ID   A1AT2_HORSE             Reviewed;         421 AA.
AC   P38029; O46519;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Alpha-1-antiproteinase 2;
DE   AltName: Full=Alpha-1-antitrypsin 2;
DE   AltName: Full=Alpha-1-proteinase inhibitor 2;
DE   AltName: Full=SPI2;
DE   Flags: Precursor;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Giffard J.M., Irvin Z.V., Bell T.K., Brandon R.B.;
RT   "Equine alpha-1-antitrypsin gene.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 25-43 AND 381-412.
RC   TISSUE=Plasma;
RX   PubMed=1772402; DOI=10.1007/bf02399689;
RA   Patterson S.D., Bell K., Shaw D.C.;
RT   "The equine major plasma serpin multigene family: partial characterization
RT   including sequence of the reactive-site regions.";
RL   Biochem. Genet. 29:477-499(1991).
RN   [3]
RP   STRUCTURE OF CARBOHYDRATES.
RX   PubMed=2111994;
RA   Patterson S.D., Bell K.;
RT   "The carbohydrate side chains of the major plasma serpins of horse and
RT   wallaby: analyses of enzymatic and chemically treated (including 'Smith
RT   degradation') protein blots by lectin binding.";
RL   Biochem. Int. 20:429-436(1990).
CC   -!- FUNCTION: Inhibitor of serine proteases. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC       protein and directs binding to the target protease. The protease
CC       cleaves the serpin at the reactive site within the RCL, establishing a
CC       covalent linkage between the serpin reactive site and the active site
CC       of the protease. The resulting inactive serpin-protease complex is
CC       highly stable (By similarity). {ECO:0000250}.
CC   -!- PTM: N-glycosylated with carbohydrates having biantennary side chains.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; AF034077; AAC83412.1; -; Genomic_DNA.
DR   PIR; B61219; B61219.
DR   RefSeq; NP_001108005.1; NM_001114533.1.
DR   AlphaFoldDB; P38029; -.
DR   SMR; P38029; -.
DR   STRING; 9796.ENSECAP00000053574; -.
DR   MEROPS; I04.001; -.
DR   PaxDb; P38029; -.
DR   PRIDE; P38029; -.
DR   GeneID; 100065158; -.
DR   KEGG; ecb:100065158; -.
DR   CTD; 103910445; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
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   Acute phase; Direct protein sequencing; Glycoprotein; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:1772402"
FT   CHAIN           25..421
FT                   /note="Alpha-1-antiproteinase 2"
FT                   /id="PRO_0000032385"
FT   REGION          376..395
FT                   /note="RCL"
FT   SITE            385..386
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        36..40
FT                   /note="HATAH -> DADKD (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="V -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  46942 MW;  D79B101312AC8259 CRC64;
     MPSSVPWCLL LLAGLCCLVP SSLAEDLQGC AVQETHATAH DEEHLQEPAE HKIAPNLADF
     AFSLYRHVAH QSNTTNIFFS PVSIATAFAL LSLGAKGDTH TQILEGLSFN LTELAEAQIH
     DGFQHLLNAL NHSDNQLQLT TGNGLFIDES AKLLDKFLED VKKLYHSEAF SINFRDTEEA
     KKQINDYVEK GTQGKIVDLV KDLDKDTVLA LVNYIFFKGT WEKPFEPEYT TEQDFHVDEK
     TTVRVPMMHR LSSFDVQYSD TLSSWVLLLD YAGNATAFFI LPDQGKLQHL EDTLTKGILA
     RFLGNRHSSF VNVHLPKLSI SGTYDLTSIL PELGITKVFS RQADLSGITE EVPLTVSKAL
     HKAVLTIDEK GTEAAGTTMW EIMPISLPPD LKFNRPFVLI IYDRNTKSPL FVGKVVDPTQ
     K