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RHBG_CANLF
ID   RHBG_CANLF              Reviewed;         458 AA.
AC   Q4VUI0; Q8HYQ5; Q8HYQ6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ammonium transporter Rh type B;
DE   AltName: Full=Rhesus blood group family type B glycoprotein;
DE            Short=Rh family type B glycoprotein;
DE            Short=Rh type B glycoprotein;
GN   Name=RHBG;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney;
RX   PubMed=16227429; DOI=10.1073/pnas.0507886102;
RA   Huang C.-H., Peng J.;
RT   "Evolutionary conservation and diversification of Rh family genes and
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:15512-15517(2005).
CC   -!- FUNCTION: Functions as a specific ammonium transporter. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with ANK2 and ANK3; required for
CC       targeting to the basolateral membrane. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q4VUI0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4VUI0-2; Sequence=VSP_024339;
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN76726.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY622224; AAV40851.1; -; mRNA.
DR   EMBL; AF447922; AAN76725.1; -; mRNA.
DR   EMBL; AF447923; AAN76726.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001003017.2; NM_001003017.2. [Q4VUI0-1]
DR   AlphaFoldDB; Q4VUI0; -.
DR   SMR; Q4VUI0; -.
DR   STRING; 9612.ENSCAFP00000033031; -.
DR   Ensembl; ENSCAFT00030002003; ENSCAFP00030001775; ENSCAFG00030001157. [Q4VUI0-2]
DR   Ensembl; ENSCAFT00030002016; ENSCAFP00030001785; ENSCAFG00030001157. [Q4VUI0-1]
DR   Ensembl; ENSCAFT00040037227; ENSCAFP00040032431; ENSCAFG00040020141. [Q4VUI0-2]
DR   Ensembl; ENSCAFT00845016469; ENSCAFP00845012807; ENSCAFG00845009336. [Q4VUI0-2]
DR   Ensembl; ENSCAFT00845016511; ENSCAFP00845012842; ENSCAFG00845009336. [Q4VUI0-1]
DR   GeneID; 403538; -.
DR   KEGG; cfa:403538; -.
DR   CTD; 57127; -.
DR   VEuPathDB; HostDB:ENSCAFG00845009336; -.
DR   eggNOG; KOG3796; Eukaryota.
DR   GeneTree; ENSGT00950000182844; -.
DR   HOGENOM; CLU_021386_0_0_1; -.
DR   InParanoid; Q4VUI0; -.
DR   OMA; IFVRYNH; -.
DR   OrthoDB; 910733at2759; -.
DR   Reactome; R-CFA-444411; Rhesus glycoproteins mediate ammonium transport.
DR   Proteomes; UP000002254; Chromosome 7.
DR   Bgee; ENSCAFG00000016811; Expressed in testis and 46 other tissues.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0014731; C:spectrin-associated cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR   GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR   GO; GO:0072488; P:ammonium transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0070634; P:transepithelial ammonium transport; IEA:Ensembl.
DR   Gene3D; 1.10.3430.10; -; 1.
DR   InterPro; IPR029020; Ammonium/urea_transptr.
DR   InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR   InterPro; IPR002229; RhesusRHD.
DR   Pfam; PF00909; Ammonium_transp; 1.
DR   PRINTS; PR00342; RHESUSRHD.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Ammonia transport; Cell membrane;
KW   Cytoplasmic vesicle; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..458
FT                   /note="Ammonium transporter Rh type B"
FT                   /id="PRO_0000283595"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..61
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..179
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..219
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        274..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..306
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..393
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        415..458
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          416..424
FT                   /note="Interaction with ANK3"
FT                   /evidence="ECO:0000250"
FT   MOTIF           429..432
FT                   /note="Basolateral sorting signal"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..63
FT                   /note="MARSPRRAGAPRLQLPLLCLLLQGATAILFAVFVRYNHETDAALWHWGNHSN
FT                   LDNEFYFRYPS -> MEQHASHPNEKAKEESNAVPLCRAKPSPSFINLQASSPPATFLN
FT                   IQRTKLPSG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16227429"
FT                   /id="VSP_024339"
SQ   SEQUENCE   458 AA;  49523 MW;  F966A0DDE22774CA CRC64;
     MARSPRRAGA PRLQLPLLCL LLQGATAILF AVFVRYNHET DAALWHWGNH SNLDNEFYFR
     YPSFQDVHVM VFVGFGFLMA FLQRYGFSSV GFTFLLAAFA LQWSTLIQGF FHSLHGGYIH
     VSVNSMINAD FCAGAVLISF GAILGKTGPA QLLLMTVLEV ALFGINEFVL LNLLQVKDAG
     GSMTIHTFGA YFGLVLSRVL YRPQLEKSKH RQCSVYHSDL FAMIGTIFLW IFWPSFNSAP
     TTLGDGQHRT ALNTYYSLSA STLGTFAMSA LVGERGRLDM VHIQNAALAG GVVVGTAGEM
     MLTPFGALAA GFLAGTVSTL GYKFFTPILE AKFKVQDTCG VHNLHGIPGV LGALLGVLVV
     GLATHEAYGE GLGSVFPLIA KGQRTAMSQA MYQLFGLFVT LMFASVGGAL GGLLLKLPCL
     GSPADCQCYE DQVYWEVPGE HEDAAQGPLK AEEPDTQA
 
 
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