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Protein

Arginase-1

Gene

Arg1

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

Functioni

Catalytic activityi

L-arginine + H2O = L-ornithine + urea.

Cofactori

Mn2+PROSITE-ProRule annotation2 PublicationsNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation2 Publications

Enzyme regulationi

Inactivated by diethyl pyrocarbonate (DEPC).

Kineticsi

  1. KM=1.4 mM for arginine2 Publications

    Pathway:iurea cycle

    This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and urea from L-arginine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Arginase-1 (Arg1), Arginase (Arg2), Arginase-2, mitochondrial (Arg2), Arginase (Arg2)
    This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and urea from L-arginine, the pathway urea cycle and in Nitrogen metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi101 – 1011Manganese 1
    Metal bindingi124 – 1241Manganese 1
    Metal bindingi124 – 1241Manganese 2
    Metal bindingi126 – 1261Manganese 2
    Metal bindingi128 – 1281Manganese 1
    Binding sitei183 – 1831Substrate
    Metal bindingi232 – 2321Manganese 1
    Metal bindingi232 – 2321Manganese 2
    Metal bindingi234 – 2341Manganese 2

    GO - Molecular functioni

    • arginase activity Source: RGD
    • manganese ion binding Source: RGD

    GO - Biological processi

    • aging Source: RGD
    • arginine catabolic process to ornithine Source: RGD
    • arginine metabolic process Source: RGD
    • cellular response to dexamethasone stimulus Source: RGD
    • cellular response to glucagon stimulus Source: RGD
    • cellular response to hydrogen peroxide Source: RGD
    • cellular response to interleukin-4 Source: RGD
    • cellular response to lipopolysaccharide Source: RGD
    • cellular response to transforming growth factor beta stimulus Source: RGD
    • collagen biosynthetic process Source: RGD
    • female pregnancy Source: RGD
    • liver development Source: RGD
    • lung development Source: RGD
    • mammary gland involution Source: RGD
    • maternal process involved in female pregnancy Source: RGD
    • positive regulation of endothelial cell proliferation Source: RGD
    • protein homotrimerization Source: RGD
    • regulation of L-arginine import Source: RGD
    • response to amine Source: RGD
    • response to amino acid Source: RGD
    • response to axon injury Source: RGD
    • response to cadmium ion Source: RGD
    • response to drug Source: RGD
    • response to herbicide Source: RGD
    • response to lipopolysaccharide Source: RGD
    • response to manganese ion Source: RGD
    • response to methylmercury Source: RGD
    • response to peptide hormone Source: RGD
    • response to selenium ion Source: RGD
    • response to steroid hormone Source: RGD
    • response to vitamin A Source: RGD
    • response to vitamin E Source: RGD
    • response to wounding Source: RGD
    • response to zinc ion Source: RGD
    • urea cycle Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Arginine metabolism, Urea cycle

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.5.3.1. 5301.
    ReactomeiREACT_328693. Urea cycle.
    SABIO-RKP07824.
    UniPathwayiUPA00158; UER00270.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginase-1 (EC:3.5.3.1)
    Alternative name(s):
    Liver-type arginase
    Type I arginase
    Gene namesi
    Name:Arg1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Chromosome 1

    Organism-specific databases

    RGDi2150. Arg1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: RGD
    • extracellular exosome Source: Ensembl
    • extracellular space Source: RGD
    • mitochondrial outer membrane Source: RGD
    • neuronal cell body Source: RGD
    • neuron projection Source: RGD
    • nucleus Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011H → E: Reduced catalytic activity. No effect on manganese binding. 1 Publication
    Mutagenesisi128 – 1281D → E or N: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication
    Mutagenesisi141 – 1411H → A, C or D: Strongly reduced catalytic activity. Minor effect on affinity for arginine. 1 Publication
    Mutagenesisi141 – 1411H → N: Reduced affinity for arginine and reduced catalytic activity. 1 Publication
    Mutagenesisi232 – 2321D → A: Loss of one manganese ion and strongly reduced catalytic activity. 1 Publication
    Mutagenesisi232 – 2321D → C: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication
    Mutagenesisi234 – 2341D → A, E or H: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication
    Mutagenesisi235 – 2351G → A: 56% of wild-type activity. 1 Publication
    Mutagenesisi235 – 2351G → R: Loss of manganese-binding and activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Arginase-1PRO_0000173697Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171N6-succinyllysineBy similarity
    Modified residuei62 – 621PhosphoserineBy similarity
    Modified residuei72 – 721PhosphoserineBy similarity
    Modified residuei75 – 751N6-succinyllysineBy similarity
    Modified residuei163 – 1631PhosphoserineBy similarity
    Modified residuei217 – 2171PhosphoserineBy similarity
    Modified residuei281 – 2811PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP07824.
    PRIDEiP07824.

