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Database: UniProt
Entry: K7G062_PELSI
LinkDB: K7G062_PELSI
Original site: K7G062_PELSI 
ID   K7G062_PELSI            Unreviewed;       996 AA.
AC   K7G062;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Potassium voltage-gated channel subfamily H member 5 {ECO:0000313|Ensembl:ENSPSIP00000013672.1};
GN   Name=KCNH5 {ECO:0000313|Ensembl:ENSPSIP00000013672.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000013672.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000013672.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AGCU01003949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01003950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01003951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01003952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01003953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01003954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01003955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01003956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01003957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01003958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K7G062; -.
DR   STRING; 13735.ENSPSIP00000013672; -.
DR   Ensembl; ENSPSIT00000013736.1; ENSPSIP00000013672.1; ENSPSIG00000012098.1.
DR   eggNOG; KOG0501; Eukaryota.
DR   GeneTree; ENSGT00940000156540; -.
DR   HOGENOM; CLU_005746_3_1_1; -.
DR   OMA; PMNKTET; -.
DR   TreeFam; TF313130; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.1200.260; -; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003949; K_chnl_volt-dep_EAG.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR10217:SF533; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 5; 1.
DR   PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   PRINTS; PR01464; EAGCHANNEL.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00086; PAC; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; 1.
PE   4: Predicted;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007267};
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};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT   TRANSMEM        212..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        471..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          86..138
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          571..671
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          860..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          968..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..886
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..905
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   996 AA;  112865 MW;  D7D552711523F975 CRC64;
     MLPYLVVNYK FSSLFYSFLE SSFLLGNAQI VDWPVVYSND GFCKLSGYHR ADVMQKSSTC
     SFMYGELTDK KTIDKVRQTF DNYESNCFEI LLYKKNRTPV WFYMQIAPIR NEHEKVVLFL
     CTFKDITLFK QPIEDDSTKG WTKFARLTRA LTNSRSVLQQ LTPMNKAEVV HKHSRLAEVL
     QLGSDILPQY KQEAPKTPPH IILHYCAFKT TWDWVILILT FYTAIMVPYN VSFKTKQNNI
     AWLVLDSVVD VIFLVDIVLN FHTTFVGPGG EVISDPKLIR MNYLKTWFVI DLLSCLPYDI
     INAFENVDEV SNFSPHKIDC SSQSSPLLVA RRSQGISSLF SSLKVVRLLR LGRVARKLDH
     YLEYGAAVLV LLVCVFGLVA HWLACIWYSI GDYEVIDEVT NTIKTDSWLY QLALSIGAPY
     RYNNSGSGQW EGGPSKDSLY ISSLYFTMTS LTTIGFGNIA PTTDGEKIFS VAMMMVGSLL
     YATIFGNVTT IFQQMYANTN RYHEMLNNVR DFLKLYQVPK GLSERVMDYI VSTWSMSKGI
     DTEKVLSICP KDMRADICVH LNRKVFNEHP AFRLASDGCL RALAVEFQTI HCAPGDLIYH
     AGESVDALCF VVSGSLEVIQ DDEVVAILGK GDVFGDIFWK ETTLAHACAN VRALTYCDLH
     IIKREALLKV LDFYTAFANS FSRNLTLTCN LRKRIIFRKI SNSRRKKKSF CARNHANEVT
     LSIPVDHPVR KLFQKFKQQK EMRNQGTTHI DPERNQLQVE SRPMQNGAAV TGTSVVTVSQ
     ITPIQTSLAY VKTSEPLKQN NRDAMELKPN GNTEKCLKVN SPIRMKNGNG KGWLRLKNNM
     GAQEEKKEDW NNVTKAESMG LLSDDPKCND SESSVTKNPL RKTDSCDSGI TKSDLRLDKA
     GETRSPLEHS PIQADAKHPF YPIPEQALQT TLQEVKHELK EDIQLLSSRM TALEKQVAEI
     LKILSEKNTS QTSSPKTHLS PQLPPQIPCQ DIFSVS
//
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