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P09006

- SPA3N_RAT

UniProt

P09006 - SPA3N_RAT

Protein

Serine protease inhibitor A3N

Gene

Serpina3n

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei381 – 3822Reactive bondSequence Analysis

    GO - Molecular functioni

    1. serine-type endopeptidase inhibitor activity Source: RefGenome

    GO - Biological processi

    1. cellular response to cAMP Source: RGD
    2. cellular response to glucocorticoid stimulus Source: RGD
    3. cellular response to interferon-gamma Source: RGD
    4. cellular response to interleukin-1 Source: RGD
    5. cellular response to interleukin-6 Source: RGD
    6. inflammatory response Source: RGD
    7. negative regulation of endopeptidase activity Source: RefGenome
    8. regulation of proteolysis Source: RefGenome
    9. response to lipopolysaccharide Source: RGD
    10. response to peptide hormone Source: Ensembl
    11. response to vitamin B6 Source: RGD

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine protease inhibitor A3N
    Short name:
    Serpin A3N
    Alternative name(s):
    CPI-26
    Contrapsin-like protease inhibitor 6
    SPI-2.2
    Serine protease inhibitor 3
    Short name:
    SPI-3
    Gene namesi
    Name:Serpina3n
    Synonyms:Spin2c
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi3747. Serpina3n.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: RefGenome
    2. extracellular space Source: RGD

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929By similarityAdd
    BLAST
    Chaini30 – 418389Serine protease inhibitor A3NPRO_0000032423Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP09006.
    PRIDEiP09006.

    Expressioni

    Tissue specificityi

    Liver.1 Publication

    Inductioni

    By acute inflammation.1 Publication

    Gene expression databases

    GenevestigatoriP09006.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000014073.

    Structurei

    3D structure databases

    ProteinModelPortaliP09006.
    SMRiP09006. Positions 47-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni367 – 39428RCLAdd
    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 serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable By similarity. Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity.By similarity

    Sequence similaritiesi

    Belongs to the serpin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4826.
    GeneTreeiENSGT00740000115120.
    HOGENOMiHOG000238521.
    HOVERGENiHBG005957.
    InParanoidiP09006.
    KOiK04525.
    OMAiVKFVPMS.
    OrthoDBiEOG78M027.
    PhylomeDBiP09006.
    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.

    P09006-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRLVTLELL MAGIGSALLC FPDCILGEDT LFHEDQDKGT QLDSLTLASI    50
    NTDFAFSLYK KLALRNPDKN VVFSPLSISA ALAVVSLGAK GNSMEEILEG 100
    LKFNLTETPE TEIHRGFGHL LQRLSQPRDE IQISTGNALF IEKRLQVLAE 150
    FQEKAKALYQ AEAFTADFQQ SREAKKLIND YVSKQTQGKI QGLITNLAKK 200
    TSMVLVNYIY FKGKWKVPFD PRDTFQSEFY SGKRRPVKVP MMKLEDLTTP 250
    YVRDEELNCT VVELKYTGNA SALFILPDQG KMQQVEASLQ PETLRRWKDS 300
    LRPSMIDELY LPKFSISADY NLEDVLPELG IKEVFSTQAD LSGITGDKDL 350
    MVSQVVHKAV LDVAETGTEA AAATGVKFVP MSAKLDPLII AFDRPFLMII 400
    SDTETAIAPF LAKIFNPK 418
    Length:418
    Mass (Da):46,652
    Last modified:November 1, 1997 - v3
    Checksum:iAADEFF087190B44F
    GO

