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Protein

Regucalcin

Gene

RGN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca2+ signaling, and Ca2+-dependent cellular processes and enzyme activities (By similarity).By similarity

Catalytic activityi

D-glucono-1,5-lactone + H2O = D-gluconate.2 Publications

Cofactori

Zn2+2 Publications, Mn2+2 Publications, Ca2+2 Publications, Mg2+2 PublicationsNote: Binds 1 divalent metal cation per subunit. Most active with Zn(2+) and Mn(2+) ions. The physiological cofactor is most likely Ca(2+) or Mg2+.2 Publications

Kineticsi

  1. KM=2.7 mM for gluconolactone (with Zn2+ as cofactor)1 Publication
  2. KM=0.6 mM for gluconolactone (with Mn2+ as cofactor)1 Publication
  3. KM=1.3 mM for gluconolactone (with Mg2+ as cofactor)1 Publication
  4. KM=3.7 mM for gluconolactone (with Ca2+ as cofactor)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi18 – 181Divalent metal cation1 Publication
    Binding sitei101 – 1011Substrate
    Binding sitei103 – 1031Substrate
    Binding sitei121 – 1211SubstrateBy similarity
    Metal bindingi154 – 1541Divalent metal cation1 Publication
    Active sitei204 – 2041Proton donor/acceptor1 Publication
    Metal bindingi204 – 2041Divalent metal cation1 Publication

    GO - Molecular functioni

    • calcium ion binding Source: UniProtKB
    • enzyme regulator activity Source: InterPro
    • gluconolactonase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regucalcin
    Short name:
    RC
    Alternative name(s):
    Gluconolactonase (EC:3.1.1.17)
    Short name:
    GNL
    Senescence marker protein 30
    Short name:
    SMP-30
    Gene namesi
    Name:RGN
    Synonyms:SMP30
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:9989. RGN.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi18 – 181E → A: Reduces enzyme activity by about 90%. 1 Publication
    Mutagenesisi103 – 1031N → A: Reduces enzyme activity by about 95%. 1 Publication
    Mutagenesisi154 – 1541N → A: Reduces enzyme activity by about 95%. 1 Publication
    Mutagenesisi204 – 2041D → A: Reduces enzyme activity by over 98%. 1 Publication

    Organism-specific databases

    PharmGKBiPA34359.

    Polymorphism and mutation databases

    BioMutaiRGN.
    DMDMi3334328.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 299299RegucalcinPRO_0000173046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei144 – 1441N6-succinyllysineBy similarity
    Modified residuei244 – 2441N6-succinyllysineBy similarity
    Modified residuei253 – 2531N6-succinyllysineBy similarity

    Proteomic databases

    PaxDbiQ15493.
    PeptideAtlasiQ15493.
    PRIDEiQ15493.

    PTM databases

    PhosphoSiteiQ15493.

    Expressioni

    Gene expression databases

    BgeeiQ15493.
    CleanExiHS_RGN.
    ExpressionAtlasiQ15493. baseline and differential.
    GenevisibleiQ15493. HS.

    Organism-specific databases

    HPAiHPA029102.
    HPA029103.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi114557. 2 interactions.
    MINTiMINT-3031653.
    STRINGi9606.ENSP00000253303.

    Structurei

    Secondary structure

    1
    299
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106Combined sources
    Beta strandi15 – 239Combined sources
    Turni24 – 274Combined sources
    Beta strandi28 – 336Combined sources
    Turni34 – 374Combined sources
    Beta strandi38 – 436Combined sources
    Turni44 – 463Combined sources
    Beta strandi49 – 535Combined sources
    Beta strandi58 – 647Combined sources
    Beta strandi67 – 737Combined sources
    Beta strandi76 – 816Combined sources
    Turni82 – 854Combined sources
    Beta strandi86 – 927Combined sources
    Beta strandi98 – 10710Combined sources
    Beta strandi113 – 1197Combined sources
    Beta strandi132 – 1376Combined sources
    Beta strandi143 – 15816Combined sources
    Beta strandi164 – 1696Combined sources
    Helixi170 – 1723Combined sources
    Beta strandi174 – 1807Combined sources
    Turni182 – 1843Combined sources
    Beta strandi187 – 1959Combined sources
    Helixi198 – 2003Combined sources
    Beta strandi202 – 2098Combined sources
    Beta strandi214 – 2196Combined sources
    Turni220 – 2223Combined sources
    Beta strandi223 – 2275Combined sources
    Turni229 – 2313Combined sources
    Beta strandi234 – 2396Combined sources
    Beta strandi241 – 2433Combined sources
    Beta strandi245 – 2528Combined sources
    Helixi253 – 2553Combined sources
    Beta strandi257 – 2637Combined sources
    Helixi269 – 2746Combined sources
    Turni276 – 2794Combined sources
    Beta strandi281 – 2855Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3G4EX-ray1.42A/B3-299[»]
    3G4HX-ray1.92A/B3-299[»]
    4GNBX-ray1.50A/B1-299[»]
    4GNCX-ray1.75A/B1-299[»]
    ProteinModelPortaliQ15493.
    SMRiQ15493. Positions 3-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15493.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SMP-30/CGR1 family.Curated

