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Q05186 (RCN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Reticulocalbin-1
Gene names
Name:Rcn1
Synonyms:Rca1, Rcn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment.

Subcellular location

Endoplasmic reticulum lumen.

Miscellaneous

This protein has four functional calcium-binding sites; potential sites II and VI have lost affinity for calcium.

Sequence similarities

Belongs to the CREC family.

Contains 6 EF-hand domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.5
Chain24 – 325302Reticulocalbin-1
PRO_0000004146

Regions

Domain73 – 10836EF-hand 1
Domain109 – 14436EF-hand 2
Domain160 – 19536EF-hand 3
Domain197 – 23236EF-hand 4
Domain238 – 27336EF-hand 5
Domain274 – 30936EF-hand 6
Calcium binding86 – 97121
Calcium binding122 – 133122; possibly ancestral
Calcium binding173 – 184123
Calcium binding210 – 221124
Calcium binding251 – 262125
Calcium binding287 – 298126; possibly ancestral
Motif322 – 3254Prevents secretion from ER

Amino acid modifications

Glycosylation471N-linked (GlcNAc...); partial

Experimental info

Sequence conflict241K → G AA sequence Ref.5
Sequence conflict341R → I AA sequence Ref.5
Sequence conflict37 – 393SEL → DEE AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q05186 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 0470B10B5A8BC76D

FASTA32538,113
        10         20         30         40         50         60 
MARGGRLGLA LGLLLALVLA LRAKPTVRKE RVVRPDSELG ERPPEDNQSF QYDHEAFLGK 

        70         80         90        100        110        120 
EDSKTFDQLS PDESKERLGK IVDRIDSDGD GLVTTEELKL WIKRVQKRYI YDNVAKVWKD 

       130        140        150        160        170        180 
YDRDKDEKIS WEEYKQATYG YYLGNPAEFH DSSDHHTFKK MLPRDERRFK ASDLDGDLTA 

       190        200        210        220        230        240 
TREEFTAFLH PEEFEHMKEI VVLETLEDID KNGDGFVDQD EYIADMFSHE DNGPEPDWVL 

       250        260        270        280        290        300 
SEREQFNDFR DLNKDGKLDK DEIRHWILPQ DYDHAQAEAR HLVYESDKNK DEMLTKEEIL 

       310        320 
DNWNMFVGSQ ATNYGEDLTK NHDEL 

« Hide

References

« Hide 'large scale' references
[1]"Reticulocalbin, a novel endoplasmic reticulum resident Ca(2+)-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence."
Ozawa M., Muramatsu T.
J. Biol. Chem. 268:699-705(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure of the gene encoding mouse reticulocalbin, a novel endoplasmic reticulum-resident Ca(2+)-binding protein with multiple EF-hand motifs."
Ozawa M.
J. Biochem. 118:154-160(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
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].
Strain: C57BL/6.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[5]"Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-39.
Tissue: Fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13003 mRNA. Translation: BAA02366.1.
D43956 Genomic DNA. Translation: BAA07896.1.
BC049108 mRNA. Translation: AAH49108.1.
AK017494 mRNA. Translation: BAB30773.1.
AK133971 mRNA. Translation: BAE21962.1.
AK159973 mRNA. Translation: BAE35525.1.
PIRA45337.
RefSeqNP_033063.1. NM_009037.2.
UniGeneMm.4876.

3D structure databases

ProteinModelPortalQ05186.
SMRQ05186. Positions 67-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202839. 2 interactions.
IntActQ05186. 1 interaction.
MINTMINT-4132049.

PTM databases

PhosphoSiteQ05186.

2D gel databases

REPRODUCTION-2DPAGEIPI00137831.

Proteomic databases

PaxDbQ05186.
PRIDEQ05186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006128; ENSMUSP00000006128; ENSMUSG00000005973.
GeneID19672.
KEGGmmu:19672.
UCSCuc008lks.1. mouse.

Organism-specific databases

CTD5954.
MGIMGI:104559. Rcn1.

Phylogenomic databases

eggNOGNOG271367.
GeneTreeENSGT00550000074546.
HOGENOMHOG000230934.
HOVERGENHBG002834.
InParanoidQ05186.
OMANPEEFQD.
OrthoDBEOG73Z2TD.
PhylomeDBQ05186.
TreeFamTF314849.

Gene expression databases

BgeeQ05186.
CleanExMM_RCN1.
GenevestigatorQ05186.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028332. Rcn1_mml.
[Graphical view]
PANTHERPTHR10827:SF18. PTHR10827:SF18. 1 hit.
PfamPF13202. EF-hand_5. 2 hits.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 6 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRCN1. mouse.
NextBio296990.
PROQ05186.
SOURCESearch...

Entry information

Entry nameRCN1_MOUSE
AccessionPrimary (citable) accession number: Q05186
Secondary accession number(s): Q3TVU3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot