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Q8BPM6 (RIC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein RIC-3
Alternative name(s):
Resistant to inhibitor of cholinesterase 3
Gene names
Name:Ric3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes functional expression of homomeric alpha-7 and alpha-8 nicotinic acetylcholine receptors at the cell surface. May also promote functional expression of homomeric serotoninergic 5-HT3 receptors, and of heteromeric acetylcholine receptors alpha-3/beta-2, alpha-3/beta-4, alpha-4/beta-2 and alpha-4/beta-4. Ref.4

Subunit structure

Monomer and homodimer. Interacts with CHRNA7, CHRNA3, CHRNA4, CHRNB2, CHRNB4 and HTR3A By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Ref.4.

Tissue specificity

Expressed in brain, with highest levels in hippocampus, cerebellum and superior colliculus. Ref.3

Domain

The coiled-coil domain mediates transient homodimerization with other acetylcholine receptor-bound RIC3 molecules, promoting stepwise ACHR homomeric assembly at the membrane.

Sequence similarities

Belongs to the ric-3 family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BPM6-1)

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: Q8BPM6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8BPM6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     223-228: YPEETY → KMPLPC
     229-367: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 367336Protein RIC-3
PRO_0000302732

Regions

Topological domain32 – 9564Lumenal Potential
Transmembrane96 – 11621Helical; Potential
Topological domain117 – 367251Cytoplasmic Potential
Coiled coil138 – 16932 Ref.4
Compositional bias81 – 9414Poly-Gly

Amino acid modifications

Modified residue2011N6-acetyllysine; alternate By similarity
Cross-link201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Natural variations

Alternative sequence1 – 159159Missing in isoform 2.
VSP_027944
Alternative sequence223 – 2286YPEETY → KMPLPC in isoform 3.
VSP_027945
Alternative sequence229 – 367139Missing in isoform 3.
VSP_027946

Experimental info

Sequence conflict461R → Q in BAC38452. Ref.1

Sequences

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

Last modified September 11, 2007. Version 2.
Checksum: 688D772716BDE892

FASTA36740,283
        10         20         30         40         50         60 
MAYSTVQRVA LASGLVLAVS LLLPKAFLSR GKRPEPPPGP EGKLDRFPPM MHHHSAPSDG 

        70         80         90        100        110        120 
QTPGARFQRS HLAEAFAKAK GAGGGAGGGG SGRGLMGQII PIYGFGIFLY ILYILFKLSK 

       130        140        150        160        170        180 
GKTAEDRNCS TAPPGNAHRK ITNFELVQLQ EKLKETEEAM EKLINRVGPN GESRAQAVTS 

       190        200        210        220        230        240 
DQEKRLLHQL REITRVMKEG KFIDTSPEKE AEEAPYMEDW EGYPEETYPI YDLSDGIKRR 

       250        260        270        280        290        300 
QETILVDYPD LKEPSAEEIA EQMGEIEEEG SERLSWDHLP TDPGAQKDNS VAPCDPKPES 

       310        320        330        340        350        360 
CSCCVHEEED PAVLAENAGF SADGYSEQEE ATKENLPQDF TNEGLGVSTD NAHVGGMLRK 


RNPQGFE 

« Hide

Isoform 2 [UniParc].

Checksum: D59EB1FB2925FC26
Show »

FASTA20823,347
Isoform 3 [UniParc].

Checksum: 5A7F826B78472F08
Show »

FASTA22824,909

References

« Hide 'large scale' references
[1]"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] (ISOFORM 3).
Strain: C57BL/6J.
Tissue: Cerebellum, Eye and Retina.
[2]"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] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Brain.
[3]"Conservation within the RIC-3 gene family. Effectors of mammalian nicotinic acetylcholine receptor expression."
Halevi S., Yassin L., Eshel M., Sala F., Sala S., Criado M., Treinin M.
J. Biol. Chem. 278:34411-34417(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"Mouse RIC-3, an endoplasmic reticulum chaperone, promotes assembly of the alpha7 acetylcholine receptor through a cytoplasmic coiled-coil domain."
Wang Y., Yao Y., Tang X.Q., Wang Z.Z.
J. Neurosci. 29:12625-12635(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, COILED-COIL REGION, SIGNAL SEQUENCE CLEAVAGE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK053760 mRNA. Translation: BAC35510.1.
AK082275 mRNA. Translation: BAC38452.1.
AK149334 mRNA. Translation: BAE28817.1.
BC059258 mRNA. Translation: AAH59258.1.
RefSeqNP_001033713.1. NM_001038624.1.
NP_848895.2. NM_178780.3.
XP_006508005.1. XM_006507942.1.
XP_006508006.1. XM_006507943.1.
UniGeneMm.71007.

3D structure databases

ProteinModelPortalQ8BPM6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000056990.

PTM databases

PhosphoSiteQ8BPM6.

Proteomic databases

PRIDEQ8BPM6.

Protocols and materials databases

DNASU320360.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000055993; ENSMUSP00000056990; ENSMUSG00000048330. [Q8BPM6-1]
GeneID320360.
KEGGmmu:320360.
UCSCuc009jdg.1. mouse. [Q8BPM6-1]
uc009jdi.1. mouse. [Q8BPM6-3]

Organism-specific databases

CTD79608.
MGIMGI:2443887. Ric3.

Phylogenomic databases

eggNOGNOG46432.
GeneTreeENSGT00440000034107.
HOGENOMHOG000034648.
HOVERGENHBG106009.
InParanoidQ8BPM6.
OMAHRKITNF.
OrthoDBEOG7MKW7H.
PhylomeDBQ8BPM6.
TreeFamTF333291.

Gene expression databases

BgeeQ8BPM6.
GenevestigatorQ8BPM6.

Family and domain databases

InterProIPR026160. Ric3.
[Graphical view]
PANTHERPTHR21723. PTHR21723. 1 hit.
ProtoNetSearch...

Other

NextBio396576.
PROQ8BPM6.
SOURCESearch...

Entry information

Entry nameRIC3_MOUSE
AccessionPrimary (citable) accession number: Q8BPM6
Secondary accession number(s): Q6PCM7, Q8C4G2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 78 of the entry and version 2 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