ID H2Q5V5_PANTR Unreviewed; 1083 AA.
AC H2Q5V5; A0A2J8LPT9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 3 {ECO:0000313|Ensembl:ENSPTRP00000008387.4};
GN Name=KCNH3 {ECO:0000313|Ensembl:ENSPTRP00000008387.4,
GN ECO:0000313|VGNC:VGNC:8426};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000008387.4, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000008387.4, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000008387.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming alpha subunits that can
CC associate with modulating beta subunits.
CC {ECO:0000256|ARBA:ARBA00011552}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AACZ04012898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016778940.1; XM_016923451.1.
DR AlphaFoldDB; H2Q5V5; -.
DR STRING; 9598.ENSPTRP00000008387; -.
DR PaxDb; 9598-ENSPTRP00000008387; -.
DR Ensembl; ENSPTRT00000009077.5; ENSPTRP00000008387.4; ENSPTRG00000004909.5.
DR GeneID; 451880; -.
DR CTD; 23416; -.
DR VGNC; VGNC:8426; KCNH3.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000161742; -.
DR HOGENOM; CLU_005746_6_0_1; -.
DR InParanoid; H2Q5V5; -.
DR OMA; YIGQQEI; -.
DR OrthoDB; 66005at2759; -.
DR TreeFam; TF313130; -.
DR Proteomes; UP000002277; Chromosome 12.
DR Bgee; ENSPTRG00000004909; Expressed in primary visual cortex and 11 other cell types or tissues.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
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; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR003950; K_chnl_volt-dep_ELK.
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:SF481; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 3; 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; PR01465; ELKCHANNEL.
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.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000002277};
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 215..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..90
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 582..646
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 137..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 878..905
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 137..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 117201 MW; 5C46E12427B2DE24 CRC64;
MPAMRGLLAP QNTFLDTIAT RFDGTHSNFV LGNAQVAGLF PVVYCSDGFC DLTGFSRAEV
MQRGCACSFL YGPDTSELVR QQIRKALDEH KEFKAELILY RKSGLPFWCL LDVIPIKNEK
GEVALFLVSH KDISETKNRG GPDRWKETGG GRRRYGRARS KGFNANRRRS RAVLYHLSGH
LQKQPKGKHK LNKGVFGEKP NLPEYKVAAI RKSPFILLHC GALRATWDGF ILLATLYVAV
TVPYSVCVST AREPSAARGP PSVCDLAVEV LFILDIVLNF RTTFVSKSGQ VVFAPKSICL
HYVTTWFLLD VIAALPFDLL HAFKVNVYFG AHLLKTVRLL RLLRLLPRLD RYSQYSAVVL
TLLMAVFALL AHWVACVWFY IGQREIESSE SELPEIGWLQ ELARRLETPY YLVGRRPAGG
NSSGQSDNCS SSSEANGTGL ELLGGPSLRS AYITSLYFAL SSLTSVGFGN VSANTDTEKI
FSICTMLIGA LMHAVVFGNV TAIIQRMYAR RFLYHSRTRD LRDYIRIHRI PKPLKQRMLE
YFQATWAVNN GIDTTELLQS LPDELRADIA MHLHKEVLQL PLFEAASRGC LRALSLALRP
AFCTPGEYLI HQGDALQALY FVCSGSMEVL KGGTVLAILG KGDLIGCELP RREQVVKANA
DVKGLTYCVL QCLQLAGLHD SLALYPEFAP RFSRGLRGEL SYNLGAGGGS AEVDTSSLSG
DNTLMSTLEE KETDGEQGPT VSPAPADEPS SPLLSPGCTS SSSAAKLLSP RRTAPRPRLG
GRGRPGRTGA LKAEAGPSAP PRALEGLRLP PMPWNVPPDL SPRVVDGIED GCGSDQPKFS
FRVGQSGPEC SSSPSPGPES GLLTVPHGPS EARNTDTLDK LRQAVTELSE QVLQMREGLQ
SLRQAVQLVL APHREGLCPR ASGEGPCPAS TSGLLQPLCV DTGASSYCLQ PPAGSVLSGT
WPHPRPGPPP LMAPWPWGPP ASQSSPWPRA TAFWTSTSDS EPPASGDLCS EPSTPASPPP
SEEGARTGPP EPVSQAEATS TGEPPPGSGG LALPWDPHSL EMVLIGCHGS GTVQWTQEEG
TGV
//
