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Q8BMN3

- ACHB3_MOUSE

UniProt

Q8BMN3 - ACHB3_MOUSE

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Protein

Neuronal acetylcholine receptor subunit beta-3

Gene

Chrnb3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.By similarity

GO - Molecular functioni

  1. acetylcholine-activated cation-selective channel activity Source: InterPro
  2. acetylcholine binding Source: Ensembl
  3. drug binding Source: Ensembl

GO - Biological processi

  1. protein heterooligomerization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198583. Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
REACT_198585. Highly calcium permeable nicotinic acetylcholine receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuronal acetylcholine receptor subunit beta-3
Gene namesi
Name:Chrnb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:106212. Chrnb3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 238208ExtracellularSequence AnalysisAdd
BLAST
Transmembranei239 – 26325HelicalSequence AnalysisAdd
BLAST
Transmembranei271 – 28818HelicalSequence AnalysisAdd
BLAST
Transmembranei305 – 32622HelicalSequence AnalysisAdd
BLAST
Topological domaini327 – 434108CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei435 – 45319HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. acetylcholine-gated channel complex Source: Ensembl
  2. cell junction Source: UniProtKB-KW
  3. neuron projection Source: Ensembl
  4. postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 464434Neuronal acetylcholine receptor subunit beta-3PRO_0000000384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi159 ↔ 173By similarity
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8BMN3.
PRIDEiQ8BMN3.

PTM databases

PhosphoSiteiQ8BMN3.

Expressioni

Gene expression databases

BgeeiQ8BMN3.
ExpressionAtlasiQ8BMN3. baseline.
GenevestigatoriQ8BMN3.

Interactioni

Subunit structurei

Neuronal AChR seems to be composed of two different types of subunits: alpha and beta.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8BMN3.
SMRiQ8BMN3. Positions 32-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG252943.
GeneTreeiENSGT00760000118930.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiQ8BMN3.
KOiK04814.
OMAiDRYSFPD.
OrthoDBiEOG72JWGV.
PhylomeDBiQ8BMN3.
TreeFamiTF315605.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 2 hits.
[Graphical view]
PRINTSiPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BMN3-1) [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
MTGFLRVFLA LSATLSGSWV TLTATAGLSS VAEHEDALLR HLFQGYQKCV
60 70 80 90 100
RPVLNSSDII KVYFGLKISQ LVDVDEKNQL MTTNVWLKQE WTDQKLRWNP
110 120 130 140 150
EDYGGINSIK VPSESLWLPD IVLFENADGR FEGSLMTKAI VKSSGTVSWT
160 170 180 190 200
PPASYKSSCT MDVTFFPFDK QNCSMKFGSW TYDGTMVDLI LINENVDRKD
210 220 230 240 250
FFDNGEWEIL NAKGMKGNRR EGFYSYPFVT YSFVLRRLPL FYTLFLIIPC
260 270 280 290 300
LGLSFLTVLV FYLPSDEGEK LSLSTSVLVS LTVFLLVIEE IIPSSSKVIP
310 320 330 340 350
LIGEYLLFIM IFVTLSIIVT VFVINVHHRS SSTYHPMAPW VKRLFLEKLP
360 370 380 390 400
RWLCMKDPRD RFSFPDGTES KGTVRGKFPG KKKQTPTSDG ERVLVAFLEK
410 420 430 440 450
ASESIRYISR HVKKEHFISQ VVQDWKFVAQ VLDRIFLWLF LTASVLGSVL
460
IFIPALKMWI HRFH
Length:464
Mass (Da):53,112
Last modified:March 1, 2003 - v1
Checksum:i2ECEA3E0DAF2D5EB
GO
Isoform 2 (identifier: Q8BMN3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-89: Missing.

Note: No experimental confirmation available.

