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
//