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RHBG_TAKRU
ID   RHBG_TAKRU              Reviewed;         458 AA.
AC   Q18PF6; Q7T3R6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Ammonium transporter Rh type B;
DE   AltName: Full=FRhbg;
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   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=17218543; DOI=10.1096/fj.06-6834com;
RA   Nakada T., Westhoff C.M., Kato A., Hirose S.;
RT   "Ammonia secretion from fish gill depends on a set of Rh glycoproteins.";
RL   FASEB J. 21:1067-1074(2007).
CC   -!- FUNCTION: Functions as an ammonia transporter. May play a role in the
CC       elimination of ammonia in the gill. {ECO:0000269|PubMed:17218543}.
CC   -!- SUBCELLULAR LOCATION: Apicolateral cell membrane
CC       {ECO:0000269|PubMed:17218543}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:17218543}. 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=Q18PF6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q18PF6-2; Sequence=VSP_024344;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the gill by pavement
CC       cells (at protein level). {ECO:0000269|PubMed:17218543}.
CC   -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM48577.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY116074; AAM48577.1; ALT_FRAME; mRNA.
DR   EMBL; AB218980; BAE96342.1; -; mRNA.
DR   RefSeq; NP_001027818.1; NM_001032646.1.
DR   RefSeq; XP_011617146.1; XM_011618844.1. [Q18PF6-1]
DR   RefSeq; XP_011617147.1; XM_011618845.1. [Q18PF6-2]
DR   AlphaFoldDB; Q18PF6; -.
DR   SMR; Q18PF6; -.
DR   STRING; 31033.ENSTRUP00000012961; -.
DR   GeneID; 445989; -.
DR   KEGG; tru:445989; -.
DR   CTD; 57127; -.
DR   eggNOG; KOG3796; Eukaryota.
DR   HOGENOM; CLU_021386_0_0_1; -.
DR   InParanoid; Q18PF6; -.
DR   OrthoDB; 910733at2759; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0016327; C:apicolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0008519; F:ammonium transmembrane transporter activity; IEA:InterPro.
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   1: Evidence at protein 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_0000283607"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..58
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..83
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..121
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..216
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..247
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..298
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        320..340
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        362..391
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        413..458
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          436..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         409..415
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16227429"
FT                   /id="VSP_024344"
SQ   SEQUENCE   458 AA;  49664 MW;  342C46E6813B7A24 CRC64;
     MTDAATNMRL KLPITCFILE IILIILFGTL VQYDYETDAK EWHNTSHQDY ENDFYFRYPS
     FQDVHVMIFV GFGFLMTFLQ RYGFGSVGFN FLIAAFSLQW ATLMQGFFHG MHGGKIHIGV
     ESMINADFCT GSVLISFGAV LGKTSPIQLL TMAIFEVTLF AVNEFILLSL LGTKDAGGSM
     TIHTFGAYFG LMVTRILYRP NLDKSKHRNS SVYHSDLFAM IGTVYLWMFW PSFNSAITAH
     GDDQHRTALN TYYSLAACTL ATYGMSAITS HDGKLDMVHI QNAALAGGVA VGTAGEMMLT
     PFGSMIVGFM AGIISVLGFK FLSPILEDKL KIQDTCGIHN LHGMPGVLGA IVGAVTAALA
     TTDVYGQGMA DVFPAVADGS VNATKQGGIQ ALSLAITLGI AVLGGLIVGF VLKLPVFGTP
     PDTLCFEDSV YWEVPGSESP EEGELTSVKP EETEHLNS
 
 
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