Full text data of SERPINA4
SERPINA4
(KST, PI4)
[Confidence: low (only semi-automatic identification from reviews)]
Kallistatin (Kallikrein inhibitor; Peptidase inhibitor 4; PI-4; Serpin A4; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Kallistatin (Kallikrein inhibitor; Peptidase inhibitor 4; PI-4; Serpin A4; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P29622
ID KAIN_HUMAN Reviewed; 427 AA.
AC P29622; Q53XB5; Q86TR9; Q96BZ5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-JUN-2005, sequence version 3.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Kallistatin;
DE AltName: Full=Kallikrein inhibitor;
DE AltName: Full=Peptidase inhibitor 4;
DE Short=PI-4;
DE AltName: Full=Serpin A4;
DE Flags: Precursor;
GN Name=SERPINA4; Synonyms=KST, PI4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8227002;
RA Chai K.X., Chen L.-M., Chao J., Chao L.;
RT "Kallistatin: a novel human serine proteinase inhibitor. Molecular
RT cloning, tissue distribution, and expression in Escherichia coli.";
RL J. Biol. Chem. 268:24498-24505(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7835886; DOI=10.1006/geno.1994.1513;
RA Chai K.X., Ward D.C., Chao J., Chao L.;
RT "Molecular cloning, sequence analysis, and chromosomal localization of
RT the human protease inhibitor 4 (kallistatin) gene (PI4).";
RL Genomics 23:370-378(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal liver;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 388-403.
RC TISSUE=Plasma;
RX PubMed=1334488;
RA Zhou G.X., Chao L., Chao J.;
RT "Kallistatin: a novel human tissue kallikrein inhibitor. Purification,
RT characterization, and reactive center sequence.";
RL J. Biol. Chem. 267:25873-25880(1992).
RN [6]
RP GLYCOSYLATION AT ASN-157.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108; ASN-157 AND ASN-238,
RP AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP GLYCOSYLATION AT ASN-238.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
CC -!- FUNCTION: Inhibits human amidolytic and kininogenase activities of
CC tissue kallikrein. Inhibition is achieved by formation of an
CC equimolar, heat- and SDS-stable complex between the inhibitor and
CC the enzyme, and generation of a small C-terminal fragment of the
CC inhibitor due to cleavage at the reactive site by tissue
CC kallikrein.
CC -!- SUBUNIT: Monomer and some homodimers.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Heparin blocks kallistatin's complex formation with
CC tissue kallikrein and abolishes its inhibitory effect on tissue
CC kallikrein's activity.
CC -!- SIMILARITY: Belongs to the serpin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD66567.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L19684; AAA59454.1; -; mRNA.
DR EMBL; L28101; AAC41706.1; -; Genomic_DNA.
DR EMBL; BX248009; CAD62337.1; -; mRNA.
DR EMBL; BX248760; CAD66567.1; ALT_INIT; mRNA.
DR EMBL; BC014992; AAH14992.1; -; mRNA.
DR PIR; A49518; A49518.
DR RefSeq; NP_006206.2; NM_006215.2.
DR RefSeq; XP_005267820.1; XM_005267763.1.
DR UniGene; Hs.719893; -.
DR ProteinModelPortal; P29622; -.
DR SMR; P29622; 57-424.
DR IntAct; P29622; 10.
DR MINT; MINT-8247389; -.
DR STRING; 9606.ENSP00000298841; -.
DR MEROPS; I04.003; -.
DR PhosphoSite; P29622; -.
DR DMDM; 68067608; -.
DR PaxDb; P29622; -.
DR PeptideAtlas; P29622; -.
DR PRIDE; P29622; -.
DR DNASU; 5267; -.
DR Ensembl; ENST00000298841; ENSP00000298841; ENSG00000100665.
DR Ensembl; ENST00000555095; ENSP00000451172; ENSG00000100665.
DR Ensembl; ENST00000557004; ENSP00000450838; ENSG00000100665.
DR GeneID; 5267; -.
DR KEGG; hsa:5267; -.
DR UCSC; uc001ydk.3; human.
