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Q9BXP8 (PAPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pappalysin-2

EC=3.4.24.-
Alternative name(s):
Pregnancy-associated plasma protein A2
Short name=PAPP-A2
Pregnancy-associated plasma protein E1
Short name=PAPP-E
Gene names
Name:PAPPA2
Synonyms:PLAC3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1791 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metalloproteinase which specifically cleaves IGFBP-5. Shows limited proteolysis toward IGFBP-3. Ref.1

Catalytic activity

Cleavage of the 143-Ser-|-Lys-144 bond in insulin-like growth factor binding protein (IGFBP)-5.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed abundantly in placenta, and non-pregnant mammary gland with low expression in the kidney, fetal brain and pancreas. Ref.1 Ref.2

Sequence similarities

Belongs to the peptidase M43B family.

Contains 5 Sushi (CCP/SCR) domains.

Sequence caution

The sequence AAL17779.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAL17780.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAC11134.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BXP8-1)

Also known as: Papp-e(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: Q9BXP8-2)

Also known as: Papp-e(2);

The sequence of this isoform differs from the canonical sequence as follows:
     811-827: DDNCTDNFTPNQVARMH → GITTVLFCFLLRIHGGL
     828-1791: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 234212
PRO_0000029249
Chain235 – 17911557Pappalysin-2
PRO_0000029250

Regions

Domain1393 – 146169Sushi 1
Domain1462 – 152160Sushi 2
Domain1523 – 159270Sushi 3
Domain1593 – 164856Sushi 4
Domain1651 – 173181Sushi 5
Region442 – 754313Metalloprotease
Compositional bias171 – 1744Poly-Thr
Compositional bias1654 – 16574Poly-Pro

Sites

Active site7341
Metal binding7331Zinc; catalytic By similarity
Metal binding7371Zinc; catalytic By similarity
Metal binding7431Zinc; catalytic By similarity

Amino acid modifications

Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation5621N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Glycosylation6791N-linked (GlcNAc...) Potential
Glycosylation8131N-linked (GlcNAc...) Potential
Glycosylation8571N-linked (GlcNAc...) Potential
Glycosylation9411N-linked (GlcNAc...) Potential
Glycosylation12431N-linked (GlcNAc...) Potential
Glycosylation13081N-linked (GlcNAc...) Potential
Glycosylation13261N-linked (GlcNAc...) Potential
Glycosylation13441N-linked (GlcNAc...) Potential
Glycosylation14081N-linked (GlcNAc...) Potential
Glycosylation14561N-linked (GlcNAc...) Potential
Glycosylation14761N-linked (GlcNAc...) Potential
Glycosylation16941N-linked (GlcNAc...) Potential
Disulfide bond312 ↔ 403 By similarity
Disulfide bond499 ↔ 793 By similarity
Disulfide bond504 ↔ 828 By similarity
Disulfide bond586 ↔ 600 By similarity
Disulfide bond596 ↔ 612 By similarity
Disulfide bond628 ↔ 644 By similarity
Disulfide bond645 ↔ 656 By similarity
Disulfide bond754 ↔ 771Or C-754 with C-783 By similarity
Disulfide bond758 ↔ 783Or C-788 with C-771 By similarity
Disulfide bond881 ↔ 1045 By similarity
Disulfide bond884 ↔ 1048 By similarity
Disulfide bond924 ↔ 1003 By similarity
Disulfide bond946 ↔ 951 By similarity
Disulfide bond1115 ↔ 1143 By similarity
Disulfide bond1128 ↔ 1139 By similarity
Disulfide bond1151 ↔ 1158 By similarity
Disulfide bond1167 ↔ 1179 By similarity
Disulfide bond1205 ↔ 1238 By similarity
Disulfide bond1219 ↔ 1318 By similarity
Disulfide bond1371 ↔ 1385 By similarity
Disulfide bond1396 ↔ 1448 By similarity
Disulfide bond1423 ↔ 1459 By similarity
Disulfide bond1464 ↔ 1508 By similarity
Disulfide bond1479 ↔ 1489 By similarity
Disulfide bond1493 ↔ 1521 By similarity
Disulfide bond1525 ↔ 1579 By similarity
Disulfide bond1541 ↔ 1552 By similarity
Disulfide bond1556 ↔ 1590 By similarity
Disulfide bond1595 ↔ 1633 By similarity
Disulfide bond1608 ↔ 1618 By similarity
Disulfide bond1622 ↔ 1646 By similarity
Disulfide bond1653 ↔ 1714 By similarity
Disulfide bond1667 ↔ 1677 By similarity
Disulfide bond1681 ↔ 1729 By similarity
Disulfide bond1733 ↔ 1751 By similarity

