ID C3YB83_BRAFL Unreviewed; 1085 AA.
AC C3YB83;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=BTB domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_123718 {ECO:0000313|EMBL:EEN62240.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN62240.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN62240.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN62240.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- FUNCTION: Mediates H(+)-dependent pyridoxine transport.
CC {ECO:0000256|ARBA:ARBA00037192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n H(+)(out) + pyridoxine(out) = n H(+)(in) + pyridoxine(in);
CC Xref=Rhea:RHEA:76203, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709;
CC Evidence={ECO:0000256|ARBA:ARBA00036956};
CC -!- SUBCELLULAR LOCATION: Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004155}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000256|ARBA:ARBA00008335}.
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DR EMBL; GG666497; EEN62240.1; -; Genomic_DNA.
DR RefSeq; XP_002606230.1; XM_002606184.1.
DR AlphaFoldDB; C3YB83; -.
DR STRING; 7739.C3YB83; -.
DR eggNOG; KOG1545; Eukaryota.
DR eggNOG; KOG2563; Eukaryota.
DR InParanoid; C3YB83; -.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; cd17397; MFS_DIRC2; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR049680; SLC49-like.
DR InterPro; IPR049604; SLC49A4-like.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10924; MAJOR FACILITATOR SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR10924:SF27; SOLUTE CARRIER FAMILY 49 MEMBER 4; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00022882};
KW Ion transport {ECO:0000256|ARBA:ARBA00022882};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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:ARBA00022882};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 136..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 568..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 670..700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 816..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..896
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 908..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 937..961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 967..991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1003..1024
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..98
FT /note="Potassium channel tetramerisation-type BTB"
FT /evidence="ECO:0000259|Pfam:PF02214"
FT DOMAIN 139..395
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
SQ SEQUENCE 1085 AA; 120288 MW; A5E2C22FF28DE991 CRC64;
MSSHKHILRI NVSGLKFAIC CCKLDQYPAT LLGSPKRRAK YYDPARREYF LDRHRPTAEA
VFHFYHSSGT LQKPEEVPMD TFIEELKFYD LGKDVMEEYL RGQGYVPKKQ HPLPPESQKL
KRTIWLLFEH SNSSKAATFI AVVSITFILV SIIGLCLETL PVFHKDKHKP ATPSDDRTNS
TSSPHQAWGR LEEEMETGDP YKDDPFFLLE TVCICWFTIE LILRFYSCPN RRVFFKSLLN
VVDLLSILPY YVTLVIAGLA GHDQDIDLRF LFVLRVLRTF KLSRYNRGFK VLGKTLARSL
SDIGMLMVFL SIVVVLFSSI MYFVEASDPA TKFQSIPDGF WWAIITIVTV GYGDMYPTTT
VGKLIGALCV ISGLLSIALP VPVIVSNFEM FYNQQVIEDD EGEEVKVKEE PEEIGTLSDI
HSLADRQSDV DSGLGRSPLH SISGNRDLND VIVTSETGPG QSLGQRIDFS GYVWPRVGGG
RQAGSYRSRM TQFAVPTSPD SEQDAVLPTT TVLPSTAPSP PQIVAYHRRW WIVGTFCLLG
IAQGAVWNCW GPISDSAKLV YRWTDGKIAM LANWGCIAFI LFAPGLMYIN ADNNDYLLVQ
SGTMANVSAP DRSVVLYRRR WYVLAVFSLL GIAQGAVWNS WGPVSVSAKL VFGWKDTDIA
LLENWDNITY VAFTIVAMWI LVVKGLRFSV VLTALLIAVG TGLRCIPASA DIATILINAG
QFLNGVAGIM LMAAPPLISS TWFPPNQRTT ATAISSIFNY VGTSVGYLIG PLFVSQPHLM
PNSTLHYNQK QSVLPSTGAY LSMFVFPAVV EDISGQIMRL MYVECGYCTA VFLAILIYFP
SKPPTPPSLS AAMDRLDFRT GLKKLFRHGQ FWLVCLAYCV PGGVIGGWTA VLDVILSPHG
ISQIDAGWLG FYGNIAGCGV GLLLGRFADY FAGHLRLIIV VMMCCATGSL TWFTIMLFGA
LPLTQVSLYF SFILTMVSVN ASIPLFLELV METTYPIEEA VSAGVMTWGN NLFALIFLLV
PLLPKVGVTW MNWAALGGVA CSVPLLCVFR ENYRRLHLDT GAVSEGNDET QHLINESSII
EDRKG
//
