ID Q22SA5_TETTS Unreviewed; 1365 AA.
AC Q22SA5;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=TTHERM_00006310 {ECO:0000313|EMBL:EAR87867.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR87867.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins
CC which plays important roles in the quality control and ER-associated
CC degradation of GPI-anchored proteins. {ECO:0000256|RuleBase:RU365011}.
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 GPI inositol-deacylase family.
CC {ECO:0000256|ARBA:ARBA00006931, ECO:0000256|RuleBase:RU365011}.
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DR EMBL; GG662845; EAR87867.2; -; Genomic_DNA.
DR RefSeq; XP_001008112.2; XM_001008112.3.
DR STRING; 312017.Q22SA5; -.
DR ESTHER; tetts-q22sa5; PGAP1.
DR EnsemblProtists; EAR87867; EAR87867; TTHERM_00006310.
DR GeneID; 7832668; -.
DR KEGG; tet:TTHERM_00006310; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_258893_0_0_1; -.
DR InParanoid; Q22SA5; -.
DR OrthoDB; 5702444at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1.
DR PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365011};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365011};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365011};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365011}.
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1088..1110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1130..1150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1156..1174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1186..1202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1237..1254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1274..1294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1306..1324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1330..1348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 55..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1365 AA; 163360 MW; F1C2D17E67702360 CRC64;
MQKKKKLHNK TKSSQKNKIQ FIQESKSRKR FIQINQIQFF YSISRFHKQA WMKNKGNNNK
KKQRVQNSTN GQGGQDHHIQ NQNYHTNQQN TVNQHYFQTQ GQFVAGQNKN QSQIMLEEIE
KNKRKYQEMI MRKRQWLQQQ QMMQGANSKV ENYQMHIEQQ EDFDLIDSYE DYDGYYEDDI
YDELQDQNSN QNQNENGQQN LEDDTSNLQD QLVQCTYKIF LGFILFGCVL FVYILYTTLS
PSMESNLKMQ ILKTVKSKQT QPSFYETQIF PQSLYQDYPF KLFSYEDKDI ASYLNQPISQ
FYCNLLLESG NAADCENCQY LKDRNSNKNS QESSKQFKGT FYKVPQETDN TKKSDQAQDI
EYLQQSNREN DELKQEDQSQ FQTVYQNFQE NESQQCYIKN KFFFEETYIP ILYIHGHGKG
NPQQINSLNH QLQKLLIYEN EKNLQQQKYF QKDQKNKLKQ FKFYAMDFKN ALSAFSITLI
EKEQASVQRA IQYITSKTSE KLILVCHSMG GFVCLNVLSQ MQEELVVKIQ QVIFLNSPLT
QHPLNSNTAF SDKYKNMYKQ LNEIKNLLQD ITFLSFTSGS SDNQVIPEET YLKLKLKNSA
HFNTQELRDV FVTLHHDDIL TYTPFLSLLS KYFIMDRYYN VFQKDINMIK HYFKQFDIHY
EDQINRNYFS FNKKHLDAEC AQFMPKFEQS QTFDLLQVGR KLNFPKQSIP EDPSSDPRSY
LNKENLLCVK ILTQNIKASN LIYYMRTNLP SQNIKIFTYR PKPFFFLRQN NKKSGFEFME
DETINVRIEP NQNERQDPHY QERIIRFNKN EHFEMEEIFP DFSYFFSTVY LHSHYPKNKE
LYLIYTIRND TYLQYEYQQL YNVTYLHTNL FFSIQNYQDS EKITLPFNKI KKEEWKSNQQ
ILKAKIEEVD DVYFYKYCSQ TQGGLFSWFS SQQSKLTQFE KWNKIDYNLL ILKNQNMNSR
LHISFSYGEN DCDYVNILNT QNKDLILVHD TKSHDIYNMF LKDKSVNEQR AWYQNTNNMQ
QRSGSQVMLS QENNLNEYSR SIGKFSKVII LNMHVILCCM LISIQIKYYE PSCYQDAPSH
INILCSNLTK FVLCYGLTIF SIISLQKWLF NDEMREQQNY NNYNMQSVEY YASSFLTSFI
ITFITISTYI LVQFVFQVFS FFSYLVCSLI