DR CTD; 5267; -.
DR GeneCards; GC14P095027; -.
DR HGNC; HGNC:8948; SERPINA4.
DR HPA; HPA003607; -.
DR MIM; 147935; gene.
DR neXtProt; NX_P29622; -.
DR PharmGKB; PA35514; -.
DR eggNOG; COG4826; -.
DR HOGENOM; HOG000238521; -.
DR HOVERGEN; HBG005957; -.
DR InParanoid; P29622; -.
DR OMA; HHWYLHD; -.
DR OrthoDB; EOG7QC7W9; -.
DR GeneWiki; SERPINA4; -.
DR GenomeRNAi; 5267; -.
DR NextBio; 20348; -.
DR PRO; PR:P29622; -.
DR Bgee; P29622; -.
DR Genevestigator; P29622; -.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:RefGenome.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:RefGenome.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Glycoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1 20 Potential.
FT CHAIN 21 427 Kallistatin.
FT /FTId=PRO_0000032425.
FT SITE 388 389 Reactive bond.
FT CARBOHYD 33 33 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 108 108 N-linked (GlcNAc...).
FT CARBOHYD 157 157 N-linked (GlcNAc...).
FT CARBOHYD 238 238 N-linked (GlcNAc...) (complex).
FT CONFLICT 382 382 S -> T (in Ref. 1 and 2).
SQ SEQUENCE 427 AA; 48542 MW; 68EBE7AF956BFB77 CRC64;
MHLIDYLLLL LVGLLALSHG QLHVEHDGES CSNSSHQQIL ETGEGSPSLK IAPANADFAF
RFYYLIASET PGKNIFFSPL SISAAYAMLS LGACSHSRSQ ILEGLGFNLT ELSESDVHRG
FQHLLHTLNL PGHGLETRVG SALFLSHNLK FLAKFLNDTM AVYEAKLFHT NFYDTVGTIQ
LINDHVKKET RGKIVDLVSE LKKDVLMVLV NYIYFKALWE KPFISSRTTP KDFYVDENTT
VRVPMMLQDQ EHHWYLHDRY LPCSVLRMDY KGDATVFFIL PNQGKMREIE EVLTPEMLMR
WNNLLRKRNF YKKLELHLPK FSISGSYVLD QILPRLGFTD LFSKWADLSG ITKQQKLEAS
KSFHKATLDV DEAGTEAAAA TSFAIKFFSA QTNRHILRFN RPFLVVIFST STQSVLFLGK
VVDPTKP
//
ID KAIN_HUMAN Reviewed; 427 AA.
AC P29622; Q53XB5; Q86TR9; Q96BZ5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-JUN-2005, sequence version 3.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Kallistatin;
DE AltName: Full=Kallikrein inhibitor;
DE AltName: Full=Peptidase inhibitor 4;
DE Short=PI-4;
DE AltName: Full=Serpin A4;
DE Flags: Precursor;
GN Name=SERPINA4; Synonyms=KST, PI4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8227002;
RA Chai K.X., Chen L.-M., Chao J., Chao L.;
RT "Kallistatin: a novel human serine proteinase inhibitor. Molecular
RT cloning, tissue distribution, and expression in Escherichia coli.";
RL J. Biol. Chem. 268:24498-24505(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7835886; DOI=10.1006/geno.1994.1513;
RA Chai K.X., Ward D.C., Chao J., Chao L.;
RT "Molecular cloning, sequence analysis, and chromosomal localization of
RT the human protease inhibitor 4 (kallistatin) gene (PI4).";
RL Genomics 23:370-378(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal liver;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 388-403.
RC TISSUE=Plasma;
RX PubMed=1334488;
RA Zhou G.X., Chao L., Chao J.;
RT "Kallistatin: a novel human tissue kallikrein inhibitor. Purification,
RT characterization, and reactive center sequence.";
RL J. Biol. Chem. 267:25873-25880(1992).
