U.S. flag

An official website of the United States government

RecName: Full=Ligand-gated cation channel ZACN; AltName: Full=Ligand-gated ion channel zinc-activated 1; AltName: Full=Ligand-gated ion-channel receptor L2; AltName: Full=Zinc-activated channel; Flags: Precursor

UniProtKB/Swiss-Prot: Q401N2.2

Identical Proteins FASTA Graphics 

LOCUS       ZACN_HUMAN               412 aa            linear   PRI 27-NOV-2024
DEFINITION  RecName: Full=Ligand-gated cation channel ZACN; AltName:
            Full=Ligand-gated ion channel zinc-activated 1; AltName:
            Full=Ligand-gated ion-channel receptor L2; AltName:
            Full=Zinc-activated channel; Flags: Precursor.
ACCESSION   Q401N2
VERSION     Q401N2.2
DBSOURCE    UniProtKB: locus ZACN_HUMAN, accession Q401N2;
            class: standard.
            extra accessions:Q2TB29,Q6ZWK3,Q86YW4
            created: Feb 5, 2008.
            sequence updated: Feb 5, 2008.
            annotation updated: Nov 27, 2024.
            xrefs: AF512521.1, AAO20969.1, AB223030.1, BAE19924.1, AK122638.1,
            AC018665.9, CH471099.1, EAW89365.1, EAW89366.1, BC110596.1,
            BC110597.1, AAI10598.1, NP_851321.2
            xrefs (non-sequence databases): CCDS:CCDS11740.2,
            AlphaFoldDB:Q401N2, SMR:Q401N2, BioGRID:131658, IntAct:Q401N2,
            STRING:9606.ENSP00000334854, DrugCentral:Q401N2,
            GuidetoPHARMACOLOGY:587, TCDB:1.A.9.2.4, GlyCosmos:Q401N2,
            GlyGen:Q401N2, iPTMnet:Q401N2, BioMuta:ZACN, DMDM:166991030,
            MassIVE:Q401N2, PaxDb:9606-ENSP00000334854, PeptideAtlas:Q401N2,
            ProteomicsDB:61925, ProteomicsDB:61926, TopDownProteomics:Q401N2-3,
            Antibodypedia:46125, DNASU:353174, Ensembl:ENST00000334586.10,
            Ensembl:ENSP00000334854.5, Ensembl:ENSG00000186919.13,
            Ensembl:ENST00000421794.1, Ensembl:ENSP00000391936.1,
            Ensembl:ENST00000425015.5, Ensembl:ENSP00000397489.1,
            GeneID:353174, KEGG:hsa:353174, MANE-Select:ENST00000334586.10,
            UCSC:uc002jqn.3, AGR:HGNC:29504, CTD:353174, DisGeNET:353174,
            GeneCards:ZACN, HGNC:29504, HPA:ENSG00000186919, MIM 610935,
            neXtProt:NX_Q401N2, OpenTargets:ENSG00000186919,
            PharmGKB:PA162409377, VEuPathDB:HostDB:ENSG00000186919,
            eggNOG:KOG3645, GeneTree:ENSGT00920000149199,
            HOGENOM:CLU_672608_0_0_1, InParanoid:Q401N2, OMA:TWPLVHG,
            OrthoDB:4630813at2759, PhylomeDB:Q401N2, TreeFam:TF315605,
            PathwayCommons:Q401N2, SignaLink:Q401N2, BioGRID-ORCS:353174,
            ChiTaRS:ZACN, GeneWiki:Zinc-activated_ion_channel,
            GenomeRNAi:353174, Pharos:Q401N2, PRO:PR:Q401N2,
            Proteomes:UP000005640, RNAct:Q401N2, Bgee:ENSG00000186919,
            GO:0005886, GO:1902495, GO:0005230, GO:0099094, GO:0015276,
            GO:0160128, GO:0004888, GO:0008270, GO:0034220, GO:0010043,
            CDD:cd18994, FunFam:1.20.58.390:FF:000068,
            FunFam:2.70.170.10:FF:000037, Gene3D:2.70.170.10,
            Gene3D:1.20.58.390, InterPro:IPR006202, InterPro:IPR036734,
            InterPro:IPR006201, InterPro:IPR036719, InterPro:IPR038050,
            InterPro:IPR018000, PANTHER:PTHR18945, PANTHER:PTHR18945:SF912,
            Pfam:PF02931, SUPFAM:SSF90112, SUPFAM:SSF63712, PROSITE:PS00236
KEYWORDS    Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
            Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
            Receptor; Reference proteome; Signal; Transmembrane; Transmembrane
            helix; Transport; Zinc.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Davies,P.A., Wang,W., Hales,T.G. and Kirkness,E.F.
  TITLE     A novel class of ligand-gated ion channel is activated by Zn2+
  JOURNAL   J Biol Chem 278 (2), 712-717 (2003)
   PUBMED   12381728
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE
            SPECIFICITY, AND VARIANT THR-152.
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Houtani,T., Munemoto,Y., Kase,M., Sakuma,S., Tsutsumi,T. and
            Sugimoto,T.
  TITLE     Cloning and expression of ligand-gated ion-channel receptor L2 in
            central nervous system
  JOURNAL   Biochem Biophys Res Commun 335 (2), 277-285 (2005)
   PUBMED   16083862
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
            TISSUE SPECIFICITY, AND GLYCOSYLATION.;
            TISSUE=Brain
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
            Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
            Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
            Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
            Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
            Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
            Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
            Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
            Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
            Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
            Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
            Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
            Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
            Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
            Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
            Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
            Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
            Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
            Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
            Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
            Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
            Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
            Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
            Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
            Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
            Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
            Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
            Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
            Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
            THR-152.;
            TISSUE=Thymus
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Mural,R.J., Istrail,S., Sutton,G.G., Florea,L., Halpern,A.L.,
            Mobarry,C.M., Lippert,R., Walenz,B., Shatkay,H., Dew,I.,
            Miller,J.R., Flanigan,M.J., Edwards,N.J., Bolanos,R., Fasulo,D.,
            Halldorsson,B.V., Hannenhalli,S., Turner,R., Yooseph,S., Lu,F.,
            Nusskern,D.R., Shue,B.C., Zheng,X.H., Zhong,F., Delcher,A.L.,
            Huson,D.H., Kravitz,S.A., Mouchard,L., Reinert,K., Remington,K.A.,
            Clark,A.G., Waterman,M.S., Eichler,E.E., Adams,M.D.,
            Hunkapiller,M.W., Myers,E.W. and Venter,J.C.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-JUL-2005) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Trattnig,S.M., Gasiorek,A., Deeb,T.Z., Ortiz,E.J., Moss,S.J.,
            Jensen,A.A. and Davies,P.A.
  TITLE     Copper and protons directly activate the zinc-activated channel
  JOURNAL   Biochem Pharmacol 103, 109-117 (2016)
   PUBMED   26872532
  REMARK    FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND
            SUBCELLULAR LOCATION.
COMMENT     On or before Feb 5, 2008 this sequence version replaced
            gi:121941806, gi:74749715, gi:74723572, gi:121945913.
            [FUNCTION] Ligand-gated cation channel that allows the movement of
            sodium and potassium monoatomic cations across cell membranes when
            activated by zinc (Zn2+), copper (Cu2+), and changes in pH
            (PubMed:26872532). Could also transport cesium (PubMed:26872532).
            {ECO:0000269|PubMed:26872532}.
            [CATALYTIC ACTIVITY] Reaction=Na(+)(in) = Na(+)(out);
            Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101;
            Evidence={ECO:0000269|PubMed:26872532}.
            [CATALYTIC ACTIVITY] Reaction=K(+)(in) = K(+)(out);
            Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
            Evidence={ECO:0000269|PubMed:26872532}.
            ACTIVITY REGULATION: Inhibited by the divalent cations magnesium
            and calcium. {ECO:0000269|PubMed:26872532}.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000269|PubMed:16083862,
            ECO:0000269|PubMed:26872532}; Multi-pass membrane protein
            {ECO:0000255}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=3; Name=1; IsoId=Q401N2-1; Sequence=Displayed; Name=2;
            IsoId=Q401N2-2; Sequence=VSP_030911, VSP_030912; Name=3;
            IsoId=Q401N2-3; Sequence=VSP_030909, VSP_030910.
            [TISSUE SPECIFICITY] Detected in pancreas, brain, liver, placenta,
            trachea, kidney, spinal cord, stomach and fetal brain. In the adult
            brain region expression is detected in the hippocampus, striatum,
            amygdala and thalamus. {ECO:0000269|PubMed:12381728,
            ECO:0000269|PubMed:16083862}.
            [PTM] Glycosylated. {ECO:0000269|PubMed:16083862}.
            [MISCELLANEOUS] [Isoform 3]: May be produced at very low levels due
            to a premature stop codon in the mRNA, leading to nonsense-mediated
            mRNA decay. {ECO:0000305}.
            [SIMILARITY] Belongs to the ligand-gated ion channel (TC 1.A.9)
            family. {ECO:0000305}.
            [CAUTION] It is uncertain whether Met-1 or Met-2 is the initiator.
            {ECO:0000305}.
            [SEQUENCE CAUTION] Sequence=AAI10598.1; Type=Erroneous initiation;
            Note=Truncated N-terminus.; Evidence={ECO:0000305};
            Sequence=AAO20969.1; Type=Erroneous initiation; Note=Truncated
            N-terminus.; Evidence={ECO:0000305}; Sequence=EAW89365.1;
            Type=Erroneous initiation; Note=Truncated N-terminus.;
            Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..412
                     /gene="ZACN"
                     /gene_synonym="L2"
                     /gene_synonym="LGICZ"
                     /gene_synonym="LGICZ1"
                     /gene_synonym="ZAC"
     Protein         1..412
                     /product="Ligand-gated cation channel ZACN"
                     /note="Ligand-gated ion channel zinc-activated 1;
                     Ligand-gated ion-channel receptor L2; Zinc-activated
                     channel"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..25
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          26..412