    PTM databases

    PhosphoSiteiP07824.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Inductioni

    By arginine or homoarginine.

    Gene expression databases

    GenevisibleiP07824. RN.

    Interactioni

    Subunit structurei

    Homotrimer.2 Publications

    Protein-protein interaction databases

    BioGridi247899. 2 interactions.
    IntActiP07824. 1 interaction.
    MINTiMINT-4567374.
    STRINGi10116.ENSRNOP00000017911.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125Combined sources
    Beta strandi19 – 213Combined sources
    Helixi22 – 265Combined sources
    Helixi27 – 337Combined sources
    Helixi36 – 405Combined sources
    Beta strandi43 – 453Combined sources
    Beta strandi47 – 526Combined sources
    Beta strandi64 – 663Combined sources
    Beta strandi67 – 693Combined sources
    Helixi70 – 8920Combined sources
    Beta strandi93 – 975Combined sources
    Helixi101 – 1033Combined sources
    Helixi104 – 11411Combined sources
    Beta strandi119 – 1268Combined sources
    Turni132 – 1343Combined sources
    Beta strandi136 – 1383Combined sources
    Helixi140 – 1423Combined sources
    Helixi144 – 1485Combined sources
    Helixi150 – 1523Combined sources
    Beta strandi153 – 1564Combined sources
    Turni160 – 1645Combined sources
    Helixi171 – 1733Combined sources
    Beta strandi174 – 1796Combined sources
    Helixi184 – 19310Combined sources
    Beta strandi196 – 1994Combined sources
    Helixi200 – 2067Combined sources
    Helixi208 – 22013Combined sources
    Beta strandi221 – 2233Combined sources
    Beta strandi227 – 2326Combined sources
    Helixi233 – 2353Combined sources
    Turni238 – 2403Combined sources
    Beta strandi244 – 2463Combined sources
    Helixi254 – 26714Combined sources
    Beta strandi270 – 2767Combined sources
    Helixi280 – 2823Combined sources
    Beta strandi283 – 2853Combined sources
    Helixi286 – 30318Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D3VX-ray1.70A/B1-323[»]
    1HQ5X-ray2.30A/B1-323[»]
    1HQFX-ray2.90A/B/C1-323[»]
    1HQGX-ray2.00A/B/C1-323[»]
    1HQHX-ray2.80A/B/C1-323[»]
    1HQXX-ray3.00A/B/C1-323[»]
    1P8MX-ray2.84A/B/C6-319[»]
    1P8NX-ray2.90A/B/C6-319[»]
    1P8OX-ray2.96A/B/C6-319[»]
    1P8PX-ray2.50A/B/C6-319[»]
    1P8QX-ray2.95A/B/C6-319[»]
    1P8RX-ray2.50A/B6-313[»]
    1P8SX-ray3.20A/B/C6-319[»]
    1R1OX-ray2.80A/B/C1-323[»]
    1RLAX-ray2.10A/B/C1-323[»]
    1T4PX-ray2.60A/B/C6-319[»]
    1T4RX-ray2.60A/B/C6-319[»]
    1T4SX-ray2.80A/B/C6-319[»]
    1T4TX-ray2.20A/B/C6-319[»]
    1T5FX-ray2.20A/B/C6-319[»]
    1T5GX-ray2.40A/B/C6-319[»]
    1TA1X-ray2.50A/B/C6-319[»]
    1TBHX-ray2.70A/B/C6-319[»]
    1TBJX-ray2.80A/B/C6-319[»]
    1TBLX-ray3.10A/B/C6-319[»]
    1ZPEX-ray1.70A/B/C6-319[»]
    1ZPGX-ray1.90A/B/C6-319[»]
    2RLAX-ray3.00A/B/C1-323[»]
    3E8QX-ray2.90A/B/C1-323[»]
    3E8ZX-ray2.00A/B/C1-323[»]
    3E9BX-ray2.15A/B/C1-323[»]
    3RLAX-ray2.54A/B/C1-323[»]
    4RLAX-ray2.94A/B/C1-323[»]
    5RLAX-ray2.74A/B/C1-323[»]
    ProteinModelPortaliP07824.
    SMRiP07824. Positions 6-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07824.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni126 – 1305Substrate binding
    Regioni137 – 1393Substrate binding

    Sequence similaritiesi

    Belongs to the arginase family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0010.
    GeneTreeiENSGT00530000063082.
    HOGENOMiHOG000204319.
    HOVERGENiHBG003030.
    InParanoidiP07824.
    KOiK01476.
    OMAiEQECDVK.
    OrthoDBiEOG747PJ5.
    PhylomeDBiP07824.
    TreeFamiTF300034.