RN [6]
RP GLYCOSYLATION AT ASN-157.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108; ASN-157 AND ASN-238,
RP AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP GLYCOSYLATION AT ASN-238.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
CC -!- FUNCTION: Inhibits human amidolytic and kininogenase activities of
CC tissue kallikrein. Inhibition is achieved by formation of an
CC equimolar, heat- and SDS-stable complex between the inhibitor and
CC the enzyme, and generation of a small C-terminal fragment of the
CC inhibitor due to cleavage at the reactive site by tissue
CC kallikrein.
CC -!- SUBUNIT: Monomer and some homodimers.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Heparin blocks kallistatin's complex formation with
CC tissue kallikrein and abolishes its inhibitory effect on tissue
CC kallikrein's activity.
CC -!- SIMILARITY: Belongs to the serpin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD66567.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L19684; AAA59454.1; -; mRNA.
DR EMBL; L28101; AAC41706.1; -; Genomic_DNA.
DR EMBL; BX248009; CAD62337.1; -; mRNA.
DR EMBL; BX248760; CAD66567.1; ALT_INIT; mRNA.
DR EMBL; BC014992; AAH14992.1; -; mRNA.
DR PIR; A49518; A49518.
DR RefSeq; NP_006206.2; NM_006215.2.
DR RefSeq; XP_005267820.1; XM_005267763.1.
DR UniGene; Hs.719893; -.
DR ProteinModelPortal; P29622; -.
DR SMR; P29622; 57-424.
DR IntAct; P29622; 10.
DR MINT; MINT-8247389; -.
DR STRING; 9606.ENSP00000298841; -.
DR MEROPS; I04.003; -.
DR PhosphoSite; P29622; -.
DR DMDM; 68067608; -.
DR PaxDb; P29622; -.
DR PeptideAtlas; P29622; -.
DR PRIDE; P29622; -.
DR DNASU; 5267; -.
DR Ensembl; ENST00000298841; ENSP00000298841; ENSG00000100665.
DR Ensembl; ENST00000555095; ENSP00000451172; ENSG00000100665.
DR Ensembl; ENST00000557004; ENSP00000450838; ENSG00000100665.
DR GeneID; 5267; -.
DR KEGG; hsa:5267; -.
DR UCSC; uc001ydk.3; human.
DR CTD; 5267; -.
DR GeneCards; GC14P095027; -.
DR HGNC; HGNC:8948; SERPINA4.
DR HPA; HPA003607; -.
DR MIM; 147935; gene.
DR neXtProt; NX_P29622; -.
DR PharmGKB; PA35514; -.
DR eggNOG; COG4826; -.
DR HOGENOM; HOG000238521; -.
DR HOVERGEN; HBG005957; -.
DR InParanoid; P29622; -.
DR OMA; HHWYLHD; -.
DR OrthoDB; EOG7QC7W9; -.
DR GeneWiki; SERPINA4; -.
DR GenomeRNAi; 5267; -.
DR NextBio; 20348; -.
DR PRO; PR:P29622; -.
DR Bgee; P29622; -.
DR Genevestigator; P29622; -.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:RefGenome.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:RefGenome.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Glycoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1 20 Potential.
FT CHAIN 21 427 Kallistatin.
FT /FTId=PRO_0000032425.
FT SITE 388 389 Reactive bond.
FT CARBOHYD 33 33 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 108 108 N-linked (GlcNAc...).
FT CARBOHYD 157 157 N-linked (GlcNAc...).
FT CARBOHYD 238 238 N-linked (GlcNAc...) (complex).
FT CONFLICT 382 382 S -> T (in Ref. 1 and 2).
