SPA31_BOVIN
ID SPA31_BOVIN Reviewed; 411 AA.
AC Q9TTE1; Q2KIQ9; Q3ZEJ7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Serpin A3-1 {ECO:0000303|PubMed:18384666};
DE AltName: Full=Endopin-1A {ECO:0000303|PubMed:10567388, ECO:0000303|PubMed:15647007, ECO:0000312|EMBL:AAF23888.2};
DE AltName: Full=Muscle endopin-1A {ECO:0000303|PubMed:10567388, ECO:0000303|PubMed:15647007, ECO:0000312|EMBL:AAF23888.2};
DE Short=mEndopin-1A {ECO:0000303|PubMed:10567388, ECO:0000303|PubMed:15647007, ECO:0000312|EMBL:AAF23888.2};
DE Flags: Precursor;
GN Name=SERPINA3-1 {ECO:0000303|PubMed:18384666}; Synonyms=SERPINA3A;
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] {ECO:0000305, ECO:0000312|EMBL:AAF23888.2}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Adrenal medulla {ECO:0000269|PubMed:10567388};
RX PubMed=10567388; DOI=10.1074/jbc.274.48.34164;
RA Hwang S.-R., Steineckert B., Yasothornsrikul S., Sei C.A., Toneff T.,
RA Rattan J., Hook V.Y.H.;
RT "Molecular cloning of endopin 1, a novel serpin localized to neurosecretory
RT vesicles of chromaffin cells. Inhibition of basic residue-cleaving
RT proteases by endopin 1.";
RL J. Biol. Chem. 274:34164-34173(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF23888.2}
RP SEQUENCE REVISION TO 113-152.
RC TISSUE=Adrenal medulla {ECO:0000269|PubMed:10567388};
RA Hwang S.-R., Steineckert B., Yasothornsrikul S., Sei C.A., Toneff T.,
RA Rattan J., Kang Y.-H., Hook V.Y.H.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-38 AND 313-327,
RP AND SUBUNIT.
RC TISSUE=Muscle {ECO:0000269|PubMed:16716310};
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAF23888.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 25-38 AND 313-327, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Diaphragm {ECO:0000269|PubMed:15647007};
RX PubMed=15647007; DOI=10.1042/bj20041921;
RA Tassy C., Herrera-Mendez C.H., Sentandreu M.A., Aubry L., Bremaud L.,
RA Pelissier P., Delourme D., Brillard M., Gauthier F., Leveziel H., Ouali A.;
RT "Muscle endopin 1, a muscle intracellular serpin inhibiting strongly
RT elastase: purification, characterization, cellular localization and tissue
RT distribution.";
RL Biochem. J. 388:273-280(2005).
RN [6]
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: Potent inhibitor of the serine proteases elastase and
CC trypsin. Moderately inhibits the serine proteases plasmin and
CC chymotrypsin, and the thiol protease proenkephalin-processing enzyme.
CC Does not inhibit the serine proteases cathepsin G, furin, kallikrein,
CC thrombin, tissue plasminogen activator and urokinase, or the cysteine
CC proteases cathepsin B, cathepsin L and papain.
CC {ECO:0000269|PubMed:10567388, ECO:0000269|PubMed:15647007}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Stable in the pH range 4.0-12.0. Incubation at a pH below 4.0 rapidly
CC decreases inhibitory activity. {ECO:0000269|PubMed:15647007};
CC Temperature dependence:
CC Stable at temperatures up to 70 degrees Celsius. Incubation at
CC temperatures above 70 degrees Celsius rapidly decreases inhibitory
CC activity. {ECO:0000269|PubMed:15647007};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16716310}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule {ECO:0000269|PubMed:10567388,
CC ECO:0000269|PubMed:15647007}. Secreted {ECO:0000269|PubMed:10567388,
CC ECO:0000269|PubMed:15647007}. Note=In longissimus muscle myocytes
CC highest levels are found between the plasma membrane and the myofibrils
CC and lower levels are found within the myofibrils. Localized to the
CC chromaffin granules of the adrenal medulla and secreted in response to
CC nicotine or KCL depolarization. {ECO:0000269|PubMed:10567388,
CC ECO:0000269|PubMed:15647007}.
CC -!- TISSUE SPECIFICITY: Detected in all tissues examined (at protein
CC level). Abundantly expressed in liver, kidney and spleen. Lowest levels
CC were observed in diaphragm muscle. {ECO:0000269|PubMed:10567388,
CC ECO:0000269|PubMed:15647007}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10567388}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000255}.
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DR EMBL; AF125526; AAF23888.2; -; mRNA.
DR EMBL; AY911536; AAY22405.2; -; Genomic_DNA.
DR EMBL; BC112546; AAI12547.1; -; mRNA.
DR RefSeq; NP_777193.2; NM_174768.2.
DR AlphaFoldDB; Q9TTE1; -.
DR SMR; Q9TTE1; -.
DR IntAct; Q9TTE1; 2.
DR MINT; Q9TTE1; -.
DR STRING; 9913.ENSBTAP00000042480; -.
DR MEROPS; I04.027; -.
DR PaxDb; Q9TTE1; -.
DR PRIDE; Q9TTE1; -.
DR GeneID; 286804; -.
DR KEGG; bta:286804; -.
DR CTD; 286804; -.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; Q9TTE1; -.
DR OrthoDB; 1124079at2759; -.
DR TreeFam; TF343201; -.
DR SABIO-RK; Q9TTE1; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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:0000269|PubMed:15647007,
FT ECO:0000269|PubMed:16716310"
FT CHAIN 25..411
FT /note="Serpin A3-1"
FT /evidence="ECO:0000269|PubMed:15647007"
FT /id="PRO_0000229752"
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 CONFLICT 20
FT /note="R -> P (in Ref. 1; AAF23888)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="A -> P (in Ref. 1; AAF23888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46237 MW; BF94BD4AB4D9C44A CRC64;
MRAERTSFLL ALGLLVAGIR SVHCLPENVV VKDQHRRVDG HTLASSNTDF AFSLYKQLAL
KNPNKNVILS PLSVSIALAF LSLGARGSTL TEILEGLKFN LTEIQEKEIH HSFQHLLQAL
NQPSNQLQLS VGNAMFVQEE LKLLDKFIED AQVLYSSEAF PTNFRDSEAA RSLINDYVKN
KTQGKIEELF KYLSPRTELV LVNYIYFKAQ WKTPFDPKHT EQAEFHVSDN KTVEVPMMTL
DLETPYFRDE ELGCTLVELT YTSNDSALFI LPDEGKMRDL EAKLTPETLT RWRNSLQPRR
IHELYLPKFS IKSNYELNDI LSQLGIRKIF ANADLSGITG TADLVVSQVV HGAALDVDEE
GTEGAAATGI SMERTILRII VRVNRPFLIA IVLKDTQSII FLGKVTNPSE A
