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Database: UniProt
Entry: I2H6M9_TETBL
LinkDB: I2H6M9_TETBL
Original site: I2H6M9_TETBL 
ID   I2H6M9_TETBL            Unreviewed;      1561 AA.
AC   I2H6M9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN   Name=TBLA0G00840 {ECO:0000313|EMBL:CCH62031.1};
GN   ORFNames=TBLA_0G00840 {ECO:0000313|EMBL:CCH62031.1};
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:CCH62031.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH62031.1, 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:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000256|ARBA:ARBA00008842,
CC       ECO:0000256|RuleBase:RU003844}.
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DR   EMBL; HE806322; CCH62031.1; -; Genomic_DNA.
DR   RefSeq; XP_004181550.1; XM_004181502.1.
DR   STRING; 1071380.I2H6M9; -.
DR   GeneID; 14497163; -.
DR   KEGG; tbl:TBLA_0G00840; -.
DR   eggNOG; KOG1737; Eukaryota.
DR   HOGENOM; CLU_001040_1_0_1; -.
DR   InParanoid; I2H6M9; -.
DR   OMA; DNHGDVT; -.
DR   OrthoDB; 960at2759; -.
DR   Proteomes; UP000002866; Chromosome 7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0120015; F:sterol transfer activity; IEA:UniProt.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProt.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProt.
DR   GO; GO:0030011; P:maintenance of cell polarity; IEA:UniProt.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:UniProt.
DR   CDD; cd13292; PH_Osh1p_Osh2p_yeast; 1.
DR   Gene3D; 2.40.160.120; -; 1.
DR   Gene3D; 3.30.70.3490; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037239; OSBP_sf.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR10972:SF205; OXYSTEROL-BINDING PROTEIN; 1.
DR   PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   REPEAT          146..168
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          246..278
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          330..428
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          33..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          843..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          923..1055
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1486..1516
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        456..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..882
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1561 AA;  174164 MW;  04456AA9647D4968 CRC64;
     MNGFNATANT FADANVVTQP VVNTNSAAIV STTPTGVPPV NPSPAHSSTP TTVSKPLLKL
     KVLDTLRQGT IDDLQELLNT SFVPRDDPIV REVSQLLLHY AVQVAPLELI KEIVKKWVPT
     STKSPKHNNS GENFVPHLDL NYQDGDGNTP LHLASEQSRG DVITYLMDLP NINDCILNDS
     ELLPLEMCKN LNVAQMMQIK RANYVAATAK ELRNCLNSRD FKRLTKIFDN PRNKELLDIN
     GIDPETGDTV LHEFIKKRDV HMCKWLIEHG SDPFKRDRSG KLPSDLLMNV NENDVPTNSK
     MSIDVQLKKM LEKAAKEQSV INVANNLNEA PTLKGYLKKW TNFAQGYKLR WFVLSNDGRL
     AYYKDQADTK NPNRGYLNMG TCYLHLDSTE KLKFEIVGGA TGTVRWHLKG NHPIETNRWV
     WAIQGAIRFA KDKELLKGKN TVSPALVMNN YVSRENSTKQ VTATSNDGRS RSKTASSLSK
     SDDSKGRTSS HKRSGSSNKS KVILPDDIRM SNNLTASGKS YVNRVLETRL ESSSPGTSIK
     GVSLENTATT TKQKQSRSPS KSQQATNIPE STQYTAEPEA QQVQESMVDD TAMPVSTDTT
     TEPPIQPQTL VQEPPLQTQQ AELQDLQEAA DSNYDYEPTD DAAYTGNYEQ QYSEGEALSD
     EDEDDGIGMN IDTDDEDIQI QYGPFTQQVE LQQKHISMEL SSLTELLDTN IMDEASWSTI
     KNSIKTITQC FEQLNTLSAS RDKKLVAMLT KQKDVNNVWI QSVKDLEREL GKKSQRLEAM
     DKERRTLKKV VNKRIQDTES PQNVAKRLSK HDDSSSTLEQ VQKFISATKE NDEDSDVEEF
     FDAEDASEDS DSVSSNIQSY DYSTVNGNTN SLSTTNPVLV TPMETPQLPA DIQPAQSTHA
     TPAPVPVQPT QAAQVLAAQA QAHVQAQQQA QAFAQQQAQL QAQQQAQQQA QLQAQQQAQL
     QAQQQAQAQA LAQQQAQAQA LAQQQAQAQA LAQQQAQAQA LAQQQAQAQA LAQQQAQAQA
     LAQQQAEAEA QAQAHQEAQA QAQAQIQAQA QAQAQAQAQA QAQAQAQAQA QAQAQAQAQA
     QAQAQAKAIQ AGPQPAKKSP EEMAEIVKVK TKEAEVIKKK APVKMMKTDL IAVTKSQAAR
     EETLNAQGTW LGYEDGQRKR LALSEDDRPS ISLWSVLKSM VGKDMTKMTL PVTFNEPTSL
     LQRVAEDLEY SELLDRACTF NDSTLRLLYV ACFAASSSAS TTQRVAKPFN PLLGETYEYA
     RPDKHYRFFT EQVSHHPPIS ATWTESPKWD FWGESYVDTK FNGRSFEVNH LGLWYVKMRP
     DDPKAPEELY TWKKPNNTVI GILVGNPQVD NHGDVTITNH NTGDKCTLHF KARGWRSSGA
     FEVRGEVFDK KGDKKWVMGG HWNESYFAKK VTNKNKGNIS LEKTKSAAGS TEGPANDGSK
     FLIWKVNDRP DAPFHLTPFA ITLNAPQPHL VKWVAPTDTR LRPDQRAMED GEYDKAANEK
     TRLEEKQRAV RKKREEGNID YKPKWFTKET HPVTKLSYWK FTGKYWNERK VHDWKRCDDI
     F
//
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