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Database: UniProt
Entry: G1SI06_RABIT
LinkDB: G1SI06_RABIT
Original site: G1SI06_RABIT 
ID   G1SI06_RABIT            Unreviewed;      1103 AA.
AC   G1SI06;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
GN   Name=PIGO {ECO:0000313|Ensembl:ENSOCUP00000002293.3};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000002293.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000002293.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000002293.3,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000002293.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000002293.3};
RG   Ensembl;
RL   Submitted (JUL-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. PIGO subfamily.
CC       {ECO:0000256|ARBA:ARBA00008695}.
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DR   EMBL; AAGW02033496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008269131.1; XM_008270909.2.
DR   AlphaFoldDB; G1SI06; -.
DR   PaxDb; 9986-ENSOCUP00000002293; -.
DR   Ensembl; ENSOCUT00000002654.4; ENSOCUP00000002293.3; ENSOCUG00000002653.4.
DR   GeneID; 100339282; -.
DR   KEGG; ocu:100339282; -.
DR   CTD; 84720; -.
DR   eggNOG; KOG2126; Eukaryota.
DR   GeneTree; ENSGT00910000144278; -.
DR   HOGENOM; CLU_004298_2_0_1; -.
DR   OMA; LGDSTWT; -.
DR   OrthoDB; 5479199at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001811; Chromosome 1.
DR   Bgee; ENSOCUG00000002653; Expressed in uterus and 14 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
DR   CDD; cd16023; GPI_EPT_3; 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; IPR037675; PIG-O_N.
DR   InterPro; IPR039524; PIGO/GPI13.
DR   PANTHER; PTHR23071:SF1; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 3; 1.
DR   PANTHER; PTHR23071; PHOSPHATIDYLINOSITOL GLYCAN; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
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:UP000001811};
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        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        467..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        491..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        520..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        559..579
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        680..700
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        715..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        746..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        843..862
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        869..891
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        956..975
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1030..1050
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1062..1084
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          981..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        983..997
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1103 AA;  120130 MW;  BAA8FF320F16B2F8 CRC64;
     MRWLGSGTVY LQMQKVSVLL FLAWVCLLFY AGIALFTSGF LLTRLELTNH SSCQEPPGPG
     SLPWGHRGQP GACWMAAQFS RVVLVLIDAL RFDFAQPQRS HGSGEPPASL PFLGKLGSLQ
     RILETEPHRA RLYRAQVDPP TTTMQRLKAL TTGSLPTFVD AGSNFASHAI VEDNLIKQLN
     SAGRRIVFMG DDTWKALFPG AFSQAFFFPS FNTRDLHTVD NGILEHLYPT MDSGEWDVLI
     AHFLGVDHCG HRHGPHHPEM AKKLSQMDQV IQGLVERLEN DTLLVVAGDH GMTVSGDHGG
     DSELEVSAAL FLYSPTALFP STPPEEPEVI PQISLVPTLA LLLGLPIPFG NIGEVIAELF
     SGGKDSQPLS SALAQASALH INAQQVSRFL HTYSAATQDF HVEELRRLQN LFSKASADYQ
     WLLKNPQGAE ETLKAVTAEL QQFLRGARAV CIEFWARFSL VRMAGGAALL AAACFLCMLA
     SQWATSPAFP FYSLLLMPVA WGVTGAVVCA GLLATTGLKL DAVVLAAVAA VGSLLPFLWK
     AWAGWGPRRP LTSLLPIPRP ILLLLLIRLA AFFSDSFVVA EAKATPFLLG SLILLLVVQL
     HWEGQMLPPK LLTIPRLGSS APTGLPRHSG TYALRLGVGL LLCTRLAGLF HRCPEETPAC
     HSSPWLNPLA SMVGGRAKNL WYGACVGALV ALLAAVRLWL RHYGNLKSPE PPVLFVRWGL
     PLMALGTAAY WALASGAEEA PPRLRALVAG ASAVLPRAVV GLAAAGLVLL LWRPVTVLVK
     AGASAPRTRT VLTPFSGPPT SQADLDYVVP QIYRHMQEEF RGRLERTRSE GPLTVAAYQL
     GSVYSAAMVT ALTLLAFPLL LLHTERISLV FLLLFLQSFL LLHLLAAGIP VPRPGPFTVP
     WQAVSAWALM ATQTFYSTGH QPVFPAIHWH AAFVGFPEGH GSSTWLPALL VGANTFASHL
     LFAVGCPLLL LWPFLCESQG PKRRQHPPGH EAEAKVRPEE EEEEEPLMEM RLREAPHHFN
     AALLQLGLKY LFVLGVQILA CVLAASILRR HLMVWKVFAP KFIFEALGFI VSSVGLLLGI
     ALVMRVDGAV SSWFRQLVLS QQR
//
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