Natural variations

Alternative sequence811 – 82717DDNCT…VARMH → GITTVLFCFLLRIHGGL in isoform 2.
VSP_012194
Alternative sequence828 – 1791964Missing in isoform 2.
VSP_012195
Natural variant1711T → S.
Corresponds to variant rs36112782 [ dbSNP | Ensembl ].
VAR_051595
Natural variant16571P → R.
Corresponds to variant rs34602579 [ dbSNP | Ensembl ].
VAR_051596

Experimental info

Mutagenesis7341E → Q: Loss of activity. Ref.1
Sequence conflict4471G → E in AAL17779. Ref.2
Sequence conflict4471G → E in CAC11134. Ref.6
Sequence conflict5681S → N in AAL17780. Ref.2
Sequence conflict8461I → T in AAL17779. Ref.2
Sequence conflict8461I → T in CAC11134. Ref.6
Sequence conflict13431L → P in AAL17779. Ref.2
Sequence conflict13431L → P in CAC11134. Ref.6
Sequence conflict17391D → N in CAC11134. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Papp-e(1)) [UniParc].

Last modified February 20, 2007. Version 4.
Checksum: F436030821EC6EDD

FASTA1,791198,539
        10         20         30         40         50         60 
MMCLKILRIS LAILAGWALC SANSELGWTR KKSLVEREHL NQVLLEGERC WLGAKVRRPR 

        70         80         90        100        110        120 
ASPQHHLFGV YPSRAGNYLR PYPVGEQEIH HTGRSKPDTE GNAVSLVPPD LTENPAGLRG 

       130        140        150        160        170        180 
AVEEPAAPWV GDSPIGQSEL LGDDDAYLGN QRSKESLGEA GIQKGSAMAA TTTTAIFTTL 

       190        200        210        220        230        240 
NEPKPETQRR GWAKSRQRRQ VWKRRAEDGQ GDSGISSHFQ PWPKHSLKHR VKKSPPEESN 

       250        260        270        280        290        300 
QNGGEGSYRE AETFNSQVGL PILYFSGRRE RLLLRPEVLA EIPREAFTVE AWVKPEGGQN 

       310        320        330        340        350        360 
NPAIIAGVFD NCSHTVSDKG WALGIRSGKD KGKRDARFFF SLCTDRVKKA TILISHSRYQ 

       370        380        390        400        410        420 
PGTWTHVAAT YDGRHMALYV DGTQVASSLD QSGPLNSPFM ASCRSLLLGG DSSEDGHYFR 

       430        440        450        460        470        480 
GHLGTLVFWS TALPQSHFQH SSQHSSGEEE ATDLVLTASF EPVNTEWVPF RDEKYPRLEV 

       490        500        510        520        530        540 
LQGFEPEPEI LSPLQPPLCG QTVCDNVELI SQYNGYWPLR GEKVIRYQVV NICDDEGLNP 

       550        560        570        580        590        600 
IVSEEQIRLQ HEALNEAFSR YNISWQLSVH QVHNSTLRHR VVLVNCEPSK IGNDHCDPEC 

       610        620        630        640        650        660 
EHPLTGYDGG DCRLQGRCYS WNRRDGLCHV ECNNMLNDFD DGDCCDPQVA DVRKTCFDPD 

       670        680        690        700        710        720 
SPKRAYMSVK ELKEALQLNS THFLNIYFAS SVREDLAGAA TWPWDKDAVT HLGGIVLSPA 

       730        740        750        760        770        780 
YYGMPGHTDT MIHEVGHVLG LYHVFKGVSE RESCNDPCKE TVPSMETGDL CADTAPTPKS 