SQ SEQUENCE 427 AA; 48542 MW; 68EBE7AF956BFB77 CRC64;
MHLIDYLLLL LVGLLALSHG QLHVEHDGES CSNSSHQQIL ETGEGSPSLK IAPANADFAF
RFYYLIASET PGKNIFFSPL SISAAYAMLS LGACSHSRSQ ILEGLGFNLT ELSESDVHRG
FQHLLHTLNL PGHGLETRVG SALFLSHNLK FLAKFLNDTM AVYEAKLFHT NFYDTVGTIQ
LINDHVKKET RGKIVDLVSE LKKDVLMVLV NYIYFKALWE KPFISSRTTP KDFYVDENTT
VRVPMMLQDQ EHHWYLHDRY LPCSVLRMDY KGDATVFFIL PNQGKMREIE EVLTPEMLMR
WNNLLRKRNF YKKLELHLPK FSISGSYVLD QILPRLGFTD LFSKWADLSG ITKQQKLEAS
KSFHKATLDV DEAGTEAAAA TSFAIKFFSA QTNRHILRFN RPFLVVIFST STQSVLFLGK
VVDPTKP
//
MIM
147935
*RECORD*
*FIELD* NO
147935
*FIELD* TI
*147935 SERPIN PEPTIDASE INHIBITOR, CLADE A, MEMBER 4; SERPINA4
;;KALLISTATIN; KST;;
read moreTISSUE KALLIKREIN INHIBITOR;;
PROTEASE INHIBITOR 4; PI4
*FIELD* TX
CLONING
Zhou et al. (1992) purified and characterized a human tissue kallikrein
inhibitor from plasma which rapidly bound to tissue kallikrein and
inhibited its activity. Designated kallistatin, this tissue kallikrein
inhibitor is a member of the serpin superfamily and represents a major
inhibitor of human tissue kallikrein in the circulation.
Chai et al. (1993) cloned a full-length SERPINA4 cDNA encoding
kallistatin from human liver RNA by PCR. The 1,284-bp cDNA encodes 427
amino acid residues, including a 26-residue signal peptide and a
401-residue mature peptide. The translated amino acid sequence of
kallistatin matches the protein sequence and shares 44 to 46% sequence
identity with other serpin family members including, human
alpha-1-antichymotrypsin (AACT; 107280), alpha-1-antitrypsin (PI;
107400), corticosteroid-binding globulin (CBG; 122500),
thyroxine-binding globulin of serum (TBG; 314200), and protein C
inhibitor (PCI; 601841).
MAPPING
By screening a chromosome 14-specific genomic DNA library, Chai et al.
(1993) localized the SERPINA4 gene to chromosome 14. By FISH analysis,
Chai et al. (1994) localized the SERPINA4 gene to chromosome
14q31-q32.1, close to the serpin genes AACT, PCI, PI, and CBG.
GENE FUNCTION
Kallistatin is a serine proteinase inhibitor (serpin) and a
heparin-binding protein. It is localized in vascular smooth muscle cells
and endothelial cells of blood vessels, suggesting that it may be
involved in the regulation of vascular function. Miao et al. (2000)
showed that kallistatin plays a role in neointima hyperplasia. Miao et
al. (2002) investigated the potential role of kallistatin in
angiogenesis in vitro and in vivo, and presented results demonstrating a
novel role of the protein in the inhibition of angiogenesis and tumor
growth.
*FIELD* RF
1. Chai, K. X.; Chen, L.-M.; Chao, J.; Chao, L.: Kallistatin: a novel
human serine proteinase inhibitor: molecular cloning, tissue distribution,
and expression in Escherichia coli. J. Biol. Chem. 268: 24498-24505,
1993.
2. Chai, K. X.; Ward, D. C.; Chao, J.; Chao, L.: Molecular cloning,
sequence analysis, and chromosomal localization of the human protease
inhibitor 4 (kallistatin) gene (PI4). Genomics 23: 370-378, 1994.
3. Miao, R. Q.; Agata, J.; Chao, L.; Chao, J.: Kallistatin is a new
inhibitor of angiogenesis and tumor growth. Blood 100: 3245-3252,
2002.
4. Miao, R. Q.; Murakami, H.; Song, Q.; Chao, L.; Chao, J.: Kallistatin
stimulates vascular smooth muscle cell proliferation and migration
in vitro and neointima formation in balloon-injured rat artery. Circ.
Res. 86: 418-424, 2000.
5. Zhou, G. X.; Chao, L.; Chao, J.: Kallistatin: a novel human tissue
kallikrein inhibitor; purification, characterization, and reactive
center sequence. J. Biol. Chem. 267: 25873-25880, 1992.
