ID A0A1S3J5C3_LINUN Unreviewed; 1031 AA.
AC A0A1S3J5C3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Potassium voltage-gated channel subfamily B member 1 isoform X1 {ECO:0000313|RefSeq:XP_013405044.1};
GN Name=LOC106169919 {ECO:0000313|RefSeq:XP_013405044.1};
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_013405044.1};
RN [1] {ECO:0000313|RefSeq:XP_013405044.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013405044.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013405044.1; XM_013549590.2.
DR AlphaFoldDB; A0A1S3J5C3; -.
DR STRING; 7574.A0A1S3J5C3; -.
DR EnsemblMetazoa; XM_013549590.2; XP_013405044.1; LOC106169919.
DR GeneID; 106169919; -.
DR KEGG; lak:106169919; -.
DR InParanoid; A0A1S3J5C3; -.
DR OrthoDB; 1478695at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR CDD; cd18413; BTB_POZ_Shab-like; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003971; K_chnl_volt-dep_Kv9.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537:SF286; POTASSIUM VOLTAGE-GATED CHANNEL PROTEIN SHAB; 1.
DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01494; KV9CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
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: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};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 514..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..246
FT /note="BTB"
FT /evidence="ECO:0000259|SMART:SM00225"
FT REGION 16..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 115397 MW; 77147D38B7B895DB CRC64;
MMFQANLVAS SAIQRSSLTD GQADSSTPSS SGPQGMARSH SYRARDTSIE NGSGTSFREQ
MLIRRKRESE STTSEAKITP NPLTAPSDAL PLQFSSGNQT DMQPQPGPPL KTPVYQPFMQ
GPPPDPYTIM QSRAHSNRVT INVGGVKHEV MWKTLDRMPH SRLGKLKTST SHESIMDLCD
DYSLMDNEYF FDRHPRSFAS IINFYRTGKL HLVEEMCVLS FSDDLEYWGV DELYLESCCQ
HRYHQKKEHV YEEMRKEAES LREGGEEENF GTGRCAKWRQ KLWDLLEKPQ TSRAARANFS
LSLYCLKTTT CDGLGQVLAV ISILFIILST IALTLNTIPS IQVDGDDNPH LNLVEAVCIS
WFTLEYLLRF WASPNKWKFF KGSLNIIDLL AILPYYISLC LVESNKSTEQ FHNVRRVVQI
FRIMRVLRIL KLARHSTGLQ SLGYTLQRSY KELGLLMMFL AIFVLVFSSL AYFAEKGIQK
DKFSSIPDTF WWAAITMTTV GYGDVVPATL WGKLIGAVCC ICGVLVIALP IPIIVNNFAE
FYKDQMRREK ALKRRAALER AKRTGSIVSF HSVNLRDAFA RSVELIDVVT DRSQYDSRST
ANNSIVSDHT NPNTSMHYGS QAKVNTNTSA KQGKDFPEVS DTTVPPNEHG DFPLERKTTT
QPVLGGETLK PEDENIKEVK SIDNHYPPLL YPTITDNAIH KIYKSPVHGG DNVYEHQSKQ
QLYINPFEQD EHLGGKEVYG HLGCLTSAEP SDQIVQKLDD GLTATWHRAN TENAPPSPKL
KSKGAITSKP RAHFEEPDIA KHSSIDSVHS PGKSKFRLRK TPFGRYSSSG ESPPSGRKPY
QLIPSPKSGR KRTSSGPECN TGSNLDTPKK KSILKRDAIN KEETENLLKD PLPVDSSGPR
HHSGTDDDEV FYTPKETPAK PATDYRAKQT TRGTSEQDSS GENGGIIDTV LTHDLDLEND
LDLPDGHCTI ESGVDNESQV SGTSSVDSNY KSNQKEQTDV QHEGYHGNSF NDVDSKPSND
AHIKYADLED L
//