A1AT_RAT
ID A1AT_RAT Reviewed; 411 AA.
AC P17475; Q6AYZ5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Alpha-1-antiproteinase;
DE AltName: Full=Alpha-1-antitrypsin;
DE AltName: Full=Alpha-1-proteinase inhibitor;
DE AltName: Full=Serpin A1;
DE Flags: Precursor;
GN Name=Serpina1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=2229024; DOI=10.1093/oxfordjournals.jbchem.a123185;
RA Misumi Y., Sohda M., Ohkubo K., Takami N., Oda K., Ikehara Y.;
RT "Molecular cloning and sequencing of the cDNA of rat alpha 1-protease
RT inhibitor and its expression in COS-1 cells.";
RL J. Biochem. 108:230-234(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-411, PROTEIN SEQUENCE OF 25-57, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=2302382; DOI=10.1021/bi00454a004;
RA Chao S., Chai K.X., Chao L., Chao J.;
RT "Molecular cloning and primary structure of rat alpha 1-antitrypsin.";
RL Biochemistry 29:323-329(1990).
RN [4]
RP PROTEIN SEQUENCE OF 44-57; 148-172; 174-181; 187-192; 278-287 AND 301-328,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 188-389.
RC TISSUE=Liver;
RA Flink I.L., Bailey T., Morkin E.;
RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibitor of serine proteases. The primary target is
CC elastase, but also has a moderate affinity for plasmin and thrombin.
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.
CC -!- TISSUE SPECIFICITY: Plasma. {ECO:0000269|PubMed:2302382}.
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; D00675; BAA00579.1; -; mRNA.
DR EMBL; BC078824; AAH78824.1; -; mRNA.
DR EMBL; M32247; AAA40788.1; -; mRNA.
DR EMBL; X16273; CAA34349.1; -; mRNA.
DR PIR; A33892; ITRT.
DR RefSeq; NP_071964.2; NM_022519.2.
DR RefSeq; XP_006240518.1; XM_006240456.1.
DR RefSeq; XP_017449521.1; XM_017594032.1.
DR AlphaFoldDB; P17475; -.
DR SMR; P17475; -.
DR STRING; 10116.ENSRNOP00000012577; -.
DR MEROPS; I04.001; -.
DR GlyGen; P17475; 3 sites.
DR iPTMnet; P17475; -.
DR PhosphoSitePlus; P17475; -.
DR SwissPalm; P17475; -.
DR jPOST; P17475; -.
DR PaxDb; P17475; -.
DR PRIDE; P17475; -.
DR GeneID; 24648; -.
DR KEGG; rno:24648; -.
DR UCSC; RGD:3326; rat.
DR CTD; 5265; -.
DR RGD; 3326; Serpina1.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P17475; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P17475; -.
DR TreeFam; TF343201; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P17475; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:RGD.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:RGD.
DR GO; GO:0046687; P:response to chromate; IDA:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IDA:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0033986; P:response to methanol; IDA:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0034014; P:response to triglyceride; IEP:RGD.
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; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:2302382"
FT CHAIN 25..411
FT /note="Alpha-1-antiproteinase"
FT /id="PRO_0000032398"
FT REGION 367..386
FT /note="RCL"
FT SITE 376..377
FT /note="Reactive bond"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01009"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01009"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14
FT /note="A -> G (in Ref. 1; BAA00579 and 2; AAH78824)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="L -> V (in Ref. 1; BAA00579)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="M -> I (in Ref. 5; CAA34349)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="H -> Y (in Ref. 1; BAA00579)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="K -> N (in Ref. 1; BAA00579)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="S -> D (in Ref. 5; CAA34349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46136 MW; B4245CFE21C5C761 CRC64;
MAPSISRGLL LLAALCCLAP SFLAEDAQET DTSQQDQSPT YRKISSNLAD FAFSLYRELV
HQSNTSNIFF SPMSITTAFA MLSLGSKGDT RKQILEGLEF NLTQIPEADI HKAFHHLLQT
LNRPDSELQL NTGNGLFVNK NLKLVEKFLE EVKNNYHSEA FSVNFADSEE AKKVINDYVE
KGTQGKIVDL MKQLDEDTVF ALVNYIFFKG KWKRPFNPEH TRDADFHVDK STTVKVPMMN
RLGMFDMHYC STLSSWVLMM DYLGNATAIF LLPDDGKMQH LEQTLTKDLI SRFLLNRQTR
SAILYFPKLS ISGTYNLKTL LSSLGITRVF NNDADLSGIT EDAPLKLSQA VHKAVLTLDE
RGTEAAGATV VEAVPMSLPP QVKFDHPFIF MIVESETQSP LFVGKVIDPT R
