GPI13_SCHPO
ID GPI13_SCHPO Reviewed; 918 AA.
AC O13663;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=GPI ethanolamine phosphate transferase 3;
DE EC=2.-.-.-;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 13;
GN Name=gpi13; ORFNames=pi072, SPBC27B12.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in glycosylphosphatidylinositol-anchor biosynthesis.
CC Transfers ethanolamine phosphate to the GPI third mannose which links
CC the GPI-anchor to the C-terminus of the proteins by an amide bond.
CC Involved in cell wall biosynthesis (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
CC {ECO:0000305}.
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DR EMBL; AB004539; BAA21454.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA16901.1; -; Genomic_DNA.
DR PIR; T40030; T40030.
DR RefSeq; NP_595538.1; NM_001021449.2.
DR AlphaFoldDB; O13663; -.
DR SMR; O13663; -.
DR STRING; 4896.SPBC27B12.06.1; -.
DR MaxQB; O13663; -.
DR PaxDb; O13663; -.
DR EnsemblFungi; SPBC27B12.06.1; SPBC27B12.06.1:pep; SPBC27B12.06.
DR GeneID; 2540594; -.
DR KEGG; spo:SPBC27B12.06; -.
DR PomBase; SPBC27B12.06; gpi13.
DR VEuPathDB; FungiDB:SPBC27B12.06; -.
DR eggNOG; KOG2126; Eukaryota.
DR HOGENOM; CLU_004298_1_0_1; -.
DR InParanoid; O13663; -.
DR OMA; DDTWMQL; -.
DR PhylomeDB; O13663; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:O13663; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; ISS:PomBase.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:PomBase.
DR CDD; cd16023; GPI_EPT_3; 1.
DR Gene3D; 3.40.720.10; -; 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; PTHR23071; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..918
FT /note="GPI ethanolamine phosphate transferase 3"
FT /id="PRO_0000316600"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 762..782
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 853..873
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 887..907
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 918 AA; 104993 MW; EB6870E37BDDC314 CRC64;
MEEKRVKCKK KLTSTIGTWK YIQACIFFAI ILISNFYGLK SFTDGFLLRR AVLNQTSLCE
NPPADVREWK NSSGCWAPKI FERAVIVIID ALRYDFLIPY NDSNYYHNAF TTPYETSVLH
PENSYLTQFI ADAPTTTSQR LKGLTTGSLP TFIDLGSNFA GTNIDEDNLL LQWKSLDKQI
VLLGDDTWDV LFHDYLNETL SQPAFSFNVP DLHGVDNKVN QYVFDYIKDA NFDVLIAHYL
GVDHVGHRLG PDHPTMRDKL NQMDRCVKEM MDLLDDSTLL IVMGDHGMDN KGNHGGDSFD
EINSVLWMYS KKPTFGYLKQ PGKVLSANQV DLVPTLSLLL GNPIPYGNLG TLIPEPFYYY
GDEYLSKAQK INIGQLNRFF SEYDLDASDF LSSSVHKNNN SYLDQYFLDF DYARDAFSYF
KAIWAEFSLF PMIIGFLLLI IGGFNLALLM QDKSVIFRMS ANMAPSVMKC LPVCLILILA
NNELHSPFPA EFYVLLPSFY ILLNSFNQKL MEYFKGFVKL DYFSIFITFL HVCSFGSNSF
TVWEDRLCHF LIITIGLVMF CKCFSEMSPL FACSTYSALA FILLQVISSY VTNCREEQGA
FCVSTYISTP DNSLRTLIVL ALMALSSIIL PLILQLHLRR VLGLSLKLYH LSILYFFELI
SSIFWIAHHV FANDALLEKQ YHHVLYSLAN TYVICILGVL IWQFFLLSRS KFAKINVIER
SYFVFALLYS FLSFLQRPLG HLSLFSCFLQ ILLLIQLKQW QPSVGHNFFS VTLGLLGLSH
FFTTGNQAAI SSLDWNFAFI HSKSAENQAI SAIFMFLHTV GAPILTCISI PLFSFEPLSK
KNRFLINLFR FSFSFILYNL LISTSTVFFA GFFRRHLMVW KVFAPRFMLS GILLVTHQLF
VLIQCFGSSV VKFPEDAE
