P29622 (KAIN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kallistatin

Alternative name(s):
Kallikrein inhibitor
Peptidase inhibitor 4
Short name=PI-4
Serpin A4

Gene names

Name:	SERPINA4
Synonyms:	KST, PI4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 427	407	Kallistatin		PRO_0000032425
Sites
	Site	388 – 389	2	Reactive bond
Amino acid modifications
	Glycosylation	33	1	N-linked (GlcNAc...) Potential
	Glycosylation	108	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	157	1	N-linked (GlcNAc...) Ref.6 Ref.7
	Glycosylation	238	1	N-linked (GlcNAc...) Ref.7
Experimental info
	Sequence conflict	382	1	S → T Ref.1
	Sequence conflict	382	1	S → T Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P29622 [UniParc]. Last modified June 21, 2005. Version 3. Checksum: 68EBE7AF956BFB77	FASTA	427	48,542
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. Tissue: Plasma.

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.
IPI	IPI00328609.
PIR	A49518.
RefSeq	NP_006206.2. NM_006215.2.
UniGene	Hs.719893.
3D structure databases
ProteinModelPortal	P29622.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000298841.
Protein family/group databases
MEROPS	I04.003.
PTM databases
PhosphoSite	P29622.
Polymorphism databases
DMDM	68067608.
Proteomic databases
PaxDb	P29622.
PeptideAtlas	P29622.
PRIDE	P29622.
Protocols and materials databases
DNASU	5267.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000298841; ENSP00000298841; ENSG00000100665. ENST00000555095; ENSP00000451172; ENSG00000100665. ENST00000557004; ENSP00000450838; ENSG00000100665.
GeneID	5267.
KEGG	hsa:5267.
UCSC	uc001ydk.3. human.
Organism-specific databases
CTD	5267.
GeneCards	GC14P095027.
HGNC	HGNC:8948. SERPINA4.
HPA	HPA003607.
MIM	147935. gene.
neXtProt	NX_P29622.
PharmGKB	PA35514.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4826.
HOGENOM	HOG000238521.
HOVERGEN	HBG005957.
InParanoid	P29622.
OMA	HHWYLHD.
OrthoDB	EOG4FFD1T.
Gene expression databases
Bgee	P29622.
Genevestigator	P29622.
GermOnline	ENSG00000100665. Homo sapiens.
Family and domain databases
InterPro	IPR023795. Protease_inhib_I4_serpin_CS. IPR023796. Serpin_dom. IPR000215. Serpin_fam. [Graphical view]
PANTHER	PTHR11461. PTHR11461. 1 hit.
Pfam	PF00079. Serpin. 1 hit. [Graphical view]
SMART	SM00093. SERPIN. 1 hit. [Graphical view]
SUPFAM	SSF56574. Prot_inh_serpin. 1 hit.
PROSITE	PS00284. SERPIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5267.
NextBio	20348.
SOURCE	Search...

Entry information

Entry name

KAIN_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.