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P05545

- SPA3K_RAT

UniProt

P05545 - SPA3K_RAT

Protein

Serine protease inhibitor A3K

Gene

Serpina3k

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Binds to and inhibits kallikreins. Inhibits trypsin but not chymotrypsin or elastase.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei379 – 3802Reactive bondBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. negative regulation of angiogenesis Source: RGD
    2. negative regulation of endothelial cell proliferation Source: RGD
    3. positive regulation of apoptotic process Source: RGD

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Protein family/group databases

    MEROPSiI04.051.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine protease inhibitor A3K
    Short name:
    Serpin A3K
    Alternative name(s):
    CPI-21
    Contrapsin-like protease inhibitor 1
    GHR-P63
    Growth hormone-regulated proteinase inhibitor
    Kallikrein-binding protein
    Short name:
    KBP
    SPI-2.3
    Serine protease inhibitor 2
    Short name:
    SPI-2
    Thyroid hormone-regulated protein
    Gene namesi
    Name:Serpina3k
    Synonyms:Spin2b
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi3746. Serpina3k.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular space Source: InterPro

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Chaini21 – 416396Serine protease inhibitor A3KPRO_0000032421Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP05545.
    PRIDEiP05545.

    PTM databases

    PhosphoSiteiP05545.

    Expressioni

    Tissue specificityi

    Liver and plasma.3 Publications

    Inductioni

    By growth hormone, thyroid hormone and sex hormones. Its expression is reduced by inflammation. In male rats, its level is several fold higher than in female rats. Reduced during acute inflammation.4 Publications

    Gene expression databases

    GenevestigatoriP05545.

    Interactioni

    Protein-protein interaction databases

    IntActiP05545. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP05545.
    SMRiP05545. Positions 45-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni365 – 39228RCLAdd
    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 similarity1 Publication

    Sequence similaritiesi

    Belongs to the serpin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4826.
    GeneTreeiENSGT00740000115120.
    HOGENOMiHOG000238521.
    HOVERGENiHBG005957.
    InParanoidiP05545.
    KOiK04525.
    OrthoDBiEOG78M027.
    PhylomeDBiP05545.
    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.

    P05545-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFIAALGLL MAGICPAVLC DGILGRDTLP HEDQGKGRQL HSLTLASINT    50
    DFTLSLYKKL ALRNPDKNVV FSPLSISAAL AILSLGAKDS TMEEILEVLK 100
    FNLTEITEEE IHQGFGHLLQ RLSQPEDQAE INTGSALFID KEQPILSEFQ 150
    EKTRALYQAE AFVADFKQCN EAKKFINDYV SNQTQGKIAE LFSELDERTS 200
    MVLVNYLLFK GKWKVPFNPN DTFESEFYLD EKRSVKVPMM KIKDLTTPYI 250
    RDEELSCSVL ELKYTGNASA LFILPDQGKM QQVESSLQPE TLKKWKDSLR 300
    PRIISELRMP KFSISTDYNL EEVLPELGIR KIFSQQADLS RITGTKNLHV 350
    SQVVHKAVLD VDETGTEGAA ATAVTAALKS LPQTIPLLNF NRPFMLVITD 400
    NNGQSVFFMG KVTNPM 416
    Length:416
    Mass (Da):46,562
    Last modified:April 1, 1993 - v3
    Checksum:i6072BAE56BFF91B1
    GO

    Sequence cautioni

    The sequence AAH62236.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA34407.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA34409.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301P → S AA sequence (PubMed:2398056)Curated
    Sequence conflicti47 – 471S → A AA sequence (PubMed:2398056)Curated
    Sequence conflicti98 – 981V → G in AAA42173. (PubMed:3494016)Curated
    Sequence conflicti98 – 981V → G in BAA00648. (PubMed:1864837)Curated
    Sequence conflicti98 – 981V → G in AAH62236. (PubMed:15489334)Curated
    Sequence conflicti112 – 1121H → HH in CAA34407. (PubMed:1694763)Curated
    Sequence conflicti194 – 1941E → D in BAA00648. (PubMed:1864837)Curated
    Sequence conflicti250 – 2501I → V in BAA00648. (PubMed:1864837)Curated
    Sequence conflicti326 – 3261E → D in CAA34409. (PubMed:2258058)Curated
    Sequence conflicti385 – 3851I → V in BAA00648. (PubMed:1864837)Curated
    Sequence conflicti387 – 3871L → P in CAA34407. (PubMed:1694763)Curated
    Sequence conflicti401 – 4011N → D in AAH62236. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti326 – 3261E → D.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05348 mRNA. Translation: CAA28958.1.
    M15916 mRNA. Translation: AAA42173.1.
    X16358 mRNA. Translation: CAA34407.1. Different initiation.
    X16362 Genomic DNA. Translation: CAA34409.1. Different initiation.
    D00751 mRNA. Translation: BAA00648.1.
    M67496 Genomic DNA. No translation available.
    BC062236 mRNA. Translation: AAH62236.2. Different initiation.
    PIRiA29035.
    B29131.
    RefSeqiNP_036789.2. NM_012657.2.
    XP_006240520.1. XM_006240458.1.
    UniGeneiRn.91257.
    Rn.97597.

    Genome annotation databases

    EnsembliENSRNOT00000013896; ENSRNOP00000013896; ENSRNOG00000010410.
    GeneIDi24794.
    KEGGirno:24794.
    UCSCiRGD:3746. rat.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05348 mRNA. Translation: CAA28958.1 .
    M15916 mRNA. Translation: AAA42173.1 .
    X16358 mRNA. Translation: CAA34407.1 . Different initiation.
    X16362 Genomic DNA. Translation: CAA34409.1 . Different initiation.
    D00751 mRNA. Translation: BAA00648.1 .
    M67496 Genomic DNA. No translation available.
    BC062236 mRNA. Translation: AAH62236.2 . Different initiation.
    PIRi A29035.
    B29131.
    RefSeqi NP_036789.2. NM_012657.2.
    XP_006240520.1. XM_006240458.1.
    UniGenei Rn.91257.
    Rn.97597.

    3D structure databases

    ProteinModelPortali P05545.
    SMRi P05545. Positions 45-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P05545. 1 interaction.

    Protein family/group databases

    MEROPSi I04.051.

    PTM databases

    PhosphoSitei P05545.

    Proteomic databases

    PaxDbi P05545.
    PRIDEi P05545.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000013896 ; ENSRNOP00000013896 ; ENSRNOG00000010410 .
    GeneIDi 24794.
    KEGGi rno:24794.
    UCSCi RGD:3746. rat.

    Organism-specific databases

    CTDi 16625.
    RGDi 3746. Serpina3k.

    Phylogenomic databases

    eggNOGi COG4826.
    GeneTreei ENSGT00740000115120.
    HOGENOMi HOG000238521.
    HOVERGENi HBG005957.
    InParanoidi P05545.
    KOi K04525.
    OrthoDBi EOG78M027.
    PhylomeDBi P05545.
    TreeFami TF343201.

    Miscellaneous databases

    NextBioi 604434.

    Gene expression databases

    Genevestigatori P05545.

    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. "Study of a growth hormone-regulated protein secreted by rat hepatocytes: cDNA cloning, anti-protease activity and regulation of its synthesis by various hormones."
      le Cam A., Pages G., Auberger P., le Cam G., Leopold P., Benarous R., Glaichenhaus N.
      EMBO J. 6:1225-1232(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, GLYCOSYLATION.
    2. le Cam A.
      Submitted (OCT-1987) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Growth hormone induces two mRNA species of the serine protease inhibitor gene family in rat liver."
      Yoon J.-B., Towle H.C., Seelig S.
      J. Biol. Chem. 262:4284-4289(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
      Tissue: Liver.
    4. "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.
    5. "Primary structure and assignment to chromosome 6 of three related rat genes encoding liver serine protease inhibitors."
      Pages G., Rouayrenc J.F., Rossi V., Le Cam G., Mariller M., Szpirer J., Szpirer C., Levan G., Le Cam A.
      Gene 94:273-282(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASP-326.
    6. "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], PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY.
      Tissue: Liver.
    7. "Molecular cloning and analysis of the rat kallikrein-binding protein gene."
      Chai K.X., Ma J.-X., Murray S.R., Chao J., Chao L.
      J. Biol. Chem. 266:16029-16036(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Sprague-Dawley.
      Tissue: Liver.
    8. "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: Pituitary.
    9. "Tissue kallikrein-binding protein is a serpin. I. Purification, characterization, and distribution in normotensive and spontaneously hypertensive rats."
      Chao J., Chai K.X., Chen L.-M., Xiong W., Chao S., Woodley-Miller C., Wang L., Lu H.S., Chao L.
      J. Biol. Chem. 265:16394-16401(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-49, PROTEIN SEQUENCE OF 21-49, CHARACTERIZATION, TISSUE SPECIFICITY, INDUCTION.
    10. Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
      Submitted (SEP-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 155-167; 188-210 AND 312-330, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Spinal cord.
    11. "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: DOMAIN RCL.

    Entry informationi

    Entry nameiSPA3K_RAT
    AccessioniPrimary (citable) accession number: P05545
    Secondary accession number(s): P14281, Q64254, Q6P6G8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 116 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.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3