    Phylogenomic databases

    eggNOGiCOG3386.
    GeneTreeiENSGT00390000014995.
    HOGENOMiHOG000220627.
    HOVERGENiHBG004347.
    InParanoidiQ15493.
    KOiK01053.
    OMAiCARDGMD.
    OrthoDBiEOG77127C.
    PhylomeDBiQ15493.
    TreeFamiTF323663.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR008367. Regucalcin.
    IPR013658. SGL.
    IPR005511. SMP-30.
    [Graphical view]
    PfamiPF08450. SGL. 1 hit.
    [Graphical view]
    PRINTSiPR01791. REGUCALCIN.
    PR01790. SMP30FAMILY.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q15493-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MSSIKIECVL PENCRCGESP VWEEVSNSLL FVDIPAKKVC RWDSFTKQVQ
    60 70 80 90 100
    RVTMDAPVSS VALRQSGGYV ATIGTKFCAL NWKEQSAVVL ATVDNDKKNN
    110 120 130 140 150
    RFNDGKVDPA GRYFAGTMAE ETAPAVLERH QGALYSLFPD HHVKKYFDQV
    160 170 180 190 200
    DISNGLDWSL DHKIFYYIDS LSYSVDAFDY DLQTGQISNR RSVYKLEKEE
    210 220 230 240 250
    QIPDGMCIDA EGKLWVACYN GGRVIRLDPV TGKRLQTVKL PVDKTTSCCF
    260 270 280 290
    GGKNYSEMYV TCARDGMDPE GLLRQPEAGG IFKITGLGVK GIAPYSYAG
    Length:299
    Mass (Da):33,253
    Last modified:November 1, 1996 - v1
    Checksum:i95BA1C73B7B77635
    GO
    Isoform 2 (identifier: Q15493-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         116-187: Missing.
         188-188: S → A

    Note: No experimental confirmation available.
    Show »
    Length:227
    Mass (Da):24,968
    Checksum:i19BC938A52DA72D4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti292 – 2932IA → TS in BAD97080 (Ref. 4) Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei116 – 18772Missing in isoform 2. 1 PublicationVSP_025456Add
    BLAST
    Alternative sequencei188 – 1881S → A in isoform 2. 1 PublicationVSP_025457

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D31815 mRNA. Translation: BAA06602.1.
    AB028125 mRNA. Translation: BAA78693.1.
    AB032064 mRNA. Translation: BAA84082.1.
    AK290136 mRNA. Translation: BAF82825.1.
    AK223360 mRNA. Translation: BAD97080.1.
    AL513366 Genomic DNA. Translation: CAI41697.1.
    BC050371 mRNA. Translation: AAH50371.1.
    BC073173 mRNA. Translation: AAH73173.1.
    CCDSiCCDS14272.1. [Q15493-1]
    CCDS75968.1. [Q15493-2]
    PIRiS60035.
    RefSeqiNP_001269777.1. NM_001282848.1.
    NP_001269778.1. NM_001282849.1. [Q15493-2]
    NP_004674.1. NM_004683.5. [Q15493-1]
    NP_690608.1. NM_152869.3. [Q15493-1]
    XP_006724630.1. XM_006724567.1. [Q15493-2]
    UniGeneiHs.77854.

    Genome annotation databases

    EnsembliENST00000336169; ENSP00000338400; ENSG00000130988. [Q15493-1]
    ENST00000352078; ENSP00000253303; ENSG00000130988. [Q15493-1]
    ENST00000397180; ENSP00000380365; ENSG00000130988. [Q15493-1]
    ENST00000457380; ENSP00000406568; ENSG00000130988. [Q15493-2]
    GeneIDi9104.
    KEGGihsa:9104.
    UCSCiuc004dgz.1. human. [Q15493-1]
    uc010nhp.1. human. [Q15493-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D31815 mRNA. Translation: BAA06602.1.
    AB028125 mRNA. Translation: BAA78693.1.
    AB032064 mRNA. Translation: BAA84082.1.
    AK290136 mRNA. Translation: BAF82825.1.
    AK223360 mRNA. Translation: BAD97080.1.
    AL513366 Genomic DNA. Translation: CAI41697.1.
    BC050371 mRNA. Translation: AAH50371.1.
    BC073173 mRNA. Translation: AAH73173.1.
    CCDSiCCDS14272.1. [Q15493-1]
    CCDS75968.1. [Q15493-2]
    PIRiS60035.
    RefSeqiNP_001269777.1. NM_001282848.1.
    NP_001269778.1. NM_001282849.1. [Q15493-2]
    NP_004674.1. NM_004683.5. [Q15493-1]
    NP_690608.1. NM_152869.3. [Q15493-1]
    XP_006724630.1. XM_006724567.1. [Q15493-2]
    UniGeneiHs.77854.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3G4EX-ray1.42A/B3-299[»]
    3G4HX-ray1.92A/B3-299[»]
    4GNBX-ray1.50A/B1-299[»]
    4GNCX-ray1.75A/B1-299[»]
    ProteinModelPortaliQ15493.
    SMRiQ15493. Positions 3-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114557. 2 interactions.
    MINTiMINT-3031653.
    STRINGi9606.ENSP00000253303.

    PTM databases

    PhosphoSiteiQ15493.

    Polymorphism and mutation databases

    BioMutaiRGN.
    DMDMi3334328.

    Proteomic databases

    PaxDbiQ15493.
    PeptideAtlasiQ15493.
    PRIDEiQ15493.

    Protocols and materials databases

    DNASUi9104.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000336169; ENSP00000338400; ENSG00000130988. [Q15493-1]
    ENST00000352078; ENSP00000253303; ENSG00000130988. [Q15493-1]
    ENST00000397180; ENSP00000380365; ENSG00000130988. [Q15493-1]
    ENST00000457380; ENSP00000406568; ENSG00000130988. [Q15493-2]
    GeneIDi9104.
    KEGGihsa:9104.
    UCSCiuc004dgz.1. human. [Q15493-1]
    uc010nhp.1. human. [Q15493-2]

    Organism-specific databases

    CTDi9104.
    GeneCardsiGC0XP046937.
    HGNCiHGNC:9989. RGN.
    HPAiHPA029102.
    HPA029103.
    MIMi300212. gene.
    neXtProtiNX_Q15493.
    PharmGKBiPA34359.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3386.
    GeneTreeiENSGT00390000014995.
    HOGENOMiHOG000220627.
    HOVERGENiHBG004347.
    InParanoidiQ15493.
    KOiK01053.
    OMAiCARDGMD.
    OrthoDBiEOG77127C.
    PhylomeDBiQ15493.
    TreeFamiTF323663.

    Miscellaneous databases

    EvolutionaryTraceiQ15493.
    GeneWikiiRGN_(gene).
    GenomeRNAii9104.
    NextBioi34129.
    PROiQ15493.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ15493.
    CleanExiHS_RGN.
    ExpressionAtlasiQ15493. baseline and differential.
    GenevisibleiQ15493. HS.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR008367. Regucalcin.
    IPR013658. SGL.
    IPR005511. SMP-30.
    [Graphical view]
    PfamiPF08450. SGL. 1 hit.
    [Graphical view]
    PRINTSiPR01791. REGUCALCIN.
    PR01790. SMP30FAMILY.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Isolation of cDNA clone encoding human homologue of senescence marker protein-30 (SMP30) and its location on the X chromosome."
      Fujita T., Mandel J.-L., Shirasawa T., Hino O., Shirai T., Maruyama N.
      Biochim. Biophys. Acta 1263:249-252(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Transcript heterogeneity of the human gene for Ca2+-binding protein regucalcin."
      Misawa H., Yamaguchi M.
      Int. J. Mol. Med. 5:283-287(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Thalamus.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Colon and PNS.
    7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Crystal structure of human senescence marker protein 30: insights linking structural, enzymatic, and physiological functions."
      Chakraborti S., Bahnson B.J.
      Biochemistry 49:3436-3444(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEXES WITH CALCIUM AND ZINC IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF GLU-18; ASN-103; ASN-154 AND ASP-204.
    9. "Structural basis of the gamma-lactone-ring formation in ascorbic acid biosynthesis by the senescence marker protein-30/gluconolactonase."
      Aizawa S., Senda M., Harada A., Maruyama N., Ishida T., Aigaki T., Ishigami A., Senda T.
      PLoS ONE 8:E53706-E53706(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH DIVALENT METAL CATION AND SUBSTRATE ANALOG, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, SUBUNIT.

    Entry informationi

    Entry nameiRGN_HUMAN
    AccessioniPrimary (citable) accession number: Q15493
    Secondary accession number(s): A4FTW1
    , A8K271, Q53FC9, Q5JRR5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: June 24, 2015
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    Gluconolactonase catalyzes a key step in ascorbic acid (vitamin C) biosynthesis, but primates lack the last enzyme in the pathway and are unable to synthesize vitamin C.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.