ID   SPB6_PONAB              Reviewed;         376 AA.
AC   Q5R899;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Serpin B6;
GN   Name=SERPINB6;
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=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play
CC       an important role in the inner ear in the protection against leakage of
CC       lysosomal content during stress. May be involved in the regulation of
CC       serine proteinases present in the brain or extravasated from the blood
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with the monomeric form of beta-tryptase.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR859854; CAH92011.1; -; mRNA.
DR   RefSeq; NP_001126167.1; NM_001132695.2.
DR   AlphaFoldDB; Q5R899; -.
DR   SMR; Q5R899; -.
DR   STRING; 9601.ENSPPYP00000018091; -.
DR   MEROPS; I04.011; -.
DR   PRIDE; Q5R899; -.
DR   GeneID; 100173128; -.
DR   KEGG; pon:100173128; -.
DR   CTD; 5269; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q5R899; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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   Acetylation; Cytoplasm; Phosphoprotein; Protease inhibitor;
KW   Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..376
FT                   /note="Serpin B6"
FT                   /id="PRO_0000230780"
FT   SITE            341..342
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P35237"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35237"
FT   MOD_RES         195
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60854"
SQ   SEQUENCE   376 AA;  42608 MW;  50DCFC7A45142B47 CRC64;
     MDVLAEANGT FALNLLKTLG KDNSKNVFFS PMSMSCALAM VYMGAKGNTA AQMAQVLSFN
     KSGSGGDIHQ GFQSLLTEVN KTGTQYLLRT ANRLFGEKSC DFLSSFRDSC QKFYQAEMEE
     LDFISAVEKS RKHINTWVAE KTEGKIAELL SPGSVDPLTR LVLVNAVYFR GNWDEQFDKE
     NTEERLFKVS KNEEKPVQMM FKQSTFKKTY IGEIFTQILV LPYVGKELNM IIMLPDETTD
     LRTVEKELTY EKFVEWTRLD MMDEEEVEVS LPRFKLEESY DMESVLRNLG MTDAFELGKA
     DFSGMSQTDL SLSKVVHKSF VEVNEEGTEA AAATAAIMMM RCARFVPRFC ADHPFLFFIQ
     HSKTNGILFC GRFSSP