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Q8BP92 (RCN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. 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-2
Alternative name(s):
Taipoxin-associated calcium-binding protein 49
Short name=TCBP-49
Gene names
Name:Rcn2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Not known. Binds calcium By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Sequence similarities

Belongs to the CREC family.

Contains 6 EF-hand domains.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 By similarity
Chain26 – 320295Reticulocalbin-2
PRO_0000004149

Regions

Domain64 – 9936EF-hand 1
Domain100 – 13536EF-hand 2
Domain150 – 18536EF-hand 3
Domain189 – 22436EF-hand 4
Domain230 – 26536EF-hand 5
Domain266 – 30136EF-hand 6
Calcium binding77 – 88121 Potential
Calcium binding113 – 124122 Potential
Calcium binding165 – 176123; possibly ancestral Potential
Calcium binding202 – 213124 Potential
Calcium binding243 – 254125 Potential
Calcium binding279 – 290126 Potential
Motif317 – 3204Prevents secretion from ER Potential

Experimental info

Sequence conflict1191A → DP in AAC05132. Ref.1
Sequence conflict302 – 3032EA → DQ in AAC05132. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BP92 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 62195C004F8D7C9D

FASTA32037,271
        10         20         30         40         50         60 
MRLGPRPAAL GLLLPLLLYA AVAGASKAEE LHYPQGEHRA DYDREALLGV QEDVDEYVKL 

        70         80         90        100        110        120 
GHEEQQRRLQ SIIKKIDSDS DGFLTENELS QWIQMSFKHY AMQEAKQQFV EYDKNSDGAV 

       130        140        150        160        170        180 
TWDEYNIQMY DRVIDFDENT ALDDTEEGSF RQLHLKDKKR FEKANQDSGP GLSLEEFIAF 

       190        200        210        220        230        240 
EHPEEVDYMT EFVIQEALEE HDKNGDGFVS LEEFLGDYRR DPTANEDPEW ILVEKDRFVN 

       250        260        270        280        290        300 
DYDKDNDGRL DPQELLSWVV PNNQGIAQEE ALHLIDEMDL NSDKKLSEEE ILENQDLFLT 

       310        320 
SEATDYGRQL HDDYFYHDEL 

« Hide

References

« Hide 'large scale' references
[1]"Mouse taipoxin-associated calcium binding protein 49 (TCBP49)."
Perin M.S.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.
[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: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF049125 mRNA. Translation: AAC05132.1.
AK077486 mRNA. Translation: BAC36825.1.
BC132320 mRNA. Translation: AAI32321.1.
BC145668 mRNA. Translation: AAI45669.1.
PIRJC5402.
RefSeqNP_036122.2. NM_011992.2.
UniGeneMm.1782.

3D structure databases

ProteinModelPortalQ8BP92.
SMRQ8BP92. Positions 58-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205029. 3 interactions.
DIPDIP-46963N.
IntActQ8BP92. 7 interactions.
MINTMINT-1605271.
STRING10090.ENSMUSP00000109915.

Proteomic databases

PaxDbQ8BP92.
PRIDEQ8BP92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000114276; ENSMUSP00000109915; ENSMUSG00000032320.
GeneID26611.
KEGGmmu:26611.
UCSCuc009pss.1. mouse.

Organism-specific databases

CTD5955.
MGIMGI:1349765. Rcn2.

Phylogenomic databases

eggNOGNOG124414.
GeneTreeENSGT00550000074546.
HOGENOMHOG000230934.
HOVERGENHBG002834.
InParanoidA2RT07.
OMASEADKDH.
TreeFamTF314849.

Gene expression databases

ArrayExpressQ8BP92.
BgeeQ8BP92.
CleanExMM_RCN2.
GenevestigatorQ8BP92.

Family and domain databases

Gene3D1.10.238.10. 3 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13202. EF-hand_5. 1 hit.
PF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTSM00054. EFh. 5 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 5 hits.
PS50222. EF_HAND_2. 5 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRCN2. mouse.
NextBio304663.
PROQ8BP92.
SOURCESearch...

Entry information

Entry nameRCN2_MOUSE
AccessionPrimary (citable) accession number: Q8BP92
Secondary accession number(s): A2RT07, O70341
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: March 1, 2003
Last modified: March 19, 2014
This is version 98 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