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Database: UniProt
Entry: A0A369SD13_9METZ
LinkDB: A0A369SD13_9METZ
Original site: A0A369SD13_9METZ 
ID   A0A369SD13_9METZ        Unreviewed;       869 AA.
AC   A0A369SD13;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cyclic nucleotide-gated cation channel alpha-3 {ECO:0000313|EMBL:RDD44818.1};
GN   ORFNames=TrispH2_002895 {ECO:0000313|EMBL:RDD44818.1};
OS   Trichoplax sp. H2.
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD44818.1, ECO:0000313|Proteomes:UP000253843};
RN   [1] {ECO:0000313|EMBL:RDD44818.1, ECO:0000313|Proteomes:UP000253843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Panama {ECO:0000313|EMBL:RDD44818.1,
RC   ECO:0000313|Proteomes:UP000253843};
RC   TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD44818.1};
RX   PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA   Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT   "Trichoplax genomes reveal profound admixture and suggest stable wild
RT   populations without bisexual reproduction.";
RL   Sci. Rep. 8:11168-11168(2018).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDD44818.1}.
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DR   EMBL; NOWV01000022; RDD44818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369SD13; -.
DR   STRING; 287889.A0A369SD13; -.
DR   Proteomes; UP000253843; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR   PANTHER; PTHR45638:SF7; CYCLIC NUCLEOTIDE-GATED ION CHANNEL-LIKE, ISOFORM E; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        168..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          482..597
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          36..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          827..861
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        7..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   869 AA;  100260 MW;  DBFEAEF190D4A4C5 CRC64;
     MSKDYDIQSA HQDYPTKNGH DPHLQQQQEH IMTVEETTPI EGGSGKKRLQ RNNRSSSSHI
     LSQFYRWSNA FTKVRAQNQS VQKRRHDSFI EKFTTRQDRR ISIDSEEDLV TVANEENSLS
     DDKSHGKGRD DDDDVVITDQ KDYFYDTYGD VRMRYERWII NPKSLTNLYW LALLSLAVLY
     NFWLIIIRTA FPEFQNETPI LWGFLDYSTD LIYIADIYLS TRTGYLSHGI VVTDRHKLRQ
     HYFRSGRVVM DVICLLPFDF FYYNVTQMFP IIRIGRLLKY YRTNDFYRLI QSRTYRPNFW
     RILNLIHTLF ILIQWFAAIY YMISGYIGFG SDGWVYPEPV GINGNLSVKY LKSVYWATLT
     LTTIGEIPSP VTQIEYLFTL LSYFCGLFIF ASIVGLLGNV IAKRNARRSQ FDQLLDDAKE
     YMSKRNVSSN LQTRVQRWFD YSWERGQLNG IGEARAISML PTKLKTELAL HVHLETLKKV
     TLFQNCEREF LHDLVLKMKH HIYTPMDLVC QLGEIAREMY IISNGKLEVL SESGAVIATL
     KEGDFFGEIG VLSLSEAANS FHLLTVYGFL DRRTANVRSI GFSELFVLLK DDVLEAMEDY
     PKAKVYLTQY AKARLAGMKR VNSETQDTKE NCETDTNTAR NRVGLRKILN LSITRNKIKP
     INKNEDQGEI QIKRSHTISG GRSGPSTSKI RRRLQSATSR KRFSNSSNNI NVDNDISLPM
     REDIERNETQ NNSKYTSNFT GPVTSTTYAN LLPYASDNTG TVENITTRLA KSAKSIENMI
     HDLQAEVASN HATNARGINS LYKLPTISSF YVPRTEDEKS SLTSVEVQQL KGLVRQLQDD
     IEEKNKTINN LTLEIHKFQG DTTNKNIEN
//
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