Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UK55 (ZPI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein Z-dependent protease inhibitor

Short name=PZ-dependent protease inhibitor
Short name=PZI
Alternative name(s):
Serpin A10
Gene names
Name:SERPINA10
Synonyms:ZPI
ORF Names:UNQ707/PRO1358
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits activity of the coagulation protease factor Xa in the presence of PROZ, calcium and phospholipids. Also inhibits factor XIa in the absence of cofactors. Ref.7

Subunit structure

Interacts with PROZ. Ref.7 Ref.12

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Post-translational modification

Phosphorylation sites are present in the extracellular medium.

Miscellaneous

Heparin acts as an important cofactor, producing 20 to 100-fold accelerations of SERPINA10 reactions with factor Xa and factor XIa.

Sequence similarities

Belongs to the serpin family.

Sequence caution

The sequence CAD62339.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.6
Chain22 – 444423Protein Z-dependent protease inhibitor
PRO_0000032482

Regions

Region136 – 15318Heparin-binding

Sites

Site2611Essential for interaction with PROZ By similarity
Site3141Essential for interaction with PROZ By similarity
Site408 – 4092Reactive bond By similarity

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Ref.9
Glycosylation1801N-linked (GlcNAc...) Ref.8
Glycosylation1971N-linked (GlcNAc...) Ref.12
Glycosylation2951N-linked (GlcNAc...) Ref.8 Ref.12

Natural variations

Natural variant461K → R. Ref.2 Ref.4
Corresponds to variant rs941590 [ dbSNP | Ensembl ].
VAR_020325
Natural variant611S → G. Ref.2 Ref.4
Corresponds to variant rs941591 [ dbSNP | Ensembl ].
VAR_020326
Natural variant1391G → R. Ref.4
Corresponds to variant rs56137907 [ dbSNP | Ensembl ].
VAR_038833
Natural variant1581L → Q.
Corresponds to variant rs2232699 [ dbSNP | Ensembl ].
VAR_051940
Natural variant1611T → S. Ref.2 Ref.4
Corresponds to variant rs2232700 [ dbSNP | Ensembl ].
VAR_020327
Natural variant1961R → H.
Corresponds to variant rs2232701 [ dbSNP | Ensembl ].
VAR_051941
Natural variant2711G → S. Ref.4
Corresponds to variant rs2232708 [ dbSNP | Ensembl ].
VAR_038834
Natural variant3841Q → P. Ref.4
VAR_038835
Natural variant3841Q → R. Ref.2
Corresponds to variant rs2232710 [ dbSNP | Ensembl ].
VAR_051942
Natural variant4201F → L. Ref.13
VAR_070192

Experimental info

Mutagenesis4081Y → A: Loss of inhibitory activity. Ref.1

Secondary structure

............................................................... 444
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UK55 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 06BD47C97BBDD700

FASTA44450,707
        10         20         30         40         50         60 
MKVVPSLLLS VLLAQVWLVP GLAPSPQSPE TPAPQNQTSR VVQAPKEEEE DEQEASEEKA 

        70         80         90        100        110        120 
SEEEKAWLMA SRQQLAKETS NFGFSLLRKI SMRHDGNMVF SPFGMSLAMT GLMLGATGPT 

       130        140        150        160        170        180 
ETQIKRGLHL QALKPTKPGL LPSLFKGLRE TLSRNLELGL TQGSFAFIHK DFDVKETFFN 

       190        200        210        220        230        240 
LSKRYFDTEC VPMNFRNASQ AKRLMNHYIN KETRGKIPKL FDEINPETKL ILVDYILFKG 

       250        260        270        280        290        300 
KWLTPFDPVF TEVDTFHLDK YKTIKVPMMY GAGKFASTFD KNFRCHVLKL PYQGNATMLV 

       310        320        330        340        350        360 
VLMEKMGDHL ALEDYLTTDL VETWLRNMKT RNMEVFFPKF KLDQKYEMHE LLRQMGIRRI 

       370        380        390        400        410        420 
FSPFADLSEL SATGRNLQVS RVLQRTVIEV DERGTEAVAG ILSEITAYSM PPVIKVDRPF 

