SPA33_BOVIN
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