ID   KAIN_PONAB              Reviewed;         427 AA.
AC   Q5RCR2;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Kallistatin;
DE   AltName: Full=Serpin A4;
DE   Flags: Precursor;
GN   Name=SERPINA4;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits human amidolytic and kininogenase activities of
CC       tissue kallikrein. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer and some homodimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; CR858207; CAH90445.1; -; mRNA.
DR   RefSeq; NP_001125226.1; NM_001131754.1.
DR   RefSeq; XP_009247727.1; XM_009249452.1.
DR   RefSeq; XP_009247728.1; XM_009249453.1.
DR   AlphaFoldDB; Q5RCR2; -.
DR   SMR; Q5RCR2; -.
DR   STRING; 9601.ENSPPYP00000006944; -.
DR   MEROPS; I04.003; -.
DR   PRIDE; Q5RCR2; -.
DR   GeneID; 100172119; -.
DR   KEGG; pon:100172119; -.
DR   CTD; 5267; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; Q5RCR2; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000001595; Chromosome 14.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
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   2: Evidence at transcript level;
KW   Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..427
FT                   /note="Kallistatin"
FT                   /id="PRO_0000032426"
FT   SITE            388..389
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   427 AA;  48558 MW;  24E05E0197F927ED CRC64;
     MHLIDYLLLL LVGLLALSHG QLHVEHDGES CSNSSHQQIL ETGEGSPSLK IAPANADFAF
     RFYYLIASET PGKNIFFSPL SISAAYAMLS LGACSHSRSQ ILEGLGFNLT ELSESDVHRG
     FQHLLHTLNL PGHGLETRVG SALFLSHNLK FLAKFLNDTM TFYEAKLFHT NFYDTVGTIQ
     LINDHVKKET RGKIVDLVSE LKKDVLMVLV NYIYFKALWE KPFISSRTTP KDFYVDENTT
     VRVPMMLQDQ EHHWYLHDRY LPCSVLRMDY KGDTTVFFIL PNQGKMGEIE EVLTPEMLMR
     WNNLLQKRNF YKKLELHFPK FSISGSYVLD QILPRLGFTD LFSKRADLSG ITKQQKLEAS
     KSFHKATLDV DEAGTEAAAA TSFAIKFFSA QTNRHILRFN RPFLVVIFST STQSVLFLGK
     VVDPTKQ