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Q15493 (RGN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regucalcin

Short name=RC
Alternative name(s):
Gluconolactonase
Short name=GNL
EC=3.1.1.17
Senescence marker protein 30
Short name=SMP-30
Gene names
Name:RGN
Synonyms:SMP30
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

D-glucono-1,5-lactone + H2O = D-gluconate. Ref.7 Ref.8

Cofactor

Binds 1 divalent metal cation per subunit. Most active with zinc and manganese ions. The physiological cofactor is most likely calcium or magnesium. Ref.7 Ref.8

Subunit structure

Monomer. Ref.8

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the SMP-30/CGR1 family.

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.

Biophysicochemical properties

Kinetic parameters:

KM=2.7 mM for gluconolactone (with Zn2+ as cofactor) Ref.7

KM=0.6 mM for gluconolactone (with Mn2+ as cofactor)

KM=1.3 mM for gluconolactone (with Mg2+ as cofactor)

KM=3.7 mM for gluconolactone (with Ca2+ as cofactor)

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15493-1)

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.
Isoform 2 (identifier: Q15493-2)

The sequence of this isoform differs from the canonical sequence as follows:
     116-187: Missing.
     188-188: S → A
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Regucalcin
PRO_0000173046

Sites

Active site2041Proton donor/acceptor Probable
Metal binding181Divalent metal cation
Metal binding1541Divalent metal cation
Metal binding2041Divalent metal cation
Binding site1011Substrate
Binding site1031Substrate
Binding site1211Substrate By similarity

Amino acid modifications

Modified residue1441N6-succinyllysine By similarity
Modified residue2441N6-succinyllysine By similarity
Modified residue2531N6-succinyllysine By similarity

Natural variations

Alternative sequence116 – 18772Missing in isoform 2.
VSP_025456
Alternative sequence1881S → A in isoform 2.
VSP_025457

Experimental info

Mutagenesis181E → A: Reduces enzyme activity by about 90%. Ref.7
Mutagenesis1031N → A: Reduces enzyme activity by about 95%. Ref.7
Mutagenesis1541N → A: Reduces enzyme activity by about 95%. Ref.7
Mutagenesis2041D → A: Reduces enzyme activity by over 98%. Ref.7
Sequence conflict292 – 2932IA → TS in BAD97080. Ref.4

Secondary structure

.............................................................. 299
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 95BA1C73B7B77635

FASTA29933,253
        10         20         30         40         50         60 
MSSIKIECVL PENCRCGESP VWEEVSNSLL FVDIPAKKVC RWDSFTKQVQ RVTMDAPVSS 

        70         80         90        100        110        120 
VALRQSGGYV ATIGTKFCAL NWKEQSAVVL ATVDNDKKNN RFNDGKVDPA GRYFAGTMAE 

       130        140        150        160        170        180 
ETAPAVLERH QGALYSLFPD HHVKKYFDQV DISNGLDWSL DHKIFYYIDS LSYSVDAFDY 

       190        200        210        220        230        240 
DLQTGQISNR RSVYKLEKEE QIPDGMCIDA EGKLWVACYN GGRVIRLDPV TGKRLQTVKL 

       250        260        270        280        290 
PVDKTTSCCF GGKNYSEMYV TCARDGMDPE GLLRQPEAGG IFKITGLGVK GIAPYSYAG 

« Hide

Isoform 2 [UniParc].

Checksum: 19BC938A52DA72D4
Show »

FASTA22724,968

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
[8]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14272.1. [Q15493-1]
PIRS60035.
RefSeqNP_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]
UniGeneHs.77854.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3G4EX-ray1.42A/B3-299[»]
3G4HX-ray1.92A/B3-299[»]
4GNBX-ray1.50A/B1-299[»]
4GNCX-ray1.75A/B1-299[»]
ProteinModelPortalQ15493.
SMRQ15493. Positions 3-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114557. 1 interaction.
MINTMINT-3031653.
STRING9606.ENSP00000253303.

PTM databases

PhosphoSiteQ15493.

Polymorphism databases

DMDM3334328.

Proteomic databases

MaxQBQ15493.
PaxDbQ15493.
PeptideAtlasQ15493.
PRIDEQ15493.

Protocols and materials databases

DNASU9104.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336169; ENSP00000338400; ENSG00000130988. [Q15493-1]
ENST00000352078; ENSP00000253303; ENSG00000130988. [Q15493-1]
ENST00000397180; ENSP00000380365; ENSG00000130988. [Q15493-1]
ENST00000457380; ENSP00000406568; ENSG00000130988. [Q15493-2]
ENST00000604038; ENSP00000474799; ENSG00000270349. [Q15493-1]
ENST00000604343; ENSP00000473757; ENSG00000270349. [Q15493-1]
ENST00000604471; ENSP00000474983; ENSG00000270349. [Q15493-2]
ENST00000605133; ENSP00000474876; ENSG00000270349. [Q15493-1]
GeneID9104.
KEGGhsa:9104.
UCSCuc004dgz.1. human. [Q15493-1]
uc010nhp.1. human. [Q15493-2]

Organism-specific databases

CTD9104.
GeneCardsGC0XP046937.
HGNCHGNC:9989. RGN.
HPAHPA029102.
HPA029103.
MIM300212. gene.
neXtProtNX_Q15493.
PharmGKBPA34359.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3386.
HOGENOMHOG000220627.
HOVERGENHBG004347.
InParanoidQ15493.
KOK01053.
OMACVLRENC.
OrthoDBEOG77127C.
PhylomeDBQ15493.
TreeFamTF323663.

Gene expression databases

BgeeQ15493.
CleanExHS_RGN.
GenevestigatorQ15493.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR008367. Regucalcin.
IPR013658. SGL.
IPR005511. SMP-30.
[Graphical view]
PfamPF08450. SGL. 1 hit.
[Graphical view]
PRINTSPR01791. REGUCALCIN.
PR01790. SMP30FAMILY.
ProtoNetSearch...

Other

EvolutionaryTraceQ15493.
GeneWikiRGN_(gene).
GenomeRNAi9104.
NextBio34129.
PROQ15493.
SOURCESearch...

Entry information

Entry nameRGN_HUMAN
AccessionPrimary (citable) accession number: Q15493
Secondary accession number(s): A4FTW1 expand/collapse secondary AC list , A8K271, Q53FC9, Q5JRR5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM