Q8R4K8 · PAPP1_MOUSE

  • Protein
    Pappalysin-1
  • Gene
    Pappa
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Metalloproteinase which specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. Cleavage of IGFBP-4 is dramatically enhanced by the presence of IGF, whereas cleavage of IGFBP-5 is slightly inhibited by the presence of IGF. Isoform 2 cleaves IGFBP-4 very slowly compared to PAPP-A, but its ability to cleave IGFBP-5 is unaffected.

Catalytic activity

  • Cleavage of the 135-Met-|-Lys-136 bond in insulin-like growth factor binding protein (IGFBP)-4, and the 143-Ser-|-Lys-144 bond in IGFBP-5.
    EC:3.4.24.79 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

116242004006008001,0001,2001,4001,600
TypeIDPosition(s)Description
Binding site559Zn2+ (UniProtKB | ChEBI); catalytic
Active site560
Binding site563Zn2+ (UniProtKB | ChEBI); catalytic
Binding site569Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular space
Molecular Functionendopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Biological Processcell surface receptor signaling pathway
Biological Processfemale pregnancy
Biological Processprotein catabolic process
Biological Processproteolysis
Biological Processresponse to dexamethasone
Biological Processresponse to follicle-stimulating hormone

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Pappalysin-1
  • EC number
  • Alternative names
    • Insulin-like growth factor-dependent IGF-binding protein 4 protease (IGF-dependent IGFBP-4 protease; IGFBP-4ase)
    • Pregnancy-associated plasma protein A (PAPP-A)

Gene names

    • Name
      Pappa

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • 129/SvJ
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8R4K8
  • Secondary accessions
    • Q80VW3
    • Q80YY1
    • Q8K423
    • Q8R4K7
    • Q9ES06
    • Q9JK57

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-22
PropeptidePRO_000002924723-81
ChainPRO_000002924882-1624Pappalysin-1
Disulfide bond141↔232
Disulfide bond324↔619
Disulfide bond329↔654
Glycosylation387N-linked (GlcNAc...) asparagine
Glycosylation398N-linked (GlcNAc...) asparagine
Disulfide bond411↔425
Disulfide bond421↔437
Glycosylation426N-linked (GlcNAc...) asparagine
Disulfide bond454↔470
Disulfide bond458Interchain (with C-49 in PRG2 proform)
Disulfide bond471↔482
Glycosylation516N-linked (GlcNAc...) asparagine
Disulfide bond580↔597Or C-580 with C-609
Disulfide bond584↔609Or C-584 with C-597
Glycosylation598N-linked (GlcNAc...) asparagine
Glycosylation616N-linked (GlcNAc...) asparagine
Disulfide bond707↔875
Disulfide bond710↔878
Glycosylation722N-linked (GlcNAc...) asparagine
Disulfide bond729Interchain (with C-170 in PRG2 proform)
Disulfide bond750↔832
Disulfide bond772↔778
Glycosylation822N-linked (GlcNAc...) asparagine
Disulfide bond944↔972
Disulfide bond957↔968
Disulfide bond980↔987
Disulfide bond996↔1008
Glycosylation1023N-linked (GlcNAc...) asparagine
Disulfide bond1033↔1067
Disulfide bond1048↔1136
Disulfide bond1189↔1202
Disulfide bond1207Interchain
Disulfide bond1212↔1266
Glycosylation1219N-linked (GlcNAc...) asparagine
Glycosylation1223N-linked (GlcNAc...) asparagine
Disulfide bond1224↔1235
Disulfide bond1239↔1277
Disulfide bond1282↔1326
Disulfide bond1297↔1307
Disulfide bond1311↔1339
Glycosylation1320N-linked (GlcNAc...) asparagine
Disulfide bond1343↔1396
Disulfide bond1359↔1370
Disulfide bond1374↔1407
Disulfide bond1412↔1455
Disulfide bond1425↔1435
Disulfide bond1439↔1468
Disulfide bond1475↔1536
Disulfide bond1489↔1499
Disulfide bond1503↔1551
Glycosylation1516N-linked (GlcNAc...) asparagine
Disulfide bond1555↔1573

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in kidney, spleen, brain, ovary, breast, skin, prostate, uterus, and placenta.

Gene expression databases

Interaction

Subunit

Homodimer; disulfide-linked. In pregnancy serum, predominantly found as a disulfide-linked 2:2 heterotetramer with the proform of PRG2 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region28-93Disordered
Region272-583Metalloprotease
Domain1210-1279Sushi 1
Domain1280-1341Sushi 2
Domain1342-1409Sushi 3
Domain1410-1470Sushi 4
Domain1473-1553Sushi 5

Sequence similarities

Belongs to the peptidase M43B family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q8R4K8-1

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.

  • Length
    1,624
  • Mass (Da)
    181,318
  • Last updated
    2004-12-07 v2
  • Checksum
    B09404C206CB60D1
MRLWSWVLRLGLLSAALGCGLAERPRRVRRDPRAVRPPRPAAGPATCATRAARGRRASPPPPPGGAWEAVRVPRRRQQRAARGAEEPSPPSRALYFSGRGEQLRLRADLELPRDAFTLQVWLRAEGGQKSPAVITGLYDKCSYTSRDRGWVMGIHTTSDQGNRDPRYFFSLKTDRARKVTTIDAHRSYLPGQWVHLAATYDGRLMKLYMNGAQVATSAEQVGGIFSPLTQKCKVLMLGGSALNHNFRGHIEHFSLWKVARTQREIVSDMETRGLHTPLPQLLLQENWDNVKRTWSPMKDGNSPQVEFSNAHGFLLDTNLEPPLCGQTLCDNTEVISSYNQLPSFRQPKVVRYRVVNIYDDHHENPTVSWQQIDFQHQQLAEAFQHYNISWELEVLNINSSSLRHRLILANCDISKIGDEKCDPECNHTLTGHDGGDCRQLRYPAFMKKQQNGVCDMDCNYERFNFDGGECCDPDITDVTKTCFDPDSPHRAYLDVNELKNILRLDGSTHLNIFFANSSEEELAGVATWPWDKEALMHLGGIVLNPSFYGIPGHTHTMIHEIGHSLGLYHIFRGISEIQSCSDPCMETEPSFETGDLCNDTNPAPKHKFCGDPGPGNDTCGFHGFFNTPYNNFMSYADDDCTDSFTPNQVSRMHCYLDLVYQSWQPSRKPAPVALAPQVVGHTMDSVMLEWFPPIDGHFFERELGSACDLCLEGRILVQYAFNASSPMPCGPSGHWSPREAEGHPDVEQPCKSSVRTWSPNSAVNPHTVPPACPEPQGCYLELEFRYPLVPESLTIWVTFVSSDWDSSGAVNDIKLLTISGKNISLGPQNVFCDIPLTIRLRDVGEEVYGIQIYTLDEHLEIDAAMLTSTVDSPLCLQCKPLQYKVLRDPPLLEDVASLLHLNRRFMDTDLKLGSVYQYRIITISGNEESEPSPAAIYTHGSGYCGDGVIQKDQGEECDDMNKVNGDGCSLFCKQEVSFNCIDEPSRCYFHDGDGMCEEFEQKTSIKDCGVYTPQGFLDQWASNASVSHQDQQCPGWVVIGQPAASQVCRTKVIDLSEGISQHAWYPCTITYPYYHLPQTTFWLQTYFSQPMVAAAVIIHLVTDGTYYGDQKQETISVQLLDTKDQSHDLGLHVLSCRNNPLIIPVVHDLSQPFYHSQAVHVSFSSPLVAISGVALRSFDNFDPVTLSSCQRGETYSPAEQSCVHFACQAADCPELAVGNASLNCSSNHHYHGAQCTVSCQTGYVLQIQRDDELIKSQVGPSITVTCTEGKWNKQVACEPVDCGIPDHHHVYAASFSCPEGTTFGRRCSFQCRHPAQLKGNNSFLTCMEDGLWSFPEALCELMCLAPPPVPNADLQTARCRENKHKVGSFCKYKCKPGYHVPGSSRKSKKRAFKTQCTQDGSWQEGTCVPVTCDPPPPKFHGLYQCTNGFQFNSECRIKCEDSDASQGRGSNIIHCRKDGTWSGSFHVCREMQGQCSAPNQLNSNLKLQCPDGYAIGSECAISCLDHNSESIILPVNLTVRDIPHWMNPTRVQRIVCTAGLQWYPHPALIHCVKGCEPFMGDNYCDAINNRAFCNYDGGDCCTSTVKTKKVTPFPMSCDLQNDCACRDPEAQEHNRKDLRGYSHG

Q8R4K8-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 490-490: R → RQSIRKRAHVVEESWLPHGKQKAKKRKRTR

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_012193490in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL691454
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL691491
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AF439513
EMBL· GenBank· DDBJ
AAM12687.1
EMBL· GenBank· DDBJ
mRNA
AF439514
EMBL· GenBank· DDBJ
AAM12688.1
EMBL· GenBank· DDBJ
mRNA
AF510317
EMBL· GenBank· DDBJ
AAM44048.1
EMBL· GenBank· DDBJ
Genomic DNA
AF258461
EMBL· GenBank· DDBJ
AAG09799.1
EMBL· GenBank· DDBJ
mRNA
AF260433
EMBL· GenBank· DDBJ
AAF70319.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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