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Database: UniProt
Entry: A0A1U8NRZ6_GOSHI
LinkDB: A0A1U8NRZ6_GOSHI
Original site: A0A1U8NRZ6_GOSHI 
ID   A0A1U8NRZ6_GOSHI        Unreviewed;       973 AA.
AC   A0A1U8NRZ6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830};
GN   Name=LOC107950408 {ECO:0000313|RefSeq:XP_016740739.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016740739.1};
RN   [1] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [2] {ECO:0000313|RefSeq:XP_016740739.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016740739.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_016740739.1; XM_016885250.1.
DR   AlphaFoldDB; A0A1U8NRZ6; -.
DR   STRING; 3635.A0A1U8NRZ6; -.
DR   PaxDb; 3635-A0A1U8NRZ6; -.
DR   GeneID; 107950408; -.
DR   KEGG; ghi:107950408; -.
DR   OrthoDB; 5479199at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000189702; Chromosome 7.
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:UP000189702};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679,
KW   ECO:0000313|RefSeq:XP_016740739.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..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..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        548..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        587..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        635..653
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        665..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        755..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        779..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        809..841
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        847..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        892..915
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        935..963
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          524..656
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
FT   DOMAIN          770..955
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
SQ   SEQUENCE   973 AA;  108122 MW;  3ED1B37994A28304 CRC64;
     MAPLTCTKLS LITIAGVVTQ IIGLSFFVFG FFPVKPALPG TSGSESFYVP ACDFVSNQSD
     TTLPSDQLKS LYQELSGIPP SFDRLILMIV DGLPAEFVFG KDGKPPNKQF KEAMPYTQSL
     LASGSAIGYH AKAAPPTVTM PRLKAMVSGA IGGFLDVAFN FNTQAMTDDN LLGQFFKIGR
     KMVMLGDETW LKLFPGLFKR HDGVSSFYVK DTVQVAQNAS RHLGDELSKD DWDLLILHYL
     GLDHVGHIGG RNSVLMTPKM KEMDEVVKLI HSSINQSQGN GLGRTLLMIV SDHGMTENGN
     HGGSTYEETD TLALFIGLRN HVFDYASVIN QIDIAPTLAL LFGVPIPKNN VGVLIREAFD
     SLKEDKHLRA LELNSWQLLR LLQAQLSGLP CRNFPCDAFY DHQSSGSTDC NHETEDMLCC
     LYMEATTLYT SWKSKRGFES ASNKYYSSAA AAYYKFLKSA SEWLSRRSTD KPVKLLALGL
     ATMFVSTVIL SSLMFCRLRE IYHGGKQQSL NLNDSMNGWS LDETFILSVI LILVSSMTSS
     SMVEEEHYIW YFLISTFYLL LLRKTAQSLC VVRLQSSFFT QNGQSREGYF RICFVFLLLT
     SGRVLRGWHQ GGVNWTSLPD ISKWLEQAGS QHVKSLQLIS AFLVISIGLF ALFSIESKGK
     CFQMVRLSFL ISGLLVLLHI TKYQDYTFSS TNYGATLLVQ IIYAILGVAT IGTVVALPWV
     IPFSTSKICP TDNTISPLFL SIHEKFPLVE LRDSLYVIGW AYVLCWCLLQ LLLQQPINTT
     PILLLLLQIL AGTLYFARSG THHKEWVEIA AFYYLGMAGH FALGNTNTLA TIDVAGAFIG
     ISSHSTLLSG ILMFIITYAS PMFILLSLVM YISMKNMAHP VIPEKAGPGD HLMMMLGFSC
     LIPLVINSIL LTAYTVVLLL MQNHLFVWSV FSPKYLYVCA TAVCTYIGVF IVAATGFYAY
     FVLVMRKQKP YSC
//
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