ID B3SAI8_TRIAD Unreviewed; 632 AA.
AC B3SAI8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV20269.1};
GN ORFNames=TRIADDRAFT_51027 {ECO:0000313|EMBL:EDV20269.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV20269.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV20269.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV20269.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; DS985261; EDV20269.1; -; Genomic_DNA.
DR RefSeq; XP_002117219.1; XM_002117183.1.
DR AlphaFoldDB; B3SAI8; -.
DR STRING; 10228.B3SAI8; -.
DR EnsemblMetazoa; TriadT51027; TriadP51027; TriadG51027.
DR GeneID; 6758432; -.
DR KEGG; tad:TRIADDRAFT_51027; -.
DR CTD; 6758432; -.
DR eggNOG; KOG0501; Eukaryota.
DR HOGENOM; CLU_005746_2_3_1; -.
DR InParanoid; B3SAI8; -.
DR OMA; MIGWMAS; -.
DR OrthoDB; 66005at2759; -.
DR PhylomeDB; B3SAI8; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
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; IPR003967; K_chnl_volt-dep_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:SF435; POTASSIUM VOLTAGE-GATED CHANNEL PROTEIN EAG; 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; PR01470; ERGCHANNEL.
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 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:UP000009022};
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 195..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 505..599
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 632 AA; 72317 MW; 715296029FF68677 CRC64;
MPLATRGLIA PQNMFLEDLI ARSKNLENCF VLANAKQEDN PIVYCSDGYC CLTGYQRHEV
LHKAADYEHL YGEETDRKSV SKLKSAFALK QKIQHELTLY KKDGTPFIAA IQIAPVKNED
QEVIMFLITL RDISALRENQ NRKSRRFSLL STTNNYHHSH SMCLTNMDTE LPDYKEETPR
SPTGIILHYS TTKVIWDWVI LFFTFYTAIF VPFELAFNRD YRKEIGFLIM DCIVDVIFLS
DVVINFRTTY VDGTGHIVSH PPLIVRNYIT GWFVIDLLAA LPYEIFTLGD VLRLLRLSRF
IRKFNEYVEY GATMIVLLMF TYVLVAHWLA CIWYRIGFDE CTTFGWLHSL AEQSGITAKV
NYTSCQQISV ASAYSTSLYF TMSSLTTVGF GNVSANTIGE KIFSIIIMII GSLMSAFIFG
NVTAILQELY SSTQRYHAIL KDMKRFNQVY SLPKDLRRRV EDYFISSWAA TKGIDTKEIL
KYWPKEIQAE IKMHMNRKIL RDATCFSNAS EGCLRQMAER FEMQHTGPGD ILIHSGQSLN
HLYFIACGSF EVYSADVGVT CILTKGDVFG DDFIKNKGLG RSHSMVRALT YCDLHTISRI
HLLEVAGLYP EWAPVFSENL NLTCSLRDSG VR
//
