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