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P33587

- PROC_MOUSE

UniProt

P33587 - PROC_MOUSE

Protein

Vitamin K-dependent protein C

Gene

Proc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids.

    Catalytic activityi

    Degradation of blood coagulation factors Va and VIIIa.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei212 – 2132Cleavage; by thrombinBy similarity
    Active sitei253 – 2531Charge relay system
    Active sitei299 – 2991Charge relay system
    Active sitei401 – 4011Charge relay system

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. peptidase activity Source: MGI
    3. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. blood coagulation Source: UniProtKB-KW
    2. negative regulation of apoptotic process Source: UniProtKB
    3. negative regulation of blood coagulation Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_225233. Cell surface interactions at the vascular wall.

    Protein family/group databases

    MEROPSiS01.218.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vitamin K-dependent protein C (EC:3.4.21.69)
    Alternative name(s):
    Anticoagulant protein C
    Autoprothrombin IIA
    Blood coagulation factor XIV
    Cleaved into the following 3 chains:
    Gene namesi
    Name:Proc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:97771. Proc.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 4123By similarityPRO_0000028112Add
    BLAST
    Chaini42 – 460419Vitamin K-dependent protein CPRO_0000028113Add
    BLAST
    Chaini42 – 196155Vitamin K-dependent protein C light chainBy similarityPRO_0000028114Add
    BLAST
    Chaini199 – 460262Vitamin K-dependent protein C heavy chainBy similarityPRO_0000028115Add
    BLAST
    Peptidei199 – 21214Activation peptideBy similarityPRO_0000028116Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei48 – 4814-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei55 – 5514-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei57 – 5714-carboxyglutamatePROSITE-ProRule annotation
    Disulfide bondi58 ↔ 63By similarity
    Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei61 – 6114-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei67 – 6714-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei70 – 7014-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei76 – 7614-carboxyglutamatePROSITE-ProRule annotation
    Disulfide bondi91 ↔ 110By similarity
    Disulfide bondi100 ↔ 105By similarity
    Disulfide bondi104 ↔ 119By similarity
    Modified residuei112 – 1121(3R)-3-hydroxyaspartateBy similarity
    Disulfide bondi121 ↔ 130By similarity
    Disulfide bondi139 ↔ 150By similarity
    Disulfide bondi146 ↔ 159By similarity
    Disulfide bondi161 ↔ 174By similarity
    Disulfide bondi182 ↔ 319Interchain (between light and heavy chains)PROSITE-ProRule annotation
    Glycosylationi214 – 2141N-linked (GlcNAc...)1 Publication
    Disulfide bondi238 ↔ 254By similarity
    Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi372 ↔ 386By similarity
    Disulfide bondi397 ↔ 425By similarity

    Post-translational modificationi

    The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.
    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Zymogen

    Proteomic databases

    PaxDbiP33587.
    PRIDEiP33587.

    PTM databases

    PhosphoSiteiP33587.

    Expressioni

    Tissue specificityi

    Plasma; synthesized in the liver.

    Gene expression databases

    BgeeiP33587.
    CleanExiMM_PROC.
    GenevestigatoriP33587.

    Interactioni

    Subunit structurei

    Synthesized as a single chain precursor, which is cleaved into a light chain and a heavy chain held together by a disulfide bond. The enzyme is then activated by thrombin, which cleaves a tetradecapeptide from the amino end of the heavy chain; this reaction, which occurs at the surface of endothelial cells, is strongly promoted by thrombomodulin.

    Structurei

    3D structure databases

    ProteinModelPortaliP33587.
    SMRiP33587. Positions 46-87, 90-184, 212-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 8746GlaPROSITE-ProRule annotationAdd
    BLAST
    Domaini96 – 13136EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini135 – 17541EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini213 – 449237Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 2 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00750000117249.
    HOGENOMiHOG000251821.
    HOVERGENiHBG013304.
    InParanoidiP33587.
    KOiK01344.
    OMAiPNYSKST.
    OrthoDBiEOG75B84T.
    PhylomeDBiP33587.
    TreeFamiTF327329.

    Family and domain databases

    Gene3Di4.10.740.10. 1 hit.
    InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR000294. GLA_domain.
    IPR012224. Pept_S1A_FX.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00594. Gla. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001143. Factor_X. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    PR00001. GLABLOOD.
    SMARTiSM00181. EGF. 1 hit.
    SM00179. EGF_CA. 1 hit.
    SM00069. GLA. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF57630. SSF57630. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 1 hit.
    PS01187. EGF_CA. 1 hit.
    PS00011. GLA_1. 1 hit.
    PS50998. GLA_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P33587-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWQFRVFLLL MSTWGISSIP AHPDPVFSSS EHAHQVLRVR RANSFLEEMR    50
    PGSLERECME EICDFEEAQE IFQNVEDTLA FWIKYFDGDQ CSAPPLDHQC 100
    DSPCCGHGTC IDGIGSFSCS CDKGWEGKFC QQELRFQDCR VNNGGCLHYC 150
    LEESNGRRCA CAPGYELADD HMRCKSTVNF PCGKLGRWIE KKRKILKRDT 200
    DLEDELEPDP RIVNGTLTKQ GDSPWQAILL DSKKKLACGG VLIHTSWVLT 250
    AAHCVEGTKK LTVRLGEYDL RRRDHWELDL DIKEILVHPN YTRSSSDNDI 300
    ALLRLAQPAT LSKTIVPICL PNNGLAQELT QAGQETVVTG WGYQSDRIKD 350
    GRRNRTFILT FIRIPLVARN ECVEVMKNVV SENMLCAGII GDTRDACDGD 400
    SGGPMVVFFR GTWFLVGLVS WGEGCGHTNN YGIYTKVGSY LKWIHSYIGE 450
    KGVSLKSQKL 460
    Length:460
    Mass (Da):51,818
    Last modified:June 7, 2004 - v2
    Checksum:i0117F26E68FCC274
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651F → L in AAK07918. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti327 – 3271Q → QQ in strain: BALB/c.
    Natural varianti392 – 3921D → N in strain: BALB/c.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10445 mRNA. Translation: BAA01235.1.
    AF034569 Genomic DNA. Translation: AAC33795.1.
    AF318182 mRNA. Translation: AAK07918.1.
    BC013896 mRNA. Translation: AAH13896.1.
    D43755 Genomic DNA. Translation: BAA07812.1.
    CCDSiCCDS29116.1.
    PIRiJX0210.
    RefSeqiNP_001036232.1. NM_001042767.2.
    NP_001036233.2. NM_001042768.2.
    NP_032960.3. NM_008934.3.
    UniGeneiMm.2786.
    Mm.489734.

    Genome annotation databases

    EnsembliENSMUST00000171765; ENSMUSP00000132226; ENSMUSG00000024386.
    GeneIDi19123.
    KEGGimmu:19123.
    UCSCiuc008eiz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10445 mRNA. Translation: BAA01235.1 .
    AF034569 Genomic DNA. Translation: AAC33795.1 .
    AF318182 mRNA. Translation: AAK07918.1 .
    BC013896 mRNA. Translation: AAH13896.1 .
    D43755 Genomic DNA. Translation: BAA07812.1 .
    CCDSi CCDS29116.1.
    PIRi JX0210.
    RefSeqi NP_001036232.1. NM_001042767.2.
    NP_001036233.2. NM_001042768.2.
    NP_032960.3. NM_008934.3.
    UniGenei Mm.2786.
    Mm.489734.

    3D structure databases

    ProteinModelPortali P33587.
    SMRi P33587. Positions 46-87, 90-184, 212-448.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.218.

    PTM databases

    PhosphoSitei P33587.

    Proteomic databases

    PaxDbi P33587.
    PRIDEi P33587.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000171765 ; ENSMUSP00000132226 ; ENSMUSG00000024386 .
    GeneIDi 19123.
    KEGGi mmu:19123.
    UCSCi uc008eiz.1. mouse.

    Organism-specific databases

    CTDi 5624.
    MGIi MGI:97771. Proc.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00750000117249.
    HOGENOMi HOG000251821.
    HOVERGENi HBG013304.
    InParanoidi P33587.
    KOi K01344.
    OMAi PNYSKST.
    OrthoDBi EOG75B84T.
    PhylomeDBi P33587.
    TreeFami TF327329.

    Enzyme and pathway databases

    Reactomei REACT_225233. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    ChiTaRSi PROC. mouse.
    NextBioi 295718.
    PROi P33587.
    SOURCEi Search...

    Gene expression databases

    Bgeei P33587.
    CleanExi MM_PROC.
    Genevestigatori P33587.

    Family and domain databases

    Gene3Di 4.10.740.10. 1 hit.
    InterProi IPR017857. Coagulation_fac_subgr_Gla_dom.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR000294. GLA_domain.
    IPR012224. Pept_S1A_FX.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00594. Gla. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001143. Factor_X. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    PR00001. GLABLOOD.
    SMARTi SM00181. EGF. 1 hit.
    SM00179. EGF_CA. 1 hit.
    SM00069. GLA. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57630. SSF57630. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 1 hit.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 1 hit.
    PS01187. EGF_CA. 1 hit.
    PS00011. GLA_1. 1 hit.
    PS50998. GLA_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a mouse protein C cDNA."
      Tada N., Sato M., Tsujimura A., Iwase R., Hashimoto-Gotoh T.
      J. Biochem. 111:491-495(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    2. "Nucleotide structure and characterization of the murine gene encoding anticoagulant protein C."
      Jalbert L.R., Rosen E.D., Lissens A., Carmeliet P., Collen D., Castellino F.J.
      Thromb. Haemost. 79:310-316(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
    3. "Complete sequence of UC72A01."
      Korf I.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: C57BL/6.
    4. "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: Liver.
    5. "A comparative study of partial primary structures of the catalytic region of mammalian protein C."
      Murakawa M., Okamura T., Kamura T., Kuroiwa M., Harada M., Niho Y.
      Br. J. Haematol. 86:590-600(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 274-433.
      Strain: BALB/c.
    6. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
      Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
      J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-214.
      Strain: C57BL/6.
      Tissue: Plasma.

    Entry informationi

    Entry nameiPROC_MOUSE
    AccessioniPrimary (citable) accession number: P33587
    Secondary accession number(s): O35498, Q91WN8, Q99PC6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Calcium also binds, with stronger affinity to another site, beyond the GLA domain. This GLA-independent binding site is necessary for the recognition of the thrombin-thrombomodulin complex.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3