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FANA_CORAP
ID   FANA_CORAP              Reviewed;         625 AA.
AC   Q25011;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=FMRFamide-activated amiloride-sensitive sodium channel;
DE   AltName: Full=FANACH;
OS   Cornu aspersum (Brown garden snail) (Helix aspersa).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC   Helicina; Helicoidea; Helicidae; Cornu; Cornu.
OX   NCBI_TaxID=6535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Nerve;
RX   PubMed=7501021; DOI=10.1038/378730a0;
RA   Lingueglia E., Champigny G., Lazdunski M., Barbry P.;
RT   "Cloning of the amiloride-sensitive FMRFamide peptide-gated sodium
RT   channel.";
RL   Nature 378:730-733(1995).
CC   -!- FUNCTION: FMRFamide-gated ionotropic receptor.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Muscle and nervous tissue.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC       1.A.6) family. {ECO:0000305}.
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DR   EMBL; X92113; CAA63084.1; -; mRNA.
DR   PIR; S68434; S68434.
DR   AlphaFoldDB; Q25011; -.
DR   TCDB; 1.A.6.3.1; the epithelial na(+) channel (enac) family.
DR   PRIDE; Q25011; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001873; ENaC.
DR   InterPro; IPR020903; ENaC_CS.
DR   PANTHER; PTHR11690; PTHR11690; 2.
DR   Pfam; PF00858; ASC; 1.
DR   PRINTS; PR01078; AMINACHANNEL.
DR   PROSITE; PS01206; ASC; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..625
FT                   /note="FMRFamide-activated amiloride-sensitive sodium
FT                   channel"
FT                   /id="PRO_0000181312"
FT   TOPO_DOM        1..67
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..536
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        537..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        558..625
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          570..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   625 AA;  71351 MW;  CF2F7409C45BB2A6 CRC64;
     MKYTSAATKP GVFPEHHQHA MMRNRYHPHH CNYSDNRSAI DIIAELGSES NAHGLAKIVT
     SRDTKRKVIW ALLVIAGFTA ATLQLSLLVR KYLQFQVVEL SEIKDSMPVQ YPSVSICNIE
     PISLRTIRRM YFNNESQNLI TWLRFIQKFR FEQDSFMNSI RAFYENLGQD AKKLSHNLED
     MLMHCRFNRE LCHVSNFSTF FDGNYFNCFT FNSGQRLQMH ATGPENGLSL IFSVEKDDPL
     PGTYGVYNFD NNILHSAGVR VVVHAPGSMP SPVDHGIDIP PGYSSSVGLK AILHTRLPYP
     YGNCTNDMLN GIKQYKYTFF ACLQLCKQRL IIQRCGCKSS ALPEVPSYNA TFCGVIKDWQ
     EINRNHSNED HNQSEEDRAF IPTPYLACEE REQKNLNNDR TYELSCGCFQ PCSETSYLKS
     VSLSYWPLEF YQLSAVERFF KQERQAGQNH FMKTAYEYLE KLAHPSQKHL ARNDSHMDDI
     LSKSYSLSEK EMAKEASDLI RQNMLRLNIY LEDLSVVEYR QLPAYGLADL FADIGGTLGL
     WMGISVLTIM ELIELVIRLT GLVFNSEKGL PRGPTTVNNN NGSNNHSQST SQHQLYNGYM
     DHDSHYSDSA GASVFDFRRG VESPV
 
 
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