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Protein

Ammonium transporter Rh type A

Gene

Rhag

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

Functioni

May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. Involved in ammonia transport across the erythrocyte membrane. Seems to act in monovalent cation transport.By similarity

GO - Molecular functioni

GO - Biological processi

  • ammonium transmembrane transport Source: GO_Central
  • ammonium transport Source: UniProtKB
  • carbon dioxide transport Source: MGI
  • cellular ion homeostasis Source: UniProtKB
  • erythrocyte development Source: MGI
  • multicellular organismal iron ion homeostasis Source: MGI
  • nitrogen utilization Source: GO_Central
  • organic cation transport Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Ammonia transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-MMU-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-MMU-444411. Rhesus glycoproteins mediate ammonium transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Ammonium transporter Rh type A
Alternative name(s):
Erythrocyte membrane glycoprotein Rh50
Rhesus blood group family type A glycoprotein
Short name:
Rh family type A glycoprotein
Short name:
Rh type A glycoprotein
CD_antigen: CD241
Gene namesi
Name:Rhag
Synonyms:Rh50
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1202713. Rhag.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence analysis
Transmembranei5 – 2521HelicalSequence analysisAdd
BLAST
Topological domaini26 – 6136ExtracellularSequence analysisAdd
BLAST
Transmembranei62 – 8221HelicalSequence analysisAdd
BLAST
Topological domaini83 – 864CytoplasmicSequence analysis
Transmembranei87 – 10721HelicalSequence analysisAdd
BLAST
Topological domaini108 – 12114ExtracellularSequence analysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence analysisAdd
BLAST
Topological domaini143 – 1486CytoplasmicSequence analysis
Transmembranei149 – 16921HelicalSequence analysisAdd
BLAST
Topological domaini170 – 1789ExtracellularSequence analysis
Transmembranei179 – 19921HelicalSequence analysisAdd
BLAST
Topological domaini200 – 21819CytoplasmicSequence analysisAdd
BLAST
Transmembranei219 – 23921HelicalSequence analysisAdd
BLAST
Topological domaini240 – 24910ExtracellularSequence analysis
Transmembranei250 – 27021HelicalSequence analysisAdd
BLAST
Topological domaini271 – 2788CytoplasmicSequence analysis
Transmembranei279 – 29618HelicalSequence analysisAdd
BLAST
Topological domaini297 – 3004ExtracellularSequence analysis
Transmembranei301 – 32121HelicalSequence analysisAdd
BLAST
Topological domaini322 – 34221CytoplasmicSequence analysisAdd
BLAST
Transmembranei343 – 36321HelicalSequence analysisAdd
BLAST
Topological domaini364 – 3729ExtracellularSequence analysis
Transmembranei373 – 39321HelicalSequence analysisAdd
BLAST
Topological domaini394 – 43845CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Ammonium transporter Rh type APRO_0000380190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi31 – 311N-linked (GlcNAc...)Sequence analysis
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence analysis
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence analysis
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9QUT0.
PaxDbiQ9QUT0.
PRIDEiQ9QUT0.

PTM databases

PhosphoSiteiQ9QUT0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000023926.
GenevisibleiQ9QUT0. MM.

Interactioni

Subunit structurei

Heterotetramer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9QUT0. 1 interaction.
MINTiMINT-4130470.
STRINGi10090.ENSMUSP00000024721.

Structurei

3D structure databases

ProteinModelPortaliQ9QUT0.
SMRiQ9QUT0. Positions 1-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3796. Eukaryota.
ENOG410XTF8. LUCA.
GeneTreeiENSGT00390000005787.
HOGENOMiHOG000007656.
InParanoidiQ9QUT0.
KOiK06580.
OMAiGHGDHSQ.
OrthoDBiEOG091G06KX.
PhylomeDBiQ9QUT0.
TreeFamiTF314450.

Family and domain databases

Gene3Di1.10.3430.10. 1 hit.
InterProiIPR029020. Ammonium/urea_transptr.
IPR001905. Ammonium_transpt.
IPR024041. NH4_transpt_AmtB-like_dom.
IPR002229. RhesusRHD.
[Graphical view]
PANTHERiPTHR11730. PTHR11730. 1 hit.
PfamiPF00909. Ammonium_transp. 1 hit.
[Graphical view]
PRINTSiPR00342. RHESUSRHD.
SUPFAMiSSF111352. SSF111352. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9QUT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFKFPLMAI SLEVAMIVLF GLFVEYETPQ NASQKNASHQ NASQQGNTSS
60 70 80 90 100
SAKKDQFFQL YPLFQDVHVM IFVGFGFLMT FLKKYGFSGV GFNLFLAALG
110 120 130 140 150
LQWGTIMQGL LHSHGKEFHF GIYNMINADF STATVLISFG AVLGKTSPIQ
160 170 180 190 200
MLIMTILEIA VFAGNEYLVT ELFEASDTGA SMTIHAFGAY FGLAVAGVLY
210 220 230 240 250
RPGLRCEHPN DESVYHSDLF AMIGTLFLWI FWPSFNSAIA DPGDHQYRAI
260 270 280 290 300
VNTYMSLAAC VITAYALSSL VERRGRLDMV HIQNATLAGG VAVGTCADME
310 320 330 340 350
IPLYAAMTIG SIAGIISVLG YKFFSPLLAN KLMIHDTCGV HNLHGLPGVF
360 370 380 390 400
GGLASIVAIS WGMSTASMAM QAAALGSSIG SAIVGGLLTG LILKLPIWNQ
410 420 430
PPDEYCYDDS VSWKVPKFRE LDNRFFQHAN HNHVEHEV
Length:438
Mass (Da):47,837
Last modified:May 1, 2000 - v1
Checksum:i077935143287FF9B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801A → P in BAE25570 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015192 mRNA. Translation: BAA32441.1.
AF065395 mRNA. Translation: AAD13387.1.
AF057526 mRNA. Translation: AAC25155.1.
AK143851 mRNA. Translation: BAE25570.1.
AK157847 mRNA. Translation: BAE34227.1.
CH466559 Genomic DNA. Translation: EDL23386.1.
BC101941 mRNA. Translation: AAI01942.1.
BC101942 mRNA. Translation: AAI01943.1.
BC103512 mRNA. Translation: AAI03513.1.
BC103662 mRNA. Translation: AAI03663.1.
CCDSiCCDS28787.1.
RefSeqiNP_035399.1. NM_011269.2.
UniGeneiMm.12961.

Genome annotation databases

EnsembliENSMUST00000024721; ENSMUSP00000024721; ENSMUSG00000023926.
GeneIDi19743.
KEGGimmu:19743.
UCSCiuc008col.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015192 mRNA. Translation: BAA32441.1.
AF065395 mRNA. Translation: AAD13387.1.
AF057526 mRNA. Translation: AAC25155.1.
AK143851 mRNA. Translation: BAE25570.1.
AK157847 mRNA. Translation: BAE34227.1.
CH466559 Genomic DNA. Translation: EDL23386.1.
BC101941 mRNA. Translation: AAI01942.1.
BC101942 mRNA. Translation: AAI01943.1.
BC103512 mRNA. Translation: AAI03513.1.
BC103662 mRNA. Translation: AAI03663.1.
CCDSiCCDS28787.1.
RefSeqiNP_035399.1. NM_011269.2.
UniGeneiMm.12961.

3D structure databases

ProteinModelPortaliQ9QUT0.
SMRiQ9QUT0. Positions 1-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QUT0. 1 interaction.
MINTiMINT-4130470.
STRINGi10090.ENSMUSP00000024721.

PTM databases

PhosphoSiteiQ9QUT0.

Proteomic databases

MaxQBiQ9QUT0.
PaxDbiQ9QUT0.
PRIDEiQ9QUT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024721; ENSMUSP00000024721; ENSMUSG00000023926.
GeneIDi19743.
KEGGimmu:19743.
UCSCiuc008col.1. mouse.

Organism-specific databases

CTDi6005.
MGIiMGI:1202713. Rhag.

Phylogenomic databases

eggNOGiKOG3796. Eukaryota.
ENOG410XTF8. LUCA.
GeneTreeiENSGT00390000005787.
HOGENOMiHOG000007656.
InParanoidiQ9QUT0.
KOiK06580.
OMAiGHGDHSQ.
OrthoDBiEOG091G06KX.
PhylomeDBiQ9QUT0.
TreeFamiTF314450.

Enzyme and pathway databases

ReactomeiR-MMU-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-MMU-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-MMU-444411. Rhesus glycoproteins mediate ammonium transport.

Miscellaneous databases

PROiQ9QUT0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000023926.
GenevisibleiQ9QUT0. MM.

Family and domain databases

Gene3Di1.10.3430.10. 1 hit.
InterProiIPR029020. Ammonium/urea_transptr.
IPR001905. Ammonium_transpt.
IPR024041. NH4_transpt_AmtB-like_dom.
IPR002229. RhesusRHD.
[Graphical view]
PANTHERiPTHR11730. PTHR11730. 1 hit.
PfamiPF00909. Ammonium_transp. 1 hit.
[Graphical view]
PRINTSiPR00342. RHESUSRHD.
SUPFAMiSSF111352. SSF111352. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRHAG_MOUSE
AccessioniPrimary (citable) accession number: Q9QUT0
Secondary accession number(s): Q3UP27, Q794G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 112 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.