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SCNNA_PANTR
ID   SCNNA_PANTR             Reviewed;         692 AA.
AC   H2Q5A1;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 2.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Amiloride-sensitive sodium channel subunit alpha;
DE   AltName: Full=Alpha-NaCH;
DE   AltName: Full=Epithelial Na(+) channel subunit alpha;
DE            Short=Alpha-ENaC;
DE   AltName: Full=Nonvoltage-gated sodium channel 1 subunit alpha;
DE   AltName: Full=SCNEA;
GN   Name=SCNN1A;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
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 eccrine sweat
CC       glands. Also plays a role in taste perception.
CC       {ECO:0000250|UniProtKB:P37088}.
CC   -!- ACTIVITY REGULATION: Activated by WNK1, WNK2, WNK3 and WNK4.
CC       {ECO:0000250|UniProtKB:Q61180}.
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).
CC       {ECO:0000250|UniProtKB:P37088}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P37089}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P37089}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:P37088}. Cytoplasmic granule
CC       {ECO:0000250|UniProtKB:P37088}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P37088}. Cytoplasmic vesicle, secretory vesicle,
CC       acrosome {ECO:0000250|UniProtKB:P37089}. Cell projection, cilium,
CC       flagellum {ECO:0000250|UniProtKB:P37089}. Note=In the oviduct and
CC       bronchus, located on cilia in multi-ciliated cells. In endometrial non-
CC       ciliated epithelial cells, restricted to apical surfaces. In epidermis,
CC       located nearly uniformly in the cytoplasm in a granular distribution.
CC       In sebaceous glands, observed only in the cytoplasmic space in between
CC       the lipid vesicles. In eccrine sweat glands, mainly located at the
CC       apical surface of the cells facing the lumen. In skin, in arrector pili
CC       muscle cells and in adipocytes, located in the cytoplasm and
CC       colocalized with actin fibers. In spermatogonia, spermatocytes and
CC       round spermatids, located in the cytoplasm. Prior to spermiation,
CC       location shifts from the cytoplasm to the spermatid tail. In
CC       spermatozoa, localizes at the acrosome and the central region of the
CC       sperm flagellum. {ECO:0000250|UniProtKB:P37088,
CC       ECO:0000250|UniProtKB:P37089}.
CC   -!- PTM: Ubiquitinated; this targets individual subunits for endocytosis
CC       and proteasome-mediated degradation. {ECO:0000250|UniProtKB:P37089}.
CC   -!- PTM: ENaC cleavage by furin, and subsequently by prostasin (PRSS8),
CC       leads to a stepwise increase in the open probability of the channel as
CC       a result of release of the alpha and gamma subunit inhibitory tracts,
CC       respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects
CC       ENaC against proteolytic activation. {ECO:0000250|UniProtKB:P37088}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P37089}.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC       1.A.6) family. SCNN1A subfamily. {ECO:0000305}.
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DR   EMBL; AACZ03089625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ03089626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ03089627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ03089628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ03089629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ03089630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H2Q5A1; -.
DR   SMR; H2Q5A1; -.
DR   STRING; 9598.ENSPTRP00000007816; -.
DR   PaxDb; H2Q5A1; -.
DR   Ensembl; ENSPTRT00000097030; ENSPTRP00000064198; ENSPTRG00000004571.
DR   VGNC; VGNC:13442; SCNN1A.
DR   eggNOG; KOG4294; Eukaryota.
DR   GeneTree; ENSGT00940000160952; -.
DR   InParanoid; H2Q5A1; -.
DR   OMA; EKTRQCK; -.
DR   Proteomes; UP000002277; Chromosome 12.
DR   Bgee; ENSPTRG00000004571; Expressed in cortex of kidney and 13 other tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0034706; C:sodium channel complex; IBA:GO_Central.
DR   GO; GO:0097228; C:sperm principal piece; ISS:UniProtKB.
DR   GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR   GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
DR   GO; GO:0071468; P:cellular response to acidic pH; IEA:Ensembl.
DR   GO; GO:0036254; P:cellular response to amiloride; IEA:Ensembl.
DR   GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0050891; P:multicellular organismal water homeostasis; IEA:Ensembl.
DR   GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
DR   GO; GO:0098719; P:sodium ion import across plasma membrane; IEA:Ensembl.
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   3: Inferred from homology;
KW   Cell membrane; Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle;
KW   Flagellum; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Sensory transduction; Sodium; Sodium channel;
KW   Sodium transport; Taste; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..692
FT                   /note="Amiloride-sensitive sodium channel subunit alpha"
FT                   /id="PRO_0000432714"
FT   TOPO_DOM        1..108
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   TRANSMEM        109..129
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..585
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   TRANSMEM        586..606
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        607..692
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..671
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   692 AA;  78073 MW;  7AF35B9A527FB9D4 CRC64;
     MSSIKGNKLE EQGPRPLQPT PGLMEGNKLE EQDSSPPQST PGLMKGDKRE EQGLGPEPAA
     PQQPTAEEEA LIEFHRSYRE LFEFFCNNTT IHGAIRLVCS QHNRMKTAFW AVLWLCTFGM
     MYWQFGLLFG EYFSYPVSLN INLNSDKLVF PAVTICTLNP YRYPEIKEEL EELDRITEQT
     LFDLYKYSSF TTLVAGSRSR RDLRGTLPHP LQRLRVPPPP HGARRARSVA SSVRDNNPQV
     DWKDWKIGFQ LCNQNKSDCF YQTYSSGVDA VREWYRFHYI NILSRLPETL PSLEKDTLGN
     FIFACRFNQV SCNQANYSHF HHPMYGNCYT FNDKNNSNLW MSSMPGINNG LSLMLRAEQN
     DFIPLLSTVT GARVMVHGQD EPAFMDDGGF NLRPGVETSI SMRKETLDRL GGDYGDCTKN
     GSDVPVENLY PSKYTQQVCI HSCFQESMIK ECGCAYIFYP RPQNVEYCDY RKHSSWGYCY
     YKLQVDFSSD HLGCFTKCRK PCSVTSYQLS AGYSRWPSVT SQEWVFQMLS RQNNYTVNNK
     RNGVAKVNIF FKELNYKTNS ESPSVTMVTL LSNLGSQWSL WFGSSVLSVV EMAELIFDLL
     VITFLMLLRR FRSRYWSPGR GGRGAQEVAS TLASSPPSHF CPHPTSLSLS QPGPAPSPAL
     TAPPPAYATL GPRPSPGGST GAGSSACPLG GP
 
 
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