ID I2H1Z6_TETBL Unreviewed; 958 AA.
AC I2H1Z6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=SPX domain-containing protein {ECO:0000259|PROSITE:PS51382};
GN Name=TBLA0C06010 {ECO:0000313|EMBL:CCH60398.1};
GN ORFNames=TBLA_0C06010 {ECO:0000313|EMBL:CCH60398.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60398.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH60398.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 EMBL; HE806318; CCH60398.1; -; Genomic_DNA.
DR RefSeq; XP_004179917.1; XM_004179869.1.
DR AlphaFoldDB; I2H1Z6; -.
DR STRING; 1071380.I2H1Z6; -.
DR GeneID; 14495516; -.
DR KEGG; tbl:TBLA_0C06010; -.
DR eggNOG; KOG1281; Eukaryota.
DR HOGENOM; CLU_005170_8_0_1; -.
DR InParanoid; I2H1Z6; -.
DR OMA; NLENCKM; -.
DR OrthoDB; 5485124at2759; -.
DR Proteomes; UP000002866; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR CDD; cd01115; SLC13_permease; 1.
DR InterPro; IPR004680; Cit_transptr-like_dom.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR10283:SF110; INORGANIC PHOSPHATE TRANSPORTER PHO87-RELATED; 1.
DR PANTHER; PTHR10283; SOLUTE CARRIER FAMILY 13 MEMBER; 1.
DR Pfam; PF03600; CitMHS; 1.
DR Pfam; PF03105; SPX; 1.
DR PROSITE; PS51382; SPX; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866};
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}.
FT TRANSMEM 483..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 518..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 571..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 613..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 655..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 738..759
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 766..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 794..814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..861
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 881..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..365
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REGION 39..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 107149 MW; F08D7D02B4A44133 CRC64;
MRFSHFLKYN AVPEWQNHYM DYNELKNLIY TLQTDELKRN PNTEDPFDDL EKQSNNSSPK
RKNFKDKLKK FSFTKKNNSS ASNSNSYLNT LPHNDTIIEL QDYDSPEKDQ SDSNNTSSTK
KNKISTKIHS LKKPKDSLFS SSRHSSISSN DDKSSIENTY DTFVNKLTDE RNKVDDFYKR
TELKLYEKFE NLLLDLQKEH IINHHDSNIL QTQDGNSNFS SELTIEDETS PYLKGNLNNS
NDLKETAIIE EIHKSSKTPD IEALEHTSIT ELRSRTTIDY SEEDFDYEED IEQYDDQENT
ALLNYNDFNS QFSKEIFIKT ILLLIYTLIC ANLKSFIELN SIGFTKITKK ADKVLLLTTR
TDLIQSRVFY NDIYTFQWDT LDVLNNKISQ LIEFYSIITN QSLNLENCKM ELKSFLHDHI
VWERSNTWKD MLGLLSQTND EISKNEEEEA RRLKLGLRYR DLPLPKPINM GKLGTINNIK
IPLLFFTWKA AKIAFIILFT GLLLGIKTMN DRVEGRCLAL VECCVFLWAL EAIPLFTTAF
LVPMLVVLFK VLKNADGTTM GAAAASAKTL STMWSSTIMI LIAGFTLGEA LSQYEIANVL
ASWLLAGAGT KPSMVLLMSM AVVFFLSMWI SNVASPVLTY SLLKPVLDDL DADTPFAKAI
IMGIALAADV GGMASPISSP QNIISMQYLA PYGIGWGQFF AVALPVGILI TLCAWGIMCT
TFKINETKLK KFTPIRTVFT LKQYFIIFVT IGTIILWCVE KQIEGAFGAS GQIAVLPIVL
FFGTGLLTSH DLNTFPWSTV ILAMGSVALG DAVSSSGLLK TIATSLQKRI EHDSVMAILC
IFGVLMLVVG TFVSHTVSAI ILIPLVQEIG DSLPDPKASP VLVFGCALLA SCGMALPSSG
FPNVTAISMI DKKGRRYLTM GEFLSRGVPT SLAGFVLVIT VGYGIMTSIL HGRTTPAT
//