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Database: UniProt
Entry: A0A2R2MKV0_LINUN
LinkDB: A0A2R2MKV0_LINUN
Original site: A0A2R2MKV0_LINUN 
ID   A0A2R2MKV0_LINUN        Unreviewed;      1146 AA.
AC   A0A2R2MKV0;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Potassium voltage-gated channel subfamily H member 8 {ECO:0000313|RefSeq:XP_023930846.1};
GN   Name=LOC106158338 {ECO:0000313|RefSeq:XP_023930846.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_023930846.1};
RN   [1] {ECO:0000313|RefSeq:XP_023930846.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_023930846.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   RefSeq; XP_023930846.1; XM_024075078.1.
DR   AlphaFoldDB; A0A2R2MKV0; -.
DR   STRING; 7574.A0A2R2MKV0; -.
DR   EnsemblMetazoa; XM_024075078.1; XP_023930846.1; LOC106158338.
DR   KEGG; lak:106158338; -.
DR   InParanoid; A0A2R2MKV0; -.
DR   OrthoDB; 74296at2759; -.
DR   Proteomes; UP000085678; Unplaced.
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; PS00889; CNMP_BINDING_2; 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:UP000085678};
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        458..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        532..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          638..741
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1031..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1087..1128
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        29..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1146 AA;  129516 MW;  31E9A5EFC3A5380C CRC64;
     MEAVAIMAEN GESEVRKRKK KKRHRPPGTV QPINSNKGKP SESLEMLGNH DSNSHMYHTK
     EVSPELEVNV TGTQVSVAAE GGMNDEEQSI SPVWLPQQPQ ESDTVNVAAV ENAHISRNVQ
     DEYNTKLPLR TRETQPSIMS SKLDQDDYQD LNVQMLDQEL KAALNSPESD ETTCTLPNSN
     NGNLIKSDEE EGMIKSEDSQ VISNQDNVLQ VGRQELAKAG MEKENLIEKT DQRVKEISGG
     RPTARWKKLQ NTLKATNEVQ RPAGREFKRK SSGMNRQDSF LQRFSTRQRE TDENEDEEEG
     QSKTQNKKNK RKWTFVVNPD GDTMFYWLGV QALCALYNLW TLIAREAFPD IQTGSPLAWF
     ILDGFMDFMY LTDIAFQFRT GYLEQGLIVY DSKQLALHYV KSHYFKIDIL ALTPLDLLQL
     TTGIHPMWRF PRFFKVYRVY QFYYMAESRT IYPNFWRVMN LIHILLLGSH WFAAFYFLIS
     KSENFPANDW SYPPLQGEYA SVTRMYLKSL YWSTLTLTTI GDLPPPKNNW EYVFTILSYL
     IGVFVFATIV GQVGNVIANR NASRLEFERL LDGAKAYMRN HNVPRDMQTR VQRWYDYAWS
     RGRISGGGDI NSLGLLPDKL KTELALHVNL ETLRKVTIFQ ECEPEFLHDL VLKMKAYIFT
     PGDLICRKGE VAREMFIIAD GVLEVLSESG EVVTQMVSGD FFGEIGILNL DGGVNRRTAD
     VRSVGYSELF VLSREDVLSA LQDHPEAEAF MQEYGRKRLK EIEERRRKKM LQNQVHVAAS
     LCQLTKPTWQ VASKKAKKNV KFKDKLTSSD GENEEDLVSP CRVLRASSRR RRFVKGKEYS
     QINNLDADDQ AKPLVPCDIQ IKVEMCGSDA SSKEDSDGSE TSPDQNVLPP PAVNSVSVDN
     SSSQAPVVHL TVKGTEENME DLPDVGSDEV FEPPEIKYVP TPILLRKKKM THHKLRKTLS
     EEIDAIASKC EKKRDCSHYS DIGMPLIPAS PSQKGSMASL RSHSCDCVLS YRDNTPGGSG
     GVDLQNLKSF DKSNLNQPQP SGPESTGLST TPAPLSSEAI PKVVVQGNEI GSQDPSSLLT
     GLKSVLMQNM DAVMNQFQDK VNMLEDDNRK KAEVIKELES KVKSLQRALL WKSSKETGMT
     VPSVDI
//
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