A1AT_PONAB
ID A1AT_PONAB Reviewed; 418 AA.
AC Q5RCW5; Q5NVR9; Q5RF76;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Alpha-1-antitrypsin;
DE AltName: Full=Alpha-1 protease inhibitor;
DE AltName: Full=Alpha-1-antiproteinase;
DE AltName: Full=Serpin A1;
DE Flags: Precursor;
GN Name=SERPINA1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, Kidney, and Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is
CC elastase, but it also has a moderate affinity for plasmin and thrombin.
CC Inhibits trypsin, chymotrypsin and plasminogen activator (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CELA2A (By similarity). Interacts with ERGIC3
CC and LMAN1/ERGIC53 (By similarity). Interacts with PRSS1/Trypsin (By
CC similarity). {ECO:0000250|UniProtKB:P01009}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 carboxyl group of the serpin reactive site
CC and the serine hydroxyl of the protease. The resulting inactive serpin-
CC protease complex is highly stable (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; CR857285; CAH89581.1; -; mRNA.
DR EMBL; CR858153; CAH90392.1; -; mRNA.
DR EMBL; CR925936; CAI29594.1; -; mRNA.
DR RefSeq; NP_001124697.1; NM_001131225.2.
DR RefSeq; NP_001128914.1; NM_001135442.1.
DR RefSeq; XP_009247699.1; XM_009249424.1.
DR RefSeq; XP_009247700.1; XM_009249425.1.
DR RefSeq; XP_009247701.1; XM_009249426.1.
DR RefSeq; XP_009247702.1; XM_009249427.1.
DR RefSeq; XP_009247703.1; XM_009249428.1.
DR RefSeq; XP_009247704.1; XM_009249429.1.
DR RefSeq; XP_009247705.1; XM_009249430.1.
DR RefSeq; XP_009247706.1; XM_009249431.1.
DR RefSeq; XP_009247707.1; XM_009249432.1.
DR RefSeq; XP_009247708.1; XM_009249433.1.
DR AlphaFoldDB; Q5RCW5; -.
DR SMR; Q5RCW5; -.
DR STRING; 9601.ENSPPYP00000006940; -.
DR MEROPS; I04.001; -.
DR PRIDE; Q5RCW5; -.
DR Ensembl; ENSPPYT00000007214; ENSPPYP00000006940; ENSPPYG00000006103.
DR GeneID; 100171544; -.
DR GeneID; 100189861; -.
DR KEGG; pon:100171544; -.
DR CTD; 5265; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154493; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; Q5RCW5; -.
DR OMA; MEAIPMS; -.
DR OrthoDB; 1124079at2759; -.
DR TreeFam; TF343201; -.
DR Proteomes; UP000001595; Chromosome 14.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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 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 2: Evidence at transcript level;
KW Acute phase; Glycoprotein; Phosphoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..418
FT /note="Alpha-1-antitrypsin"
FT /id="PRO_0000032379"
FT REGION 373..392
FT /note="RCL"
FT SITE 382..383
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01009"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01009"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 289
FT /note="N -> D (in Ref. 1; CAH89581)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="R -> RS (in Ref. 1; CAH89581/CAI29594)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="I -> T (in Ref. 1; CAH89581)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..404
FT /note="FLMIEQNTK -> CLISVFQNA (in Ref. 1; CAI29594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46861 MW; BF93D2080AEDBE56 CRC64;
MPSSVSWGIL LLAGLCCLVP VSLAEDPQGD AAQKTDTSHH DQDHPTFNKI TPNLAEFAFS
LYRQLAHQSN STNIFFSPVS IATAFAMLSL GTKADTHSEI LEGLHFNLTE IPEAQVHEGF
QELLRTLNQP DSQLQLTTGN GLFLNESLKL VDKFLEDVKK LYHSDAFTVN FGDTEEAKKQ
INDYVEKGTQ GKIVDLVKEL DRDTVFALVN YIFFKGKWER PFEVKDTKEE DFHVDEVTTV
KVPMMRRLGM FNIHYCEKLS SWVLLMKYLG NATAIFFLPD EGKLQHLENE LTHDIITKFL
ENENRRSASL HLPKLSITGT YDLKRVLGQL GITKVFSNGA DLSGVTEEAP LKLSKAVHKA
VLTIDEKGTE AAGAMFLEAI PMSIPPEVKF NKPFVFLMIE QNTKSPLFVG KVVNPTQK
