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SCNNB_RABIT
ID   SCNNB_RABIT             Reviewed;         641 AA.
AC   O97742; Q9N132;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Amiloride-sensitive sodium channel subunit beta;
DE   AltName: Full=Beta-NaCH;
DE   AltName: Full=Epithelial Na(+) channel subunit beta;
DE            Short=Beta-ENaC;
DE   AltName: Full=Nonvoltage-gated sodium channel 1 subunit beta;
DE   AltName: Full=SCNEB;
GN   Name=SCNN1B;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kudlacek O., Weisz E., Wiener H., Plass H.;
RT   "The rabbit epithelial sodium channel.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 275-456.
RA   Velazquez H., Silva T.C., Andujar E., Jaffer A., Ortiz D.;
RT   "The rabbit DCT does not express amiloride sensitive sodium channel.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited
CC       by the diuretic amiloride. Mediates the electrodiffusion of the luminal
CC       sodium (and water, which follows osmotically) through the apical
CC       membrane of epithelial cells. Plays an essential role in electrolyte
CC       and blood pressure homeostasis, but also in airway surface liquid
CC       homeostasis, which is important for proper clearance of mucus. Controls
CC       the reabsorption of sodium in kidney, colon, lung and sweat glands.
CC       Also plays a role in taste perception. {ECO:0000250|UniProtKB:P51168}.
CC   -!- ACTIVITY REGULATION: Activated by WNK1, WNK2, WNK3 and WNK4.
CC       {ECO:0000250|UniProtKB:Q9WU38}.
CC   -!- SUBUNIT: Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B and a
CC       gamma/SCNN1G subunit. An additional delta/SCNN1D subunit exists only in
CC       some organisms and can replace the alpha/SCNN1A subunit to form an
CC       alternative channel with specific properties. Interacts with NEDD4 (via
CC       WW domains). Interacts with NEDD4L (via WW domains). Interacts with
CC       WWP1 (via WW domains). Interacts with WWP2 (via WW domains). Interacts
CC       with the full-length immature form of PCSK9 (pro-PCSK9). Interacts (N-
CC       glycosylated) with BPIFA1; the interaction is direct and inhibits the
CC       proteolytic processing of SCNN1A and SCNN1G and the activation of ENaC.
CC       {ECO:0000250|UniProtKB:P51168}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P37090}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P37089}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:P37090}. Note=Apical membrane of epithelial
CC       cells. {ECO:0000250|UniProtKB:P37090}.
CC   -!- PTM: Phosphorylated on serine and threonine residues. Aldosterone and
CC       insulin increase the basal level of phosphorylation.
CC       {ECO:0000250|UniProtKB:P37090}.
CC   -!- PTM: N-glycosylated. N-glycosylation is required for interaction with
CC       BPIFA1. {ECO:0000250|UniProtKB:P51168}.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC       1.A.6) family. SCNN1B subfamily. {ECO:0000305}.
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DR   EMBL; AJ132109; CAA10572.1; -; mRNA.
DR   EMBL; AF229026; AAF43681.1; -; mRNA.
DR   RefSeq; NP_001076244.1; NM_001082775.1.
DR   AlphaFoldDB; O97742; -.
DR   BMRB; O97742; -.
DR   SMR; O97742; -.
DR   STRING; 9986.ENSOCUP00000007259; -.
DR   GeneID; 100009564; -.
DR   KEGG; ocu:100009564; -.
DR   CTD; 6338; -.
DR   eggNOG; KOG4294; Eukaryota.
DR   InParanoid; O97742; -.
DR   OrthoDB; 686369at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0034706; C:sodium channel complex; ISS:UniProtKB.
DR   GO; GO:0015280; F:ligand-gated sodium channel activity; IEA:InterPro.
DR   GO; GO:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
DR   GO; GO:0055078; P:sodium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
DR   InterPro; IPR001873; ENaC.
DR   InterPro; IPR004724; ENaC_chordates.
DR   InterPro; IPR020903; ENaC_CS.
DR   PANTHER; PTHR11690; PTHR11690; 1.
DR   Pfam; PF00858; ASC; 1.
DR   PRINTS; PR01078; AMINACHANNEL.
DR   TIGRFAMs; TIGR00859; ENaC; 1.
DR   PROSITE; PS01206; ASC; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasmic vesicle; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW   Sensory transduction; Sodium; Sodium channel; Sodium transport; Taste;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..641
FT                   /note="Amiloride-sensitive sodium channel subunit beta"
FT                   /id="PRO_0000181270"
FT   TOPO_DOM        1..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   TRANSMEM        51..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..533
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   TRANSMEM        534..554
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        555..641
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   REGION          596..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         634
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WU38"
FT   MOD_RES         636
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WU38"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        275
FT                   /note="V -> I (in Ref. 2; AAF43681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        389
FT                   /note="H -> R (in Ref. 2; AAF43681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        415
FT                   /note="Y -> H (in Ref. 2; AAF43681)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   641 AA;  71973 MW;  1FBE6181B232AD06 CRC64;
     MHVKKYLLKC LHRLQKGPGY TYKELLVWYC DNTNTHGPKR IIREGPKKKA MWFLITLLFA
     SLVCWQWGVF IKTYLSWEVS VSLSMGFKAM DFPAVTICNA SPFRYSKVRH LLKDLDELME
     AVLARILAPE SSQANATAAM NLSMWNYTPL VLIDERDPHH PVVLDLFAND PTGSASSSPG
     PRGACNAQGC KVAMRLCSLN GTSCTFRNFS SATQAVTEWY ALQATNIFSQ VPQRELVELG
     YSAERLILAC LFGAEPCSYR NFTSIFYPDY GNCYVFNWGM TEKALPSANP GTEFGLKLIL
     DIGQEDYVPF LASTAGVRLM LHEQRSYPFI REEGVDAMSG TETSIGVLVD KLQRKGEPYS
     PCTVNGSDVP VQNLYGSYNT TYSIQACLHS CFQTQMIASC QCGHYLYPLP RGQEYCNSRD
     FPDWAPCYLA LRMSEAERET CIRMCKESCN DTQYKMTISM ADWPSEASED WIFHVLSQER
     DQSTNVTLSR KGVVKLNIYF QEFNYRTIEE SAANNIVWLL SNLGGQFGFW MGGSVLCLIE
     FAEIIIDFVW ITIIKLVALA KGLRQRQAQA RYAGPPPTVA ELVEAHTNFG FQPDVGHRSP
     DAEAYPDEQA LPIPGTPPPN YDSLRLQPLD VVESDSEGDA V
 
 
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