    Sequence cautioni

    The sequence CAA34408.1 differs from that shown. Reason: Frameshift at position 7.
    The sequence AAH78796.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA34408.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121A → D in CAA34408. (PubMed:15489334)Curated
    Sequence conflicti20 – 201C → S in CAA34408. (PubMed:15489334)Curated
    Sequence conflicti68 – 681D → H in CAA34408. (PubMed:15489334)Curated
    Sequence conflicti92 – 921N → S in CAA34408. (PubMed:15489334)Curated
    Sequence conflicti236 – 2361P → S in CAA34408. (PubMed:15489334)Curated
    Sequence conflicti323 – 3231E → EE in CAA31548. (PubMed:3493437)Curated
    Sequence conflicti334 – 3341V → A in CAA31548. (PubMed:3493437)Curated
    Sequence conflicti353 – 3531S → F in CAA34408. (PubMed:15489334)Curated
    Sequence conflicti354 – 3541Q → E in CAA31548. (PubMed:3493437)Curated
    Sequence conflicti381 – 3811M → V in CAA31548. (PubMed:3493437)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16359 mRNA. Translation: CAA34408.1. Sequence problems.
    D00753 mRNA. Translation: BAA00650.1.
    BC078796 mRNA. Translation: AAH78796.2. Different initiation.
    X13150 mRNA. Translation: CAA31548.1.
    PIRiB26423.
    RefSeqiNP_113719.1. NM_031531.1.
    UniGeneiRn.202939.

    Genome annotation databases

    EnsembliENSRNOT00000014073; ENSRNOP00000014073; ENSRNOG00000010527.
    GeneIDi24795.
    KEGGirno:24795.
    UCSCiRGD:3747. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16359 mRNA. Translation: CAA34408.1 . Sequence problems.
    D00753 mRNA. Translation: BAA00650.1 .
    BC078796 mRNA. Translation: AAH78796.2 . Different initiation.
    X13150 mRNA. Translation: CAA31548.1 .
    PIRi B26423.
    RefSeqi NP_113719.1. NM_031531.1.
    UniGenei Rn.202939.

    3D structure databases

    ProteinModelPortali P09006.
    SMRi P09006. Positions 47-418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000014073.

    Proteomic databases

    PaxDbi P09006.
    PRIDEi P09006.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000014073 ; ENSRNOP00000014073 ; ENSRNOG00000010527 .
    GeneIDi 24795.
    KEGGi rno:24795.
    UCSCi RGD:3747. rat.

    Organism-specific databases

    CTDi 20716.
    RGDi 3747. Serpina3n.

    Phylogenomic databases

    eggNOGi COG4826.
    GeneTreei ENSGT00740000115120.
    HOGENOMi HOG000238521.
    HOVERGENi HBG005957.
    InParanoidi P09006.
    KOi K04525.
    OMAi VKFVPMS.
    OrthoDBi EOG78M027.
    PhylomeDBi P09006.
    TreeFami TF343201.

    Miscellaneous databases

    NextBioi 604438.
    PROi P09006.

    Gene expression databases

    Genevestigatori P09006.

    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 characterization of three rat liver serine-protease inhibitors affected by inflammation and hypophysectomy. Protein and mRNA analysis and cDNA cloning."
      Pages G., Rouayrenc J.F., le Cam G., Mariller M., le Cam A.
      Eur. J. Biochem. 190:385-391(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, GLYCOSYLATION.
      Tissue: Liver.
    2. "Molecular cloning and characterization of rat contrapsin-like protease inhibitor and related proteins."
      Ohkubo K., Ogata S., Misumi Y., Takami N., Ikehara Y.
      J. Biochem. 109:243-250(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "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: Kidney.
    4. "Accelerated evolution in the reactive centre regions of serine protease inhibitors."
      Hill R.E., Hastie N.D.
      Nature 326:96-99(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 203-408.
    5. "Expression patterns of murine antichymotrypsin-like genes reflect evolutionary divergence at the Serpina3 locus."
      Horvath A.J., Forsyth S.L., Coughlin P.B.
      J. Mol. Evol. 59:488-497(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGION RCL.

    Entry informationi

    Entry nameiSPA3N_RAT
    AccessioniPrimary (citable) accession number: P09006
    Secondary accession number(s): Q03312
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 112 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The single human alpha1-antichymotrypsin gene (SERPINA3) is represented by a cluster of 6 individual rat paralogs.

    Caution

    It is uncertain whether Met-1 or Met-11 is the initiator.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3