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P29622 (KAIN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kallistatin
Alternative name(s):
Kallikrein inhibitor
Peptidase inhibitor 4
Short name=PI-4
Serpin A4
Gene names
Name:SERPINA4
Synonyms:KST, PI4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein. Ref.1

Subunit structure

Monomer and some homodimers.

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Post-translational modification

The N-terminus is blocked.

Miscellaneous

Heparin blocks kallistatin's complex formation with tissue kallikrein and abolishes its inhibitory effect on tissue kallikrein's activity.

Sequence similarities

Belongs to the serpin family.

Sequence caution

The sequence CAD66567.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 427407Kallistatin
PRO_0000032425

Sites

Site388 – 3892Reactive bond

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation1081N-linked (GlcNAc...) Ref.7
Glycosylation1571N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation2381N-linked (GlcNAc...) (complex) Ref.7 Ref.8

Experimental info

Sequence conflict3821S → T Ref.1
Sequence conflict3821S → T Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29622 [UniParc].

Last modified June 21, 2005. Version 3.
Checksum: 68EBE7AF956BFB77

FASTA42748,542
        10         20         30         40         50         60 
MHLIDYLLLL LVGLLALSHG QLHVEHDGES CSNSSHQQIL ETGEGSPSLK IAPANADFAF 

        70         80         90        100        110        120 
RFYYLIASET PGKNIFFSPL SISAAYAMLS LGACSHSRSQ ILEGLGFNLT ELSESDVHRG 

       130        140        150        160        170        180 
FQHLLHTLNL PGHGLETRVG SALFLSHNLK FLAKFLNDTM AVYEAKLFHT NFYDTVGTIQ 

       190        200        210        220        230        240 
LINDHVKKET RGKIVDLVSE LKKDVLMVLV NYIYFKALWE KPFISSRTTP KDFYVDENTT 

       250        260        270        280        290        300 
VRVPMMLQDQ EHHWYLHDRY LPCSVLRMDY KGDATVFFIL PNQGKMREIE EVLTPEMLMR 

       310        320        330        340        350        360 
WNNLLRKRNF YKKLELHLPK FSISGSYVLD QILPRLGFTD LFSKWADLSG ITKQQKLEAS 

       370        380        390        400        410        420 
KSFHKATLDV DEAGTEAAAA TSFAIKFFSA QTNRHILRFN RPFLVVIFST STQSVLFLGK 


VVDPTKP 

« Hide

References

« Hide 'large scale' references
[1]"Kallistatin: a novel human serine proteinase inhibitor. Molecular cloning, tissue distribution, and expression in Escherichia coli."
Chai K.X., Chen L.-M., Chao J., Chao L.
J. Biol. Chem. 268:24498-24505(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"Molecular cloning, sequence analysis, and chromosomal localization of the human protease inhibitor 4 (kallistatin) gene (PI4)."
Chai K.X., Ward D.C., Chao J., Chao L.
Genomics 23:370-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]"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: Colon.
[5]"Kallistatin: a novel human tissue kallikrein inhibitor. Purification, characterization, and reactive center sequence."
Zhou G.X., Chao L., Chao J.
J. Biol. Chem. 267:25873-25880(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 388-403.
Tissue: Plasma.
[6]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-157.
[7]"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-108; ASN-157 AND ASN-238.
Tissue: Plasma.
[8]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-238.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19684 mRNA. Translation: AAA59454.1.
L28101 Genomic DNA. Translation: AAC41706.1.
BX248009 mRNA. Translation: CAD62337.1.
BX248760 mRNA. Translation: CAD66567.1. Different initiation.
BC014992 mRNA. Translation: AAH14992.1.
CCDSCCDS9927.1.
PIRA49518.
RefSeqNP_001275961.1. NM_001289032.1.
NP_001275962.1. NM_001289033.1.
NP_006206.2. NM_006215.3.
UniGeneHs.719893.

3D structure databases

ProteinModelPortalP29622.
SMRP29622. Positions 57-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111285. 12 interactions.
IntActP29622. 10 interactions.
MINTMINT-8247389.
STRING9606.ENSP00000298841.

Protein family/group databases

MEROPSI04.003.

PTM databases

PhosphoSiteP29622.

Polymorphism databases

DMDM68067608.

Proteomic databases

PaxDbP29622.
PeptideAtlasP29622.
PRIDEP29622.

Protocols and materials databases

DNASU5267.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298841; ENSP00000298841; ENSG00000100665.
ENST00000555095; ENSP00000451172; ENSG00000100665.
ENST00000557004; ENSP00000450838; ENSG00000100665.
GeneID5267.
KEGGhsa:5267.
UCSCuc001ydk.3. human.

Organism-specific databases

CTD5267.
GeneCardsGC14P095027.
HGNCHGNC:8948. SERPINA4.
HPAHPA003607.
MIM147935. gene.
neXtProtNX_P29622.
PharmGKBPA35514.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4826.
HOGENOMHOG000238521.
HOVERGENHBG005957.
InParanoidP29622.
OMAVPMMLQD.
OrthoDBEOG7QC7W9.
PhylomeDBP29622.
TreeFamTF343201.

Gene expression databases

BgeeP29622.
GenevestigatorP29622.

Family and domain databases

InterProIPR023795. Serpin_CS.
IPR023796. 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. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSERPINA4.
GenomeRNAi5267.
NextBio20348.
PROP29622.
SOURCESearch...

Entry information

Entry nameKAIN_HUMAN
AccessionPrimary (citable) accession number: P29622
Secondary accession number(s): Q53XB5, Q86TR9, Q96BZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 21, 2005
Last modified: July 9, 2014
This is version 130 of the entry and version 3 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

MIM cross-references

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

Human chromosome 14

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