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Q8BUX5 (RHBG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. Feed History...

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

Names and origin

Protein namesRecommended name:
Ammonium transporter Rh type B
Alternative name(s):
Rhesus blood group family type B glycoprotein
Short name=Rh family type B glycoprotein
Short name=Rh type B glycoprotein
Gene names
Name:Rhbg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a specific ammonium transporter. Ref.2 Ref.8

Subunit structure

Interacts (via C-terminus) with ANK2 and ANK3; required for targeting to the basolateral membrane By similarity.

Subcellular location

Basolateral cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein By similarity Ref.5 Ref.6 Ref.7.

Tissue specificity

Expressed in kidney by connecting segments and collecting tubules. Also expressed in liver by perivenous hepatocytes. Expressed in the forestomach and the fundus of the stomach. Expressed in duodenum, jejunum, ileum and colon at the level of villous (at protein level). Specifically expressed in kidney where it is restricted to the epithelial linings of the convoluted tubules and the loop of Henle. Also detected in ovary. Expressed by hepatocytes and dermal hair follicles and papillae. Ref.1 Ref.5 Ref.6 Ref.7

Developmental stage

Detected in embryos at E15 and E17. Expressed in kidney, skin and liver of E16.5 embryos. Ref.1

Post-translational modification

N-glycosylated. Ref.1

Sequence similarities

Belongs to the ammonium transporter (TC 2.A.49) family. Rh subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Ammonium transporter Rh type B
PRO_0000283599

Regions

Topological domain1 – 1010Cytoplasmic Potential
Transmembrane11 – 3121Helical; Potential
Topological domain32 – 5827Extracellular Potential
Transmembrane59 – 7921Helical; Potential
Topological domain80 – 834Cytoplasmic Potential
Transmembrane84 – 10421Helical; Potential
Topological domain105 – 12117Extracellular Potential
Transmembrane122 – 14221Helical; Potential
Topological domain143 – 1464Cytoplasmic Potential
Transmembrane147 – 16721Helical; Potential
Topological domain168 – 1758Extracellular Potential
Transmembrane176 – 19823Helical; Potential
Topological domain199 – 21618Cytoplasmic Potential
Transmembrane217 – 23721Helical; Potential
Topological domain238 – 24811Extracellular Potential
Transmembrane249 – 26921Helical; Potential
Topological domain270 – 27910Cytoplasmic Potential
Transmembrane280 – 30021Helical; Potential
Topological domain3011Extracellular Potential
Transmembrane302 – 32221Helical; Potential
Topological domain323 – 34321Cytoplasmic Potential
Transmembrane344 – 36421Helical; Potential
Topological domain365 – 39026Extracellular Potential
Transmembrane391 – 41121Helical; Potential
Topological domain412 – 45544Cytoplasmic Potential
Region413 – 4219Interaction with ANK3 By similarity

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1951W → R in AAF19371. Ref.1
Sequence conflict1951W → R in AAH29236. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8BUX5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C8D57B88A37089D2

FASTA45549,543
        10         20         30         40         50         60 
MARVPRHRRL VLPLLCLLFQ GATALLFAIF VRYNHETDAA LWHWGNHSNV DNEFYFRYPS 

        70         80         90        100        110        120 
FQDVHVMVFV GFGFLMVFLQ RYGFSSVGFT FLVASLTLQW ATLLQGFLHS FHGGHIHVGV 

       130        140        150        160        170        180 
ESLINADFCA GAVLISFGAV LGKTGPAQLL LMALLEAVLF SVNEFILLSL LGVRDAGGSM 

       190        200        210        220        230        240 
TIHTFGAYFG LFLSWVLYRS QLEKSRHRQS SVYNSDLFAM IGTIFLWVFW PSFNSAPTAL 

       250        260        270        280        290        300 
GDGQHRTVVN TYYSLTASTL STFALSALVS GDGRLDMVHV QNAALAGGVV VGTSSEMMLT 