Show »
Length:449
Mass (Da):51,282
Checksum:iFF54824C5DAAC8E7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701K → R in AAL75573. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei75 – 8915Missing in isoform 2. 1 PublicationVSP_013775Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF467896 mRNA. Translation: AAL75573.1.
AY574268 mRNA. Translation: AAS90364.1.
AK017571 mRNA. Translation: BAB30812.1.
AK030464 mRNA. Translation: BAC26973.1.
BC058193 mRNA. Translation: AAH58193.1.
CCDSiCCDS22216.1. [Q8BMN3-2]
CCDS22217.1. [Q8BMN3-1]
RefSeqiNP_081730.1. NM_027454.4. [Q8BMN3-2]
NP_775304.1. NM_173212.4. [Q8BMN3-1]
UniGeneiMm.110444.

Genome annotation databases

EnsembliENSMUST00000060943; ENSMUSP00000052297; ENSMUSG00000031492. [Q8BMN3-1]
ENSMUST00000079463; ENSMUSP00000078428; ENSMUSG00000031492. [Q8BMN3-2]
GeneIDi108043.
KEGGimmu:108043.
UCSCiuc009lit.2. mouse. [Q8BMN3-1]
uc009liu.2. mouse. [Q8BMN3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF467896 mRNA. Translation: AAL75573.1 .
AY574268 mRNA. Translation: AAS90364.1 .
AK017571 mRNA. Translation: BAB30812.1 .
AK030464 mRNA. Translation: BAC26973.1 .
BC058193 mRNA. Translation: AAH58193.1 .
CCDSi CCDS22216.1. [Q8BMN3-2 ]
CCDS22217.1. [Q8BMN3-1 ]
RefSeqi NP_081730.1. NM_027454.4. [Q8BMN3-2 ]
NP_775304.1. NM_173212.4. [Q8BMN3-1 ]
UniGenei Mm.110444.

3D structure databases

ProteinModelPortali Q8BMN3.
SMRi Q8BMN3. Positions 32-459.
ModBasei Search...
MobiDBi Search...

Chemistry

GuidetoPHARMACOLOGYi 473.

PTM databases

PhosphoSitei Q8BMN3.

Proteomic databases

PaxDbi Q8BMN3.
PRIDEi Q8BMN3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000060943 ; ENSMUSP00000052297 ; ENSMUSG00000031492 . [Q8BMN3-1 ]
ENSMUST00000079463 ; ENSMUSP00000078428 ; ENSMUSG00000031492 . [Q8BMN3-2 ]
GeneIDi 108043.
KEGGi mmu:108043.
UCSCi uc009lit.2. mouse. [Q8BMN3-1 ]
uc009liu.2. mouse. [Q8BMN3-2 ]

Organism-specific databases

CTDi 1142.
MGIi MGI:106212. Chrnb3.

Phylogenomic databases

eggNOGi NOG252943.
GeneTreei ENSGT00760000118930.
HOGENOMi HOG000006756.
HOVERGENi HBG003756.
InParanoidi Q8BMN3.
KOi K04814.
OMAi DRYSFPD.
OrthoDBi EOG72JWGV.
PhylomeDBi Q8BMN3.
TreeFami TF315605.

Enzyme and pathway databases

Reactomei REACT_198583. Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
REACT_198585. Highly calcium permeable nicotinic acetylcholine receptors.

Miscellaneous databases

NextBioi 359931.
PROi Q8BMN3.
SOURCEi Search...

Gene expression databases

Bgeei Q8BMN3.
ExpressionAtlasi Q8BMN3. baseline.
Genevestigatori Q8BMN3.

Family and domain databases

Gene3Di 1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProi IPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view ]
PANTHERi PTHR18945. PTHR18945. 1 hit.
Pfami PF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 2 hits.
[Graphical view ]
PRINTSi PR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMi SSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsi TIGR00860. LIC. 1 hit.
PROSITEi PS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Stitzel J.A., Lautner M.A., Jimenez M., Bhandarkar S.J., Curtis C.D., Remias J.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Groot-Kormelink P.J.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
    Tissue: Brain.
  3. "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.
    , 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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Pituitary.
  4. "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 1).
    Tissue: Eye.

Entry informationi

Entry nameiACHB3_MOUSE
AccessioniPrimary (citable) accession number: Q8BMN3
Secondary accession number(s): Q8R5H3, Q9CYK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3