       430        440 
HFMIYEETSG MLLFLGRVVN PTLL 

« Hide

References

« Hide 'large scale' references
[1]"The protein Z-dependent protease inhibitor is a serpin."
Han X., Huang Z.-F., Fiehler R., Broze G.J. Jr.
Biochemistry 38:11073-11078(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF TYR-408.
Tissue: Liver.
[2]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-46; GLY-61; SER-161 AND ARG-384.
[3]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal liver.
[4]SeattleSNPs variation discovery resource
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-46; GLY-61; ARG-139; SER-161; SER-271 AND PRO-384.
[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].
Tissue: Liver.
[6]"Isolation of a protein Z-dependent plasma protease inhibitor."
Han X., Fiehler R., Broze G.J. Jr.
Proc. Natl. Acad. Sci. U.S.A. 95:9250-9255(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-33, CHARACTERIZATION.
Tissue: Plasma.
[7]"Characterization of the protein Z-dependent protease inhibitor."
Han X., Fiehler R., Broze G.J. Jr.
Blood 96:3049-3055(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PROZ.
[8]"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-180 AND ASN-295.
Tissue: Plasma.
[9]"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-36.
Tissue: Liver.
[10]"Characterization of the heparin-binding site of the protein z-dependent protease inhibitor."
Yang L., Ding Q., Huang X., Olson S.T., Rezaie A.R.
Biochemistry 51:4078-4085(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: HEPARIN-BINDING REGION.
[11]"Crystal structure of protein Z-dependent inhibitor complex shows how protein Z functions as a cofactor in the membrane inhibition of factor X."
Wei Z., Yan Y., Carrell R.W., Zhou A.
Blood 114:3662-3667(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 60-444 IN COMPLEX WITH PROZ.
[12]"Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa."
Huang X., Dementiev A., Olson S.T., Gettins P.G.
J. Biol. Chem. 285:20399-20409(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.26 ANGSTROMS) OF 22-444 IN COMPLEX WITH PROZ, GLYCOSYLATION AT ASN-197 AND ASN-295, SUBUNIT.
[13]"Identification of mutations in SLC24A4, encoding a potassium-dependent sodium/calcium exchanger, as a cause of amelogenesis imperfecta."
Parry D.A., Poulter J.A., Logan C.V., Brookes S.J., Jafri H., Ferguson C.H., Anwari B.M., Rashid Y., Zhao H., Johnson C.A., Inglehearn C.F., Mighell A.J.
Am. J. Hum. Genet. 92:307-312(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-420.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF181467 mRNA. Translation: AAD53962.1.
AY358597 mRNA. Translation: AAQ88960.1.
BX248011 mRNA. Translation: CAD62339.1. Different initiation.
EF621762 Genomic DNA. Translation: ABR09269.1.
BC022261 mRNA. Translation: AAH22261.1.
CCDSCCDS9923.1.
RefSeqNP_001094077.1. NM_001100607.2.
NP_057270.1. NM_016186.2.
XP_005267790.1. XM_005267733.2.
XP_006725227.1. XM_006725164.1.
UniGeneHs.118620.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3F1SX-ray2.30A60-444[»]
3H5CX-ray3.26A22-444[»]
4AFXX-ray2.09A23-408[»]
B409-444[»]
4AJUX-ray2.65A23-408[»]
B409-444[»]
ProteinModelPortalQ9UK55.
SMRQ9UK55. Positions 26-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119339. 2 interactions.
IntActQ9UK55. 1 interaction.
STRING9606.ENSP00000261994.

Protein family/group databases

MEROPSI04.005.

PTM databases

PhosphoSiteQ9UK55.

Polymorphism databases

DMDM12585541.

Proteomic databases

PaxDbQ9UK55.
PRIDEQ9UK55.

Protocols and materials databases

DNASU51156.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261994; ENSP00000261994; ENSG00000140093.
ENST00000393096; ENSP00000376809; ENSG00000140093.
ENST00000554173; ENSP00000450971; ENSG00000140093.
GeneID51156.
KEGGhsa:51156.
UCSCuc001yct.3. human.

Organism-specific databases

CTD51156.
GeneCardsGC14M094749.
HGNCHGNC:15996. SERPINA10.
HPAHPA048739.
MIM602455. gene.
605271. gene+phenotype.
neXtProtNX_Q9UK55.
PharmGKBPA38078.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4826.
HOGENOMHOG000238519.
HOVERGENHBG101138.
InParanoidQ9UK55.
PhylomeDBQ9UK55.
TreeFamTF343094.

Gene expression databases

ArrayExpressQ9UK55.
BgeeQ9UK55.
CleanExHS_SERPINA10.
GenevestigatorQ9UK55.

Family and domain databases

InterProIPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ9UK55.
GenomeRNAi51156.
NextBio54061.
PROQ9UK55.
SOURCESearch...

Entry information

Entry nameZPI_HUMAN
AccessionPrimary (citable) accession number: Q9UK55
Secondary accession number(s): A5Z2A5, Q6UWX9, Q86U20
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 136 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 14

Human chromosome 14: entries, gene names and cross-references to MIM