*FIELD* CN
Victor A. McKusick - updated: 12/30/2002
*FIELD* CD
Victor A. McKusick: 2/1/1993
*FIELD* ED
wwang: 03/30/2010
carol: 10/4/2007
tkritzer: 2/10/2003
tkritzer: 1/6/2003
terry: 12/30/2002
terry: 3/13/2002
mark: 10/14/1997
carol: 11/30/1994
pfoster: 5/9/1994
carol: 2/1/1993
*RECORD*
*FIELD* NO
147935
*FIELD* TI
*147935 SERPIN PEPTIDASE INHIBITOR, CLADE A, MEMBER 4; SERPINA4
;;KALLISTATIN; KST;;
read moreTISSUE KALLIKREIN INHIBITOR;;
PROTEASE INHIBITOR 4; PI4
*FIELD* TX
CLONING
Zhou et al. (1992) purified and characterized a human tissue kallikrein
inhibitor from plasma which rapidly bound to tissue kallikrein and
inhibited its activity. Designated kallistatin, this tissue kallikrein
inhibitor is a member of the serpin superfamily and represents a major
inhibitor of human tissue kallikrein in the circulation.
Chai et al. (1993) cloned a full-length SERPINA4 cDNA encoding
kallistatin from human liver RNA by PCR. The 1,284-bp cDNA encodes 427
amino acid residues, including a 26-residue signal peptide and a
401-residue mature peptide. The translated amino acid sequence of
kallistatin matches the protein sequence and shares 44 to 46% sequence
identity with other serpin family members including, human
alpha-1-antichymotrypsin (AACT; 107280), alpha-1-antitrypsin (PI;
107400), corticosteroid-binding globulin (CBG; 122500),
thyroxine-binding globulin of serum (TBG; 314200), and protein C
inhibitor (PCI; 601841).
MAPPING
By screening a chromosome 14-specific genomic DNA library, Chai et al.
(1993) localized the SERPINA4 gene to chromosome 14. By FISH analysis,
Chai et al. (1994) localized the SERPINA4 gene to chromosome
14q31-q32.1, close to the serpin genes AACT, PCI, PI, and CBG.
GENE FUNCTION
Kallistatin is a serine proteinase inhibitor (serpin) and a
heparin-binding protein. It is localized in vascular smooth muscle cells
and endothelial cells of blood vessels, suggesting that it may be
involved in the regulation of vascular function. Miao et al. (2000)
showed that kallistatin plays a role in neointima hyperplasia. Miao et
al. (2002) investigated the potential role of kallistatin in
angiogenesis in vitro and in vivo, and presented results demonstrating a
novel role of the protein in the inhibition of angiogenesis and tumor
growth.
*FIELD* RF
1. Chai, K. X.; Chen, L.-M.; Chao, J.; Chao, L.: Kallistatin: a novel
human serine proteinase inhibitor: molecular cloning, tissue distribution,
and expression in Escherichia coli. J. Biol. Chem. 268: 24498-24505,
1993.
2. Chai, K. X.; Ward, D. C.; Chao, J.; Chao, L.: Molecular cloning,
sequence analysis, and chromosomal localization of the human protease
inhibitor 4 (kallistatin) gene (PI4). Genomics 23: 370-378, 1994.
3. Miao, R. Q.; Agata, J.; Chao, L.; Chao, J.: Kallistatin is a new
inhibitor of angiogenesis and tumor growth. Blood 100: 3245-3252,
2002.
4. Miao, R. Q.; Murakami, H.; Song, Q.; Chao, L.; Chao, J.: Kallistatin
stimulates vascular smooth muscle cell proliferation and migration
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*FIELD* CN
Victor A. McKusick - updated: 12/30/2002
*FIELD* CD
Victor A. McKusick: 2/1/1993
*FIELD* ED
wwang: 03/30/2010
carol: 10/4/2007
tkritzer: 2/10/2003
tkritzer: 1/6/2003
terry: 12/30/2002
terry: 3/13/2002
mark: 10/14/1997
carol: 11/30/1994
pfoster: 5/9/1994
carol: 2/1/1993