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SPB6_MACFA
ID   SPB6_MACFA              Reviewed;         376 AA.
AC   Q4R3G2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Serpin B6;
GN   Name=SERPINB6; ORFNames=QtsA-17114;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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; AB179304; BAE02355.1; -; mRNA.
DR   RefSeq; NP_001272307.1; NM_001285378.1.
DR   AlphaFoldDB; Q4R3G2; -.
DR   SMR; Q4R3G2; -.
DR   STRING; 9541.XP_005593412.1; -.
DR   MEROPS; I04.011; -.
DR   PRIDE; Q4R3G2; -.
DR   GeneID; 101866493; -.
DR   CTD; 5269; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   Proteomes; UP000233100; 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_0000311815"
FT   SITE            341..342
FT                   /note="Reactive bond"
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;  42500 MW;  F053BB296C25B429 CRC64;
     MDVLAEANGT FALNLLKTLG KDNSKNVFFS PMSMSCALAM VYMGAKGNTA AQMAQVLSFN
     KSGGGGDIHQ GFQSLLTEVN KTGTQYLLRT ANRLFGEKSC DFLSSFRDSC QKFYQAEMEE
     LDFISAVEKS RKHINSWVAE KTEGKIAELL SPGSVDPLTR LVLVNAVYFK GNWNEQFDKE
     NTEERRFKVS KNEEKPVQMM FMQSTFRKTY IGEIFTQILV LPYVGKELNM IIMLPDETTD
     LRTVEKELTY EKFVEWTRLD MMDEEKVEVS LPRFKLEESY DMESVLCSLG MTDAFELGKA
     DFSGMSKADL CLSKVVHKSF VEVNEEGTEA AAATAAIMMM RCARFVPRFC ADHPFLFFIQ
     HSKTNGVLFC GRFSSP
 
 
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