       790        800        810        820        830        840 
ELCREPEPTS DTCGFTRFPG APFTNYMSYT DDNCTDNFTP NQVARMHCYL DLVYQQWTES 

       850        860        870        880        890        900 
RKPTPIPIPP MVIGQTNKSL TIHWLPPISG VVYDRASGSL CGACTEDGTF RQYVHTASSR 

       910        920        930        940        950        960 
RVCDSSGYWT PEEAVGPPDV DQPCEPSLQA WSPEVHLYHM NMTVPCPTEG CSLELLFQHP 

       970        980        990       1000       1010       1020 
VQADTLTLWV TSFFMESSQV LFDTEILLEN KESVHLGPLD TFCDIPLTIK LHVDGKVSGV 

      1030       1040       1050       1060       1070       1080 
KVYTFDERIE IDAALLTSQP HSPLCSGCRP VRYQVLRDPP FASGLPVVVT HSHRKFTDVE 

      1090       1100       1110       1120       1130       1140 
VTPGQMYQYQ VLAEAGGELG EASPPLNHIH GAPYCGDGKV SERLGEECDD GDLVSGDGCS 

      1150       1160       1170       1180       1190       1200 
KVCELEEGFN CVGEPSLCYM YEGDGICEPF ERKTSIVDCG IYTPKGYLDQ WATRAYSSHE 

      1210       1220       1230       1240       1250       1260 
DKKKCPVSLV TGEPHSLICT SYHPDLPNHR PLTGWFPCVA SENETQDDRS EQPEGSLKKE 

      1270       1280       1290       1300       1310       1320 
DEVWLKVCFN RPGEARAIFI FLTTDGLVPG EHQQPTVTLY LTDVRGSNHS LGTYGLSCQH 

      1330       1340       1350       1360       1370       1380 
NPLIINVTHH QNVLFHHTTS VLLNFSSPRV GISAVALRTS SRIGLSAPSN CISEDEGQNH 

      1390       1400       1410       1420       1430       1440 
QGQSCIHRPC GKQDSCPSLL LDHADVVNCT SIGPGLMKCA ITCQRGFALQ ASSGQYIRPM 

      1450       1460       1470       1480       1490       1500 
QKEILLTCSS GHWDQNVSCL PVDCGVPDPS LVNYANFSCS EGTKFLKRCS ISCVPPAKLQ 

      1510       1520       1530       1540       1550       1560 
GLSPWLTCLE DGLWSLPEVY CKLECDAPPI ILNANLLLPH CLQDNHDVGT ICKYECKPGY 

      1570       1580       1590       1600       1610       1620 
YVAESAEGKV RNKLLKIQCL EGGIWEQGSC IPVVCEPPPP VFEGMYECTN GFSLDSQCVL 

      1630       1640       1650       1660       1670       1680 
NCNQEREKLP ILCTKEGLWT QEFKLCENLQ GECPPPPSEL NSVEYKCEQG YGIGAVCSPL 

      1690       1700       1710       1720       1730       1740 
CVIPPSDPVM LPENITADTL EHWMEPVKVQ SIVCTGRRQW HPDPVLVHCI QSCEPFQADG 

      1750       1760       1770       1780       1790 
WCDTINNRAY CHYDGGDCCS STLSSKKVIP FAADCDLDEC TCRDPKAEEN Q 

« Hide

Isoform 2 (Papp-e(2)) [UniParc].

Checksum: FB3B6F1E944F7C24
Show »

FASTA82792,136

References

« Hide 'large scale' references
[1]"Pregnancy-associated plasma protein-A2 (PAPP-A2), a novel insulin-like growth factor-binding protein-5 proteinase."
Overgaard M.T., Boldt H.B., Laursen L.S., Sottrup-Jensen L., Conover C.A., Oxvig C.
J. Biol. Chem. 276:21849-21853(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 234-241, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-734, FUNCTION.
Tissue: Term placenta.
[2]"The characterization of pregnancy associated plasma protein-E and the identification of an alternative splice variant."
Page N.M., Butlin D.J., Lomthaisong K., Lowry P.J.
Placenta 22:681-687(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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).
[6]"Pregnancy-associated plasma protein-E (PAPP-E)."
Farr M., Struebe J., Geppert H.-G., Kocourek A., Mahne M., Tschesche H.
Biochim. Biophys. Acta 1493:356-362(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-1791 (ISOFORM 1).
Tissue: Placenta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF311940 mRNA. Translation: AAK31073.1.
AF342989 mRNA. Translation: AAL17779.1. Different initiation.
AF342990 mRNA. Translation: AAL17780.1. Different initiation.
AL031290 expand/collapse EMBL AC list , AL031734, AL139282, AL596254 Genomic DNA. Translation: CAI22721.1.
AL031734 expand/collapse EMBL AC list , AL031290, AL139282, AL596254 Genomic DNA. Translation: CAI22172.1.
AL031734, AL596254 Genomic DNA. Translation: CAI22173.1.
AL139282 expand/collapse EMBL AC list , AL031290, AL031734, AL596254 Genomic DNA. Translation: CAI19567.1.
AL596254 expand/collapse EMBL AC list , AL031290, AL031734, AL139282 Genomic DNA. Translation: CAH71731.1.
AL596254, AL031734 Genomic DNA. Translation: CAH71732.1.
CH471067 Genomic DNA. Translation: EAW91003.1.
BC117193 mRNA. Translation: AAI17194.3.
BC117195 mRNA. Translation: AAI17196.3.
AJ278348 mRNA. Translation: CAC11134.1. Different initiation.
RefSeqNP_064714.2. NM_020318.2.
NP_068755.2. NM_021936.2.
XP_005245479.1. XM_005245422.1.
UniGeneHs.187284.

3D structure databases

ProteinModelPortalQ9BXP8.
SMRQ9BXP8. Positions 582-708, 877-913, 1398-1767.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121951. 3 interactions.
IntActQ9BXP8. 3 interactions.
MINTMINT-1181124.
STRING9606.ENSP00000356634.

Protein family/group databases

MEROPSM43.005.

PTM databases

PhosphoSiteQ9BXP8.

Polymorphism databases

DMDM126302580.

Proteomic databases

PaxDbQ9BXP8.
PRIDEQ9BXP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367661; ENSP00000356633; ENSG00000116183. [Q9BXP8-2]
ENST00000367662; ENSP00000356634; ENSG00000116183. [Q9BXP8-1]
GeneID60676.
KEGGhsa:60676.
UCSCuc001gky.1. human. [Q9BXP8-2]
uc001gkz.3. human. [Q9BXP8-1]

Organism-specific databases

CTD60676.
GeneCardsGC01P176432.
HGNCHGNC:14615. PAPPA2.
HPAHPA018412.
HPA018430.
neXtProtNX_Q9BXP8.
PharmGKBPA33373.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG128309.
HOGENOMHOG000033711.
HOVERGENHBG053501.
InParanoidQ9BXP8.
KOK08647.
OMAPFMASCR.
OrthoDBEOG7HB58B.
PhylomeDBQ9BXP8.
TreeFamTF331636.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

BgeeQ9BXP8.
CleanExHS_PAPPA2.
GenevestigatorQ9BXP8.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR003961. Fibronectin_type3.
IPR011936. Myxo_disulph_rpt.
IPR000800. Notch_dom.
IPR026918. PAPPA2.
IPR008754. Peptidase_M43.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PANTHERPTHR19325:SF222. PTHR19325:SF222. 1 hit.
PfamPF00066. Notch. 2 hits.
PF05572. Peptidase_M43. 1 hit.
PF00084. Sushi. 1 hit.
[Graphical view]
SMARTSM00032. CCP. 4 hits.
SM00060. FN3. 1 hit.
SM00004. NL. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF57535. SSF57535. 3 hits.
TIGRFAMsTIGR02232. myxo_disulf_rpt. 1 hit.
PROSITEPS50923. SUSHI. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAPPA2. human.
GeneWikiPAPPA2.
GenomeRNAi60676.
NextBio65486.
PROQ9BXP8.

Entry information

Entry namePAPP2_HUMAN
AccessionPrimary (citable) accession number: Q9BXP8
Secondary accession number(s): A9Z1Y8 expand/collapse secondary AC list , Q96PH7, Q96PH8, Q9H4C9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: February 20, 2007
Last modified: March 19, 2014
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM