Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Kallistatin

Gene

SERPINA4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei388 – 3892Reactive bond

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: ProtInc

GO - Biological processi

  1. negative regulation of endopeptidase activity Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI04.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Kallistatin
Alternative name(s):
Kallikrein inhibitor
Peptidase inhibitor 4
Short name:
PI-4
Serpin A4
Gene namesi
Name:SERPINA4
Synonyms:KST, PI4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:8948. SERPINA4.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35514.

Polymorphism and mutation databases

DMDMi68067608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 427407KallistatinPRO_0000032425Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi108 – 1081N-linked (GlcNAc...)1 Publication
Glycosylationi157 – 1571N-linked (GlcNAc...)2 Publications
Glycosylationi238 – 2381N-linked (GlcNAc...) (complex)2 Publications

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP29622.
PeptideAtlasiP29622.
PRIDEiP29622.

PTM databases

PhosphoSiteiP29622.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiP29622.
ExpressionAtlasiP29622. baseline and differential.
GenevestigatoriP29622.

Organism-specific databases

HPAiHPA003607.

Interactioni

Subunit structurei

Monomer and some homodimers.

Protein-protein interaction databases

BioGridi111285. 14 interactions.
IntActiP29622. 10 interactions.
MINTiMINT-8247389.
STRINGi9606.ENSP00000298841.

Structurei

3D structure databases

ProteinModelPortaliP29622.
SMRiP29622. Positions 57-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP29622.
OMAiVPMMLQD.
OrthoDBiEOG7QC7W9.
PhylomeDBiP29622.
TreeFamiTF343201.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29622-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLIDYLLLL LVGLLALSHG QLHVEHDGES CSNSSHQQIL ETGEGSPSLK
60 70 80 90 100
IAPANADFAF RFYYLIASET PGKNIFFSPL SISAAYAMLS LGACSHSRSQ
110 120 130 140 150
ILEGLGFNLT ELSESDVHRG FQHLLHTLNL PGHGLETRVG SALFLSHNLK
160 170 180 190 200
FLAKFLNDTM AVYEAKLFHT NFYDTVGTIQ LINDHVKKET RGKIVDLVSE
210 220 230 240 250
LKKDVLMVLV NYIYFKALWE KPFISSRTTP KDFYVDENTT VRVPMMLQDQ
260 270 280 290 300
EHHWYLHDRY LPCSVLRMDY KGDATVFFIL PNQGKMREIE EVLTPEMLMR
310 320 330 340 350
WNNLLRKRNF YKKLELHLPK FSISGSYVLD QILPRLGFTD LFSKWADLSG
360 370 380 390 400
ITKQQKLEAS KSFHKATLDV DEAGTEAAAA TSFAIKFFSA QTNRHILRFN
410 420
RPFLVVIFST STQSVLFLGK VVDPTKP
Length:427
Mass (Da):48,542
Last modified:June 21, 2005 - v3
Checksum:i68EBE7AF956BFB77
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti382 – 3821S → T (PubMed:8227002).Curated
Sequence conflicti382 – 3821S → T (PubMed:7835886).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9927.1.
PIRiA49518.
RefSeqiNP_001275961.1. NM_001289032.1.
NP_001275962.1. NM_001289033.1.
NP_006206.2. NM_006215.3.
UniGeneiHs.719893.

Genome annotation databases

EnsembliENST00000298841; ENSP00000298841; ENSG00000100665.
ENST00000555095; ENSP00000451172; ENSG00000100665.
ENST00000557004; ENSP00000450838; ENSG00000100665.
GeneIDi5267.
KEGGihsa:5267.
UCSCiuc001ydk.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9927.1.
PIRiA49518.
RefSeqiNP_001275961.1. NM_001289032.1.
NP_001275962.1. NM_001289033.1.
NP_006206.2. NM_006215.3.
UniGeneiHs.719893.

3D structure databases

ProteinModelPortaliP29622.
SMRiP29622. Positions 57-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111285. 14 interactions.
IntActiP29622. 10 interactions.
MINTiMINT-8247389.
STRINGi9606.ENSP00000298841.

Protein family/group databases

MEROPSiI04.003.

PTM databases

PhosphoSiteiP29622.

Polymorphism and mutation databases

DMDMi68067608.

Proteomic databases

PaxDbiP29622.
PeptideAtlasiP29622.
PRIDEiP29622.

Protocols and materials databases

DNASUi5267.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298841; ENSP00000298841; ENSG00000100665.
ENST00000555095; ENSP00000451172; ENSG00000100665.
ENST00000557004; ENSP00000450838; ENSG00000100665.
GeneIDi5267.
KEGGihsa:5267.
UCSCiuc001ydk.3. human.

Organism-specific databases

CTDi5267.
GeneCardsiGC14P095027.
HGNCiHGNC:8948. SERPINA4.
HPAiHPA003607.
MIMi147935. gene.
neXtProtiNX_P29622.
PharmGKBiPA35514.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP29622.
OMAiVPMMLQD.
OrthoDBiEOG7QC7W9.
PhylomeDBiP29622.
TreeFamiTF343201.

Miscellaneous databases

GeneWikiiSERPINA4.
GenomeRNAii5267.
NextBioi20348.
PROiP29622.
SOURCEiSearch...

Gene expression databases

BgeeiP29622.
ExpressionAtlasiP29622. baseline and differential.
GenevestigatoriP29622.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GLYCOSYLATION AT ASN-238.

Entry informationi

Entry nameiKAIN_HUMAN
AccessioniPrimary (citable) accession number: P29622
Secondary accession number(s): Q53XB5, Q86TR9, Q96BZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 21, 2005
Last modified: April 29, 2015
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.