                     /region_name="Mature chain"
                     /note="Ligand-gated cation channel ZACN.
                     /id=PRO_0000317165."
     Region          26..233
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          60..229
                     /region_name="LGIC_ECD_ZAC"
                     /note="extracellular domain of zinc-activated ligand-gated
                     ion channel; cd18994"
                     /db_xref="CDD:349795"
     Region          75..126
                     /region_name="Splicing variant"
                     /note="DILRYTMSSMLLLRLSWLDTRLAWNTSAHPRHAITLPWESLWTPRLTILEA
                     L -> SSVLPRATALHSHGDCSGSAPCSKARGSGCHGLTPGNHLKVQPPCINPSGDI
                     (in isoform 3). /evidence=ECO:0000303|PubMed:15489334.
                     /id=VSP_030909."
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          127..412
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 3).
                     /evidence=ECO:0000303|PubMed:15489334. /id=VSP_030910."
     Region          152
                     /region_name="Variant"
                     /note="A -> T (in dbSNP:rs2257020).
                     /evidence=ECO:0000269|PubMed:12381728,
                     ECO:0000269|PubMed:14702039. /id=VAR_038483."
     Region          157..171
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349795"
     Bond            bond(157,171)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            170
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          182..266
                     /region_name="Splicing variant"
                     /note="AMELEFQAHVVNEIVSVKREYVVYDLKTQVPPQQLVPCFQVTLRLKNTALK
                     SIIALLVPAEALLLADVCGGLLPLRAIERIGYKV ->
                     GADRAGAAGLRRGGGRWGRGTPRSVVQGQGAGQGEGAKADRRRTPRSVFRAVYPRLRR
                     AAPALPLRPPLEWQPISVLSGSLRAPL (in isoform 2).
                     /evidence=ECO:0000303|PubMed:14702039,
                     ECO:0000303|PubMed:15489334. /id=VSP_030911."
     Region          231..407
                     /region_name="LGIC_TM"
                     /note="transmembrane domain of Cys-loop
                     neurotransmitter-gated ion channels; cl38911"
                     /db_xref="CDD:476813"
     Region          234..254
                     /region_name="Transmembrane region"
                     /note="Helical; Name=1. /evidence=ECO:0000255."
     Site            order(235..236,243..244,246..247,250,253..255,263..264,
                     266..268,270..271,274..275,281..282,284,305,309,312,316,
                     371)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349850"
     Region          235..255
                     /region_name="TM1 helix"
                     /note="TM1 helix [structural motif]"
                     /db_xref="CDD:349850"
     Region          255..265
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          263..284
                     /region_name="TM2 helix"
                     /note="TM2 helix [structural motif]"
                     /db_xref="CDD:349850"
     Region          266..286
                     /region_name="Transmembrane region"
                     /note="Helical; Name=2. /evidence=ECO:0000255."
     Region          267..412
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:14702039,
                     ECO:0000303|PubMed:15489334. /id=VSP_030912."
     Region          287..298
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Region          295..317
                     /region_name="TM3 helix"
                     /note="TM3 helix [structural motif]"
                     /db_xref="CDD:349850"
     Region          299..319
                     /region_name="Transmembrane region"
                     /note="Helical; Name=3. /evidence=ECO:0000255."
     Region          320..368
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          328..360
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          365..386
                     /region_name="TM4 helix"
                     /note="TM4 helix [structural motif]"
                     /db_xref="CDD:349850"
     Region          369..389
                     /region_name="Transmembrane region"
                     /note="Helical; Name=4. /evidence=ECO:0000255."
     Region          390..412
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
ORIGIN      
        1 mmalwsllhl tflgfsitll lvhgqgfqgt aaiwpslfnv nlskkvqesi qipnngsapl
       61 lvdvrvfvsn vfnvdilryt mssmlllrls wldtrlawnt sahprhaitl pweslwtprl
      121 tilealwvdw rdqspqarvd qdghvklnla latetncnfe llhfprdhsn cslsfyalsn
      181 tamelefqah vvneivsvkr eyvvydlktq vppqqlvpcf qvtlrlknta lksiiallvp
      241 aeallladvc ggllplraie rigykvtlll sylvlhsslv qalpsssscn plliyyftil
      301 llllflstie tvllagllar gnlgaksgps paprgeqreh gnpgphpaee psrgvkgsqr
      361 swpetadrif flvyvvgvlc tqfvfagiwm waacksdaap geaaphgrrp rl
//
Feature
Display: FASTA GenBank Help
Details

Supplemental Content

Change region shown

Customize view

Reference sequence information

  • RefSeq genomic sequence
    See the genomic reference sequence for the ZACN gene (NG_030672.1).
  • RefSeq protein
    See the reference protein sequence for ligand-gated cation channel ZACN precursor (NP_851321.2).

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
External link. Please review our privacy policy.