ID   SPA33_BOVIN             Reviewed;         411 AA.
AC   Q3ZEJ6; Q2T9M2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Serpin A3-3;
DE   AltName: Full=Endopin-1B;
DE   AltName: Full=Muscle endopin-1B;
DE            Short=mEndopin-1B;
DE   Flags: Precursor;
GN   Name=SERPINA3-3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-37, FUNCTION, AND
RP   SUBUNIT.
RC   TISSUE=Muscle;
RX   PubMed=16716310; DOI=10.1016/j.febslet.2006.04.099;
RA   Herrera-Mendez C.H., Bremaud L., Coulis G., Pelissier P., Sentandreu M.A.,
RA   Aubry L., Delourme D., Chambon C., Maftah A., Leveziel H., Ouali A.;
RT   "Purification of the skeletal muscle protein endopin 1B and
RT   characterization of the genes encoding endopin 1A and 1B isoforms.";
RL   FEBS Lett. 580:3477-3484(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=18384666; DOI=10.1186/1471-2164-9-151;
RA   Pelissier P., Delourme D., Germot A., Blanchet X., Becila S., Maftah A.,
RA   Leveziel H., Ouali A., Bremaud L.;
RT   "An original SERPINA3 gene cluster: elucidation of genomic organization and
RT   gene expression in the Bos taurus 21q24 region.";
RL   BMC Genomics 9:151-151(2008).
CC   -!- FUNCTION: Serine protease inhibitor. Strongly inhibits elastase and
CC       trypsin stoichiometrically at the molar ratio of 1:1. Acts as a
CC       moderate inhibitor of plasmin and chymotrypsin. Does not inhibit
CC       thrombin, urokinase, kallikrein, tissue plasminogen activator,
CC       cathepsin G or the cysteine proteases papain, cathepsin B or cathepsin
CC       L. {ECO:0000269|PubMed:16716310}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16716310}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       chromaffin granule {ECO:0000250}. Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; BC111356; AAI11357.1; -; mRNA.
DR   EMBL; AY911537; AAY22406.2; -; Genomic_DNA.
DR   RefSeq; NP_001033293.1; NM_001038204.2.
DR   AlphaFoldDB; Q3ZEJ6; -.
DR   SMR; Q3ZEJ6; -.
DR   IntAct; Q3ZEJ6; 2.
DR   MINT; Q3ZEJ6; -.
DR   STRING; 9913.ENSBTAP00000055847; -.
DR   MEROPS; I04.027; -.
DR   PaxDb; Q3ZEJ6; -.
DR   GeneID; 615103; -.
DR   KEGG; bta:615103; -.
DR   CTD; 615103; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q3ZEJ6; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Direct protein sequencing; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..411
FT                   /note="Serpin A3-3"
FT                   /id="PRO_0000392468"
FT   SITE            377..378
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   411 AA;  46326 MW;  70B31CD4D8A8DBC5 CRC64;
     MRAERLSPLL ALGLLVAGIR SVHCLPENVV VKDRHRRVDG HTLASSNTDF AFSLYKQLAL
     KNPNKNVMFS PLSVSMALAF LSLGARGPTL TEILEGLKFN LTEIQETQIH QGFQHLLQAL
     NRPRNQLQLS VGNAMFVQEE LKLLDKFIED ARVLYSSEAF PTNFRDPEAA KSLINDYVKN
     KTQGKIEELF KDLSPRTELV LVNYVYFKAQ WKTRFDPKHT EQAEFHVSDN KTVEVPMMTL
     DLETPYFRDE ELGCTLVELT YTSNDSALFI LPDKGKMQDL EAKLTPEMLT RWRNSLQPRR
     IHELYLPKFS IKSNYELNDT LSQMGIKKIF TDADLSGITG TADLVVSQVV HGAALDVDEE
     GTEGAAATGI GIERTFLRII VRVNRPFLIA VVLKDTQSII FLGKVTNPSE A