ID   A1AT_NOTEU              Reviewed;          46 AA.
AC   P38027;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   23-FEB-2022, entry version 68.
DE   RecName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   Flags: Fragments;
OS   Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX   NCBI_TaxID=9315;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Plasma;
RX   PubMed=1676950; DOI=10.1016/0742-8413(91)90217-h;
RA   Patterson S.D., Bell K., Shaw D.C.;
RT   "The tammar wallaby major plasma serpin: partial characterization including
RT   the sequence of the reactive site region.";
RL   Comp. Biochem. Physiol. 98C:359-367(1991).
RN   [2]
RP   GLYCOSYLATION.
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   -!- 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; contains bi- and triantennary glycans with a
CC       bisecting N-acetylglucosamine and fucose residue.
CC       {ECO:0000269|PubMed:2111994}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   MEROPS; I04.974; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Acute phase; Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW   Protease inhibitor; Secreted; Serine protease inhibitor.
FT   CHAIN           1..>46
FT                   /note="Alpha-1-antiproteinase"
FT                   /id="PRO_0000094095"
FT   SITE            29..30
FT                   /note="Reactive bond"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   NON_CONS        24..25
FT                   /evidence="ECO:0000305"
FT   NON_TER         46
SQ   SEQUENCE   46 AA;  5197 MW;  715339FDF4C64E9E CRC64;
     EELPDSKDRA XPLSASKXIS PYMKEAIPMS IPPVIDFNKP FLIIXY