875; DOI=10.1095/biolreprod.104.029835;
RA He H., McCartney D.J., Wei Q., Esadeg S., Zhang J., Foster R.A.,
RA Hayes M.A., Tayade C., Van Leuven F., Croy B.A.;
RT "Characterization of a murine alpha 2 macroglobulin gene expressed in
RT reproductive and cardiovascular tissue.";
RL Biol. Reprod. 72:266-275(2005).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157; ASN-405; ASN-412;
RP ASN-1003; ASN-1385 AND ASN-1443.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157; ASN-568; ASN-881;
RP ASN-1003; ASN-1385 AND ASN-1443.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highest expression in liver, medium expression in
CC ovary, heart and stomach. Low expression in lung, kidney and uterus.
CC Protein found in plasma. {ECO:0000269|PubMed:15355875}.
CC -!- DEVELOPMENTAL STAGE: Unlike the rat protein, which is an acute phase
CC protein, this protein is always in circulation at high levels.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39508.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M93264; AAA39508.1; ALT_FRAME; mRNA.
DR EMBL; AC123060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057983; AAH57983.1; -; mRNA.
DR EMBL; U06977; AAA87890.1; -; Genomic_DNA.
DR CCDS; CCDS39650.1; -.
DR PIR; S27001; S27001.
DR AlphaFoldDB; Q61838; -.
DR SMR; Q61838; -.
DR BioGRID; 197897; 3.
DR IntAct; Q61838; 3.
DR MINT; Q61838; -.
DR STRING; 10090.ENSMUSP00000032510; -.
DR MEROPS; I39.004; -.
DR CarbonylDB; Q61838; -.
DR GlyConnect; 675; 9 N-Linked glycans (5 sites).
DR GlyGen; Q61838; 11 sites, 14 N-linked glycans (5 sites).
DR iPTMnet; Q61838; -.
DR PhosphoSitePlus; Q61838; -.
DR SwissPalm; Q61838; -.
DR CPTAC; non-CPTAC-3606; -.
DR jPOST; Q61838; -.
DR MaxQB; Q61838; -.
DR PaxDb; Q61838; -.
DR PeptideAtlas; Q61838; -.
DR PRIDE; Q61838; -.
DR ProteomicsDB; 301900; -.
DR Ensembl; ENSMUST00000112132; ENSMUSP00000107760; ENSMUSG00000030359.
DR UCSC; uc009eef.1; mouse.
DR MGI; MGI:87854; Pzp.
DR VEuPathDB; HostDB:ENSMUSG00000030359; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000163775; -.
DR HOGENOM; CLU_001634_0_1_1; -.
DR InParanoid; Q61838; -.
DR OMA; EMFPVVY; -.
DR OrthoDB; 354230at2759; -.
DR ChiTaRS; Pzp; mouse.
DR PRO; PR:Q61838; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q61838; protein.
DR Bgee; ENSMUSG00000030359; Expressed in left lobe of liver and 59 other tissues.
DR ExpressionAtlas; Q61838; baseline and differential.
DR Genevisible; Q61838; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0048403; F:brain-derived neurotrophic factor binding; ISO:MGI.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:MGI.
DR GO; GO:0048406; F:nerve growth factor binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007566; P:embryo implantation; IGI:MGI.
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 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 Bait region; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1495
FT /note="Pregnancy zone protein"
FT /id="PRO_0000338413"
FT CHAIN 25..1239
FT /note="Alpha-2-macroglobulin 165 kDa subunit"
FT /id="PRO_0000000056"
FT CHAIN 1240..1495
FT /note="Alpha-2-macroglobulin 35 kDa subunit"
FT /id="PRO_0000000057"
FT REGION 686..744
FT /note="Bait region"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1003
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 1385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 1443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT DISULFID 48..86
FT /evidence="ECO:0000250"
FT DISULFID 249..298
FT /evidence="ECO:0000250"
FT DISULFID 267..286
FT /evidence="ECO:0000250"
FT DISULFID 277
FT /note="Interchain (with C-430)"
FT /evidence="ECO:0000250"
FT DISULFID 430
FT /note="Interchain (with C-277)"
FT /evidence="ECO:0000250"