    Family and domain databases

    Gene3Di3.40.800.10. 1 hit.
    InterProiIPR014033. Arginase.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view]
    PANTHERiPTHR11358. PTHR11358. 1 hit.
    PfamiPF00491. Arginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036979. Arginase. 1 hit.
    PRINTSiPR00116. ARGINASE.
    TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
    PROSITEiPS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07824-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSKPKPIEI IGAPFSKGQP RGGVEKGPAA LRKAGLVEKL KETEYNVRDH
    60 70 80 90 100
    GDLAFVDVPN DSPFQIVKNP RSVGKANEQL AAVVAETQKN GTISVVLGGD
    110 120 130 140 150
    HSMAIGSISG HARVHPDLCV IWVDAHTDIN TPLTTSSGNL HGQPVAFLLK
    160 170 180 190 200
    ELKGKFPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYII KTLGIKYFSM
    210 220 230 240 250
    TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPVF TPATGTPVVG
    260 270 280 290 300
    GLSYREGLYI TEEIYKTGLL SGLDIMEVNP TLGKTPEEVT RTVNTAVALT
    310 320
    LSCFGTKREG NHKPETDYLK PPK
    Length:323
    Mass (Da):34,973
    Last modified:April 1, 1990 - v2
    Checksum:i5A92CB0931F9A053
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti298 – 2981A → P in AAA40761 (PubMed:3571256).Curated
    Sequence conflicti298 – 2981A → P in AAA40760 (PubMed:3571256).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02720 mRNA. Translation: AAA40761.1.
    M17931
    , M17924, M17925, M17926, M17927, M17928, M17929, M17930 Genomic DNA. Translation: AAA40760.1.
    BC091158 mRNA. Translation: AAH91158.1.
    PIRiA26702.
    RefSeqiNP_058830.2. NM_017134.3.
    UniGeneiRn.9857.

    Genome annotation databases

    EnsembliENSRNOT00000017911; ENSRNOP00000017911; ENSRNOG00000013304.
    GeneIDi29221.
    KEGGirno:29221.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02720 mRNA. Translation: AAA40761.1.
    M17931
    , M17924, M17925, M17926, M17927, M17928, M17929, M17930 Genomic DNA. Translation: AAA40760.1.
    BC091158 mRNA. Translation: AAH91158.1.
    PIRiA26702.
    RefSeqiNP_058830.2. NM_017134.3.
    UniGeneiRn.9857.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D3VX-ray1.70A/B1-323[»]
    1HQ5X-ray2.30A/B1-323[»]
    1HQFX-ray2.90A/B/C1-323[»]
    1HQGX-ray2.00A/B/C1-323[»]
    1HQHX-ray2.80A/B/C1-323[»]
    1HQXX-ray3.00A/B/C1-323[»]
    1P8MX-ray2.84A/B/C6-319[»]
    1P8NX-ray2.90A/B/C6-319[»]
    1P8OX-ray2.96A/B/C6-319[»]
    1P8PX-ray2.50A/B/C6-319[»]
    1P8QX-ray2.95A/B/C6-319[»]
    1P8RX-ray2.50A/B6-313[»]
    1P8SX-ray3.20A/B/C6-319[»]
    1R1OX-ray2.80A/B/C1-323[»]
    1RLAX-ray2.10A/B/C1-323[»]
    1T4PX-ray2.60A/B/C6-319[»]
    1T4RX-ray2.60A/B/C6-319[»]
    1T4SX-ray2.80A/B/C6-319[»]
    1T4TX-ray2.20A/B/C6-319[»]
    1T5FX-ray2.20A/B/C6-319[»]
    1T5GX-ray2.40A/B/C6-319[»]
    1TA1X-ray2.50A/B/C6-319[»]
    1TBHX-ray2.70A/B/C6-319[»]
    1TBJX-ray2.80A/B/C6-319[»]
    1TBLX-ray3.10A/B/C6-319[»]
    1ZPEX-ray1.70A/B/C6-319[»]
    1ZPGX-ray1.90A/B/C6-319[»]
    2RLAX-ray3.00A/B/C1-323[»]
    3E8QX-ray2.90A/B/C1-323[»]
    3E8ZX-ray2.00A/B/C1-323[»]
    3E9BX-ray2.15A/B/C1-323[»]
    3RLAX-ray2.54A/B/C1-323[»]
    4RLAX-ray2.94A/B/C1-323[»]
    5RLAX-ray2.74A/B/C1-323[»]
    ProteinModelPortaliP07824.
    SMRiP07824. Positions 6-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi247899. 2 interactions.
    IntActiP07824. 1 interaction.
    MINTiMINT-4567374.
    STRINGi10116.ENSRNOP00000017911.

    Chemistry

    ChEMBLiCHEMBL3232699.

    PTM databases

    PhosphoSiteiP07824.

    Proteomic databases

    PaxDbiP07824.
    PRIDEiP07824.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000017911; ENSRNOP00000017911; ENSRNOG00000013304.
    GeneIDi29221.
    KEGGirno:29221.

    Organism-specific databases

    CTDi383.
    RGDi2150. Arg1.

    Phylogenomic databases

    eggNOGiCOG0010.
    GeneTreeiENSGT00530000063082.
    HOGENOMiHOG000204319.
    HOVERGENiHBG003030.
    InParanoidiP07824.
    KOiK01476.
    OMAiEQECDVK.
    OrthoDBiEOG747PJ5.
    PhylomeDBiP07824.
    TreeFamiTF300034.

    Enzyme and pathway databases

    UniPathwayiUPA00158; UER00270.
    BRENDAi3.5.3.1. 5301.
    ReactomeiREACT_328693. Urea cycle.
    SABIO-RKP07824.

    Miscellaneous databases

    EvolutionaryTraceiP07824.
    NextBioi608419.
    PROiP07824.

    Gene expression databases

    GenevisibleiP07824. RN.

    Family and domain databases

    Gene3Di3.40.800.10. 1 hit.
    InterProiIPR014033. Arginase.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view]
    PANTHERiPTHR11358. PTHR11358. 1 hit.
    PfamiPF00491. Arginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036979. Arginase. 1 hit.
    PRINTSiPR00116. ARGINASE.
    TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
    PROSITEiPS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver arginase."
      Kawamoto S., Amaya Y., Murakami K., Tokunaga F., Iwanaga S., Kobayashi K., Saheki T., Kimura S., Mori M.
      J. Biol. Chem. 262:6280-6283(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Structural organization of the gene for rat liver-type arginase."
      Ohtake A., Takiguchi M., Shigeto Y., Amaya Y., Kawamoto S., Mori M.
      J. Biol. Chem. 263:2245-2249(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      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: Liver.
    4. "Functional consequences of the G235R mutation in liver arginase leading to hyperargininemia."
      Lavulo L.T., Emig F.A., Ash D.E.
      Arch. Biochem. Biophys. 399:49-55(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-235.
    5. "Structure of a unique binuclear manganese cluster in arginase."
      Kanyo Z.F., Scolnick L.R., Ash D.E., Christianson D.W.
      Nature 383:554-557(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    6. "Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function."
      Scolnick L.R., Kanyo Z.F., Cavalli R.C., Ash D.E., Christianson D.W.
      Biochemistry 36:10558-10565(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    7. "Arginase-boronic acid complex highlights a physiological role in erectile function."
      Cox J.D., Kim N.N., Traish A.M., Christianson D.W.
      Nat. Struct. Biol. 6:1043-1047(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    8. "Structural and functional importance of first-shell metal ligands in the binuclear manganese cluster of arginase I."
      Cama E., Emig F.A., Ash D.E., Christianson D.W.
      Biochemistry 42:7748-7758(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 6-319 OF MUTANTS ASN-101; GLU-101; ASN-128; GLU-128; ALA-232; CYS-232 AND GLU-234 IN COMPLEXES WITH MANGANESE IONS, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-101; ASP-128; ASP-232 AND ASP-234.
    9. "Design of amino acid aldehydes as transition-state analogue inhibitors of arginase."
      Shin H., Cama E., Christianson D.W.
      J. Am. Chem. Soc. 126:10278-10284(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-319 IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR (S)-2-AMINO-7-OXOHEPTANOIC ACID.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 6-319 OF MUTANTS ALA-141; ASN-141; ASP-141 AND CYS-141 IN COMPLEX WITH MANGANESE IONS, COFACTOR, MUTAGENESIS OF HIS-141, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiARGI1_RAT
    AccessioniPrimary (citable) accession number: P07824
    Secondary accession number(s): Q5BK93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: April 1, 1990
    Last modified: July 22, 2015
    This is version 156 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.