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Database: UniProt
Entry: A0A061DJ48_THECC
LinkDB: A0A061DJ48_THECC
Original site: A0A061DJ48_THECC 
ID   A0A061DJ48_THECC        Unreviewed;       980 AA.
AC   A0A061DJ48;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830};
GN   ORFNames=TCM_000994 {ECO:0000313|EMBL:EOX91956.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX91956.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOX91956.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC       {ECO:0000256|ARBA:ARBA00005315}.
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DR   EMBL; CM001879; EOX91956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061DJ48; -.
DR   STRING; 3641.A0A061DJ48; -.
DR   EnsemblPlants; EOX91956; EOX91956; TCM_000994.
DR   Gramene; EOX91956; EOX91956; TCM_000994.
DR   eggNOG; KOG2125; Eukaryota.
DR   HOGENOM; CLU_004770_1_0_1; -.
DR   InParanoid; A0A061DJ48; -.
DR   OMA; RVKFGHD; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000026915; Chromosome 1.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   CDD; cd16024; GPI_EPT_2; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   InterPro; IPR037674; PIG-G_N.
DR   InterPro; IPR039527; PIGG/GPI7.
DR   InterPro; IPR045687; PIGG/GPI7_C.
DR   PANTHER; PTHR23072:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 2; 1.
DR   PANTHER; PTHR23072; PHOSPHATIDYLINOSITOL GLYCAN-RELATED; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   Pfam; PF19316; PIGO_PIGG; 2.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        475..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        519..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        548..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        588..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        635..655
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        664..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        701..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        757..775
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        781..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        812..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        849..873
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        893..917
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        937..961
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          524..654
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
FT   DOMAIN          771..959
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
SQ   SEQUENCE   980 AA;  108422 MW;  131E6D7B06B4678B CRC64;
     MPPLTCTKLA LITLTGVIIQ IIGLSLFVFG FFPVKPALTG TSGSESFHLP ICNSVGNQSE
     TTLPSDQLRS LYKELSGIPS LFDRLILMVI DGLPAEFVLG KNGKPPSKQF LEAMPYTQSL
     LASGLAVGYH AKAAPPTVTM PRLKAMVSGA IGGFLDVAFN FNTQAMLDDN LLGQFFRIGW
     EMVMLGDETW LKLFPGVFKR HDGVSSFYVK DTVQVDQNVS RHLGDELSRD DWNLMILHYL
     GLDHVGHIGG RSSMLMAPKL KEMDEVVKLI HSSTTQSQGN ARGRTLLMVV SDHGMTENGN
     HGGSSYEETD SLALFIGLRN HDFDYASVIH QVDIAPTLAL LFGMPIPKNN VGVLITEAFD
     SLKEDQRLRA LELNSWQLLR LLQAQLSGLP CRNFPCDVFS NHQSSGPSEC NHSTANMLCC
     LYMEAEALHS SLKSKGGSEF ASNKEYSRTA AAYYKFLKSA SEWLSRRSTD KPVKLLAVGL
     ATMFISCVIL SSLMFCWVRE IYLGGKRQPS NLNDSMNGWS LDETFILGVI LILVTSMGSS
     SMVEEEHYIW YFVVSTFYLL LLRKTAQSLA PVGVQSSLGI HKGQSGKVYS RMCLIFLLLI
     SGRILRGWHQ GGVNWTSLPD ISKWLELAGS HYVKLLQLIS AFLVISIGVC ALFSIESKGK
     FFQMVRLSFL MSALLVLLHI IRYQDYTFSS TNYGATLLAQ IIYAILGAAT MGIVVALPWL
     IPFSTFKICP TDNTLSPTSF FLSIQEKFPL VELRDSLYVI GWSYILCWCL LQLLLQQPIN
     STPILLLLVQ ILASLLYFAS NETHHKEWIE IAALYYLGMA GHFALGNSNT LATIDVAGAF
     IGISSHSTLL SGVLMFIITY ASPMFILLSL VMYISMKNTA HLVIPEKADA GDLLMMMLGF
     PCLVPLVFNS ILLTAYTVVL LLMRNHLFVW SVFSPKYLYV CATTLCTYIG VSIVAATGIY
     THLVLGIRKR KQVPISNNTR
//
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