FT DISULFID 469..562
FT /evidence="ECO:0000250"
FT DISULFID 594..783
FT /evidence="ECO:0000250"
FT DISULFID 642..689
FT /evidence="ECO:0000250"
FT DISULFID 833..861
FT /evidence="ECO:0000250"
FT DISULFID 859..895
FT /evidence="ECO:0000250"
FT DISULFID 933..1339
FT /evidence="ECO:0000250"
FT DISULFID 1092..1140
FT /evidence="ECO:0000250"
FT CROSSLNK 984..987
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT CONFLICT 43
FT /note="V -> I (in Ref. 1; AAA39508, 3; AAH57983 and 4;
FT AAA87890)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="I -> V (in Ref. 4; AAA87890)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..144
FT /note="VKF -> GII (in Ref. 4; AAA87890)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..161
FT /note="FP -> VS (in Ref. 4; AAA87890)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="E -> A (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="R -> S (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="R -> S (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="D -> T (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="F -> G (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="I -> V (in Ref. 3; AAH57983)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="L -> S (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="A -> R (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 890..892
FT /note="QSP -> ESQ (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="W -> S (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 1133
FT /note="A -> V (in Ref. 3; AAH57983)"
FT /evidence="ECO:0000305"
FT CONFLICT 1263..1268
FT /note="HGGFSS -> DGGLLL (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 1284
FT /note="A -> S (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 1298..1299
FT /note="IE -> SR (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 1375
FT /note="G -> E (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
FT CONFLICT 1417
FT /note="K -> R (in Ref. 1; AAA39508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1495 AA; 165853 MW; 5D060D6C639DF3BC CRC64;
MRRNQLPTPA FLLLFLLLPR DATTATAKPQ YVVLVPSEVY SGVPEKACVS LNHVNETVML
SLTLEYAMQQ TKLLTDQAVD KDSFYCSPFT ISGSPLPYTF ITVEIKGPTQ RFIKKKSIQI
IKAESPVFVQ TDKPIYKPGQ IVKFRVVSVD ISFRPLNETF PVVYIETPKR NRIFQWQNIH
LAGGLHQLSF PLSVEPALGI YKVVVQKDSG KKIEHSFEVK EYVLPKFEVI IKMQKTMAFL
EEELPITACG VYTYGKPVPG LVTLRVCRKY SRYRSTCHNQ NSMSICEEFS QQADDKGCFR
QVVKTKVFQL RQKGHDMKIE VEAKIKEEGT GIELTGIGSC EIANALSKLK FTKVNTNYRP
GLPFSGQVLL VDEKGKPIPN KNITSVVSPL GYLSIFTTDE HGLANISIDT SNFTAPFLRV
VVTYKQNHVC YDNWWLDEFH TQADHSATLV FSPSQSYIQL ELVFGTLACG QTQEIRIHYL
LNEDIMKNEK DLTFYYLIKA RGSIFNLGSH VLSLEQGNMK GVFSLPIQVE PGMAPEAQLL
IYAILPNEEL VADAQNFEIE KCFANKVNLS FPSAQSLPAS DTHLKVKAAP LSLCALTAVD
QSVLLLKPEA KLSPQSIYNL LPGKTVQGAF FGVPVYKDHE NCISGEDITH NGIVYTPKHS
LGDNDAHSIF QSVGINIFTN SKIHKPRFCQ EFQHYPAMGG VAPQALAVAA SGPGSSFRAM
GVPMMGLDYS DEINQVVEVR ETVRKYFPET WIWDLVPLDV SGDGELAVKV PDTITEWKAS
AFCLSGTTGL GLSSTISLQA FQPFFLELTL PYSVVRGEAF TLKATVLNYM SHCIQIRVDL
EISPDFLAVP VGGHENSHCI CGNERKTVSW AVTPKSLGEV NFTATAEALQ SPELCGNKLT
EVPALVHKDT VVKSVIVEPE GIEKEQTYNT LLCPQDTELQ DNWSLELPPN VVEGSARATH
SVLGDILGSA MQNLQNLLQM PYGCGEQNMV LFVPNIYVLN YLNETQQLTE AIKSKAINYL
ISGYQRQLNY QHSDGSYSTF GNHGGGNTPG NTWLTAFVLK AFAQAQSHIF IEKTHITNAF
NWLSMKQKEN GCFQQSGYLL NNAMKGGVDD EVTLSAYITI ALLEMPLPVT HSAVRNALFC
LETAWASISQ SQESHVYTKA LLAYAFALAG NKAKRSELLE SLNKDAVKEE DSLHWQRPGD
VQKVKALSFY QPRAPSAEVE MTAYVLLAYL TSESSRPTRD LSSSDLSTAS KIVKWISKQQ
NSHGGFSSTQ DTVVALQALS KYGAATFTRS QKEVLVTIES SGTFSKTFHV NSGNRLLLQE
VRLPDLPGNY VTKGSGSGCV YLQTSLKYNI LPVADGKAPF ALQVNTLPLN FDKAGDHRTF
QIRINVSYTG ERPSSNMVIV DVKMVSGFIP MKPSVKKLQD QPNIQRTEVN TNHVLIYIEK
LTNQTLGFSF AVEQDIPVKN LKPAPIKVYD YYETDEFTVE EYSAPFSDGS EQGNA
