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P17475

- A1AT_RAT

UniProt

P17475 - A1AT_RAT

Protein

Alpha-1-antiproteinase

Gene

Serpina1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
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    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

    1. endopeptidase inhibitor activity Source: RGD
    2. protein binding Source: RGD
    3. serine-type endopeptidase inhibitor activity Source: RGD

    GO - Biological processi

    1. acute-phase response Source: UniProtKB-KW
    2. inflammatory response Source: RGD
    3. negative regulation of endopeptidase activity Source: RefGenome
    4. negative regulation of serine-type endopeptidase activity Source: RGD
    5. regulation of proteolysis Source: RefGenome
    6. response to chromate Source: RGD
    7. response to cytokine Source: RGD
    8. response to estradiol Source: RGD
    9. response to hypoxia Source: RGD
    10. response to inorganic substance Source: RGD
    11. response to lead ion Source: RGD
    12. response to lipopolysaccharide Source: RGD
    13. response to methanol Source: RGD
    14. response to organic cyclic compound Source: RGD
    15. response to triglyceride Source: RGD

    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: Chromosome 6

    Organism-specific databases

    RGDi3326. Serpina1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: Ensembl
    2. extracellular space Source: RGD

    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

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP17475.
    PRIDEiP17475.

    PTM databases

    PhosphoSiteiP17475.

    Expressioni

    Tissue specificityi

    Plasma.1 Publication

    Gene expression databases

    GenevestigatoriP17475.

    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.
    GeneTreeiENSGT00750000117448.
    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

    MAPSISRGLL LLAALCCLAP SFLAEDAQET DTSQQDQSPT YRKISSNLAD    50
    FAFSLYRELV HQSNTSNIFF SPMSITTAFA MLSLGSKGDT RKQILEGLEF 100
    NLTQIPEADI HKAFHHLLQT LNRPDSELQL NTGNGLFVNK NLKLVEKFLE 150
    EVKNNYHSEA FSVNFADSEE AKKVINDYVE KGTQGKIVDL MKQLDEDTVF 200
    ALVNYIFFKG KWKRPFNPEH TRDADFHVDK STTVKVPMMN RLGMFDMHYC 250
    STLSSWVLMM DYLGNATAIF LLPDDGKMQH LEQTLTKDLI SRFLLNRQTR 300
    SAILYFPKLS ISGTYNLKTL LSSLGITRVF NNDADLSGIT EDAPLKLSQA 350
    VHKAVLTLDE RGTEAAGATV VEAVPMSLPP QVKFDHPFIF MIVESETQSP 400
    LFVGKVIDPT R 411
    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. 1 PublicationCurated
    Sequence conflicti248 – 2481H → Y in BAA00579. (PubMed:2229024)Curated
    Sequence conflicti318 – 3181K → N in BAA00579. (PubMed:2229024)Curated
    Sequence conflicti322 – 3221S → D in CAA34349. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    XP_006240519.1. XM_006240457.1.
    UniGeneiRn.1419.

    Genome annotation databases

    EnsembliENSRNOT00000012577; ENSRNOP00000012577; ENSRNOG00000032669.
    GeneIDi24648.
    KEGGirno:24648.
    UCSCiRGD:3326. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00675 mRNA. Translation: BAA00579.1 .
    BC078824 mRNA. Translation: AAH78824.1 .
    M32247 mRNA. Translation: AAA40788.1 .
    X16273 mRNA. Translation: CAA34349.1 .
    PIRi A33892. ITRT.
    RefSeqi NP_071964.2. NM_022519.2.
    XP_006240518.1. XM_006240456.1.
    XP_006240519.1. XM_006240457.1.
    UniGenei Rn.1419.

    3D structure databases

    ProteinModelPortali P17475.
    SMRi P17475. Positions 39-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000012577.

    Protein family/group databases

    MEROPSi I04.001.

    PTM databases

    PhosphoSitei P17475.

    Proteomic databases

    PaxDbi P17475.
    PRIDEi P17475.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000012577 ; ENSRNOP00000012577 ; ENSRNOG00000032669 .
    GeneIDi 24648.
    KEGGi rno:24648.
    UCSCi RGD:3326. rat.

    Organism-specific databases

    CTDi 5265.
    RGDi 3326. Serpina1.

    Phylogenomic databases

    eggNOGi COG4826.
    GeneTreei ENSGT00750000117448.
    HOGENOMi HOG000238521.
    HOVERGENi HBG005957.
    InParanoidi P17475.
    KOi K03984.
    OrthoDBi EOG7QC7W9.
    PhylomeDBi P17475.
    TreeFami TF343201.

    Miscellaneous databases

    NextBioi 603964.

    Gene expression databases

    Genevestigatori P17475.

    Family and domain databases

    InterProi IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view ]
    PANTHERi PTHR11461. PTHR11461. 1 hit.
    Pfami PF00079. Serpin. 1 hit.
    [Graphical view ]
    SMARTi SM00093. SERPIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56574. SSF56574. 1 hit.
    PROSITEi PS00284. SERPIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 118 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