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Protein

Alpha-1-antiproteinase

Gene

Serpina1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibitor of serine proteases. The primary target is elastase, but also has a moderate affinity for plasmin and thrombin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei376 – 3772Reactive bond

GO - Molecular functioni

  • endopeptidase inhibitor activity Source: RGD
  • serine-type endopeptidase inhibitor activity Source: RGD

GO - Biological processi

  • acute-phase response Source: UniProtKB-KW
  • inflammatory response Source: RGD
  • negative regulation of serine-type endopeptidase activity Source: RGD
  • response to chromate Source: RGD
  • response to cytokine Source: RGD
  • response to estradiol Source: RGD
  • response to hypoxia Source: RGD
  • response to inorganic substance Source: RGD
  • response to lead ion Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to methanol Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to triglyceride Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Acute phase

Protein family/group databases

MEROPSiI04.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1-antiproteinase
Alternative name(s):
Alpha-1-antitrypsin
Alpha-1-proteinase inhibitor
Serpin A1
Gene namesi
Name:Serpina1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3326. Serpina1.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 411387Alpha-1-antiproteinasePRO_0000032398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence Analysis
Modified residuei377 – 3771PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP17475.
PRIDEiP17475.

PTM databases

PhosphoSiteiP17475.

Expressioni

Tissue specificityi

Plasma.1 Publication

Gene expression databases

GenevisibleiP17475. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012577.

Structurei

3D structure databases

ProteinModelPortaliP17475.
SMRiP17475. Positions 39-411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 38620RCLAdd
BLAST

Domaini

The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity).By similarity

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP17475.
KOiK03984.
OrthoDBiEOG7QC7W9.
PhylomeDBiP17475.
TreeFamiTF343201.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17475-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSISRGLL LLAALCCLAP SFLAEDAQET DTSQQDQSPT YRKISSNLAD
60 70 80 90 100
FAFSLYRELV HQSNTSNIFF SPMSITTAFA MLSLGSKGDT RKQILEGLEF
110 120 130 140 150
NLTQIPEADI HKAFHHLLQT LNRPDSELQL NTGNGLFVNK NLKLVEKFLE
160 170 180 190 200
EVKNNYHSEA FSVNFADSEE AKKVINDYVE KGTQGKIVDL MKQLDEDTVF
210 220 230 240 250
ALVNYIFFKG KWKRPFNPEH TRDADFHVDK STTVKVPMMN RLGMFDMHYC
260 270 280 290 300
STLSSWVLMM DYLGNATAIF LLPDDGKMQH LEQTLTKDLI SRFLLNRQTR
310 320 330 340 350
SAILYFPKLS ISGTYNLKTL LSSLGITRVF NNDADLSGIT EDAPLKLSQA
360 370 380 390 400
VHKAVLTLDE RGTEAAGATV VEAVPMSLPP QVKFDHPFIF MIVESETQSP
410
LFVGKVIDPT R
Length:411
Mass (Da):46,136
Last modified:February 1, 1991 - v2
Checksum:iB4245CFE21C5C761
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141A → G in BAA00579 (PubMed:2229024).Curated
Sequence conflicti14 – 141A → G in AAH78824 (PubMed:15489334).Curated
Sequence conflicti84 – 841L → V in BAA00579 (PubMed:2229024).Curated
Sequence conflicti247 – 2471M → I in CAA34349 (Ref. 5) Curated
Sequence conflicti248 – 2481H → Y in BAA00579 (PubMed:2229024).Curated
Sequence conflicti318 – 3181K → N in BAA00579 (PubMed:2229024).Curated
Sequence conflicti322 – 3221S → D in CAA34349 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00675 mRNA. Translation: BAA00579.1.
BC078824 mRNA. Translation: AAH78824.1.
M32247 mRNA. Translation: AAA40788.1.
X16273 mRNA. Translation: CAA34349.1.
PIRiA33892. ITRT.
RefSeqiNP_071964.2. NM_022519.2.
XP_006240518.1. XM_006240456.1.
UniGeneiRn.1419.

Genome annotation databases

GeneIDi24648.
KEGGirno:24648.
UCSCiRGD:3326. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00675 mRNA. Translation: BAA00579.1.
BC078824 mRNA. Translation: AAH78824.1.
M32247 mRNA. Translation: AAA40788.1.
X16273 mRNA. Translation: CAA34349.1.
PIRiA33892. ITRT.
RefSeqiNP_071964.2. NM_022519.2.
XP_006240518.1. XM_006240456.1.
UniGeneiRn.1419.

3D structure databases

ProteinModelPortaliP17475.
SMRiP17475. Positions 39-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012577.

Protein family/group databases

MEROPSiI04.001.

PTM databases

PhosphoSiteiP17475.

Proteomic databases

PaxDbiP17475.
PRIDEiP17475.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24648.
KEGGirno:24648.
UCSCiRGD:3326. rat.

Organism-specific databases

CTDi5265.
RGDi3326. Serpina1.

Phylogenomic databases

eggNOGiCOG4826.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP17475.
KOiK03984.
OrthoDBiEOG7QC7W9.
PhylomeDBiP17475.
TreeFamiTF343201.

Miscellaneous databases

NextBioi603964.
PROiP17475.

Gene expression databases

GenevisibleiP17475. RN.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequencing of the cDNA of rat alpha 1-protease inhibitor and its expression in COS-1 cells."
    Misumi Y., Sohda M., Ohkubo K., Takami N., Oda K., Ikehara Y.
    J. Biochem. 108:230-234(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "Molecular cloning and primary structure of rat alpha 1-antitrypsin."
    Chao S., Chai K.X., Chao L., Chao J.
    Biochemistry 29:323-329(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-411, PROTEIN SEQUENCE OF 25-57, TISSUE SPECIFICITY.
    Tissue: Liver.
  4. Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 44-57; 148-172; 174-181; 187-192; 278-287 AND 301-328, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  5. Flink I.L., Bailey T., Morkin E.
    Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-389.
    Tissue: Liver.

Entry informationi

Entry nameiA1AT_RAT
AccessioniPrimary (citable) accession number: P17475
Secondary accession number(s): Q6AYZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1991
Last modified: July 22, 2015
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.