       310        320        330        340        350        360 
PFGALAAGFL AGTVSTLGYK FFTPILESRF KLQDTCGVHN LHGMPGVLGA ILGVVVAALA 

       370        380        390        400        410        420 
THEAYGDGLQ SVFPLIAKGQ RSATSQAVYQ LFGMFVTLVF ASVGGSLGGL LLRLPFLDSP 

       430        440        450 
PDSQCFEDQV YWEVPGEQET ETQRPLRGGE SDTRA

« Hide

References

« Hide 'large scale' references
[1]"Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals."
Liu Z., Peng J., Mo R., Hui C.-C., Huang C.-H.
J. Biol. Chem. 276:1424-1433(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, GLYCOSYLATION.
Tissue: Liver.
[2]"Characteristics of renal Rhbg as an NH4(+) transporter."
Nakhoul N.L., Dejong H., Abdulnour-Nakhoul S.M., Boulpaep E.L., Hering-Smith K., Hamm L.L.
Am. J. Physiol. 288:F170-F181(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: C3H.
Tissue: Kidney cortex.
[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. 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.
Tissue: Head.
[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].
Strain: FVB/N.
Tissue: Colon.
[5]"Localization of the ammonium transporter proteins RhBG and RhCG in mouse kidney."
Verlander J.W., Miller R.T., Frank A.E., Royaux I.E., Kim Y.-H., Weiner I.D.
Am. J. Physiol. 284:F323-F337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Localization of the ammonium transporters, Rh B glycoprotein and Rh C glycoprotein, in the mouse liver."
Weiner I.D., Miller R.T., Verlander J.W.
Gastroenterology 124:1432-1440(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]"Expression of the ammonia transporter proteins Rh B glycoprotein and Rh C glycoprotein in the intestinal tract."
Handlogten M.E., Hong S.-P., Zhang L., Vander A.W., Steinbaum M.L., Campbell-Thompson M., Weiner I.D.
Am. J. Physiol. 288:G1036-G1047(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Characterization of ammonia transport by the kidney Rh glycoproteins RhBG and RhCG."
Mak D.-O., Dang B., Weiner I.D., Foskett J.K., Westhoff C.M.
Am. J. Physiol. 290:F297-F305(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF193808 mRNA. Translation: AAF19371.1.
AY254685 mRNA. Translation: AAP81167.1.
AK081882 mRNA. Translation: BAC38359.1.
BC029236 mRNA. Translation: AAH29236.1.
IPIIPI00387290.
RefSeqNP_067350.2. NM_021375.3.
UniGeneMm.103777.

3D structure databases

ProteinModelPortalQ8BUX5.
SMRQ8BUX5. Positions 9-435.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000001453.

Proteomic databases

PaxDbQ8BUX5.
PRIDEQ8BUX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000171887; ENSMUSP00000130767; ENSMUSG00000001417.
GeneID58176.
KEGGmmu:58176.
UCSCuc008pui.1. mouse.

Organism-specific databases

CTD57127.
MGIMGI:1927379. Rhbg.

Phylogenomic databases

eggNOGNOG276393.
GeneTreeENSGT00390000005787.
HOGENOMHOG000007656.
HOVERGENHBG004374.
InParanoidQ8BUX5.
KOK06580.
OMADSQCYED.
OrthoDBEOG45DWPJ.

Gene expression databases

ArrayExpressQ8BUX5.
BgeeQ8BUX5.
CleanExMM_RHBG.
GenevestigatorQ8BUX5.

Family and domain databases

InterProIPR024041. NH4_transpt_AmtB-like_dom.
IPR002229. RhesusRHD.
[Graphical view]
PfamPF00909. Ammonium_transp. 1 hit.
[Graphical view]
PRINTSPR00342. RHESUSRHD.
SUPFAMSSF111352. RH_like_transpt. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRHBG. mouse.
NextBio314119.
SOURCESearch...

Entry information

Entry nameRHBG_MOUSE
AccessionPrimary (citable) accession number: Q8BUX5
Secondary accession number(s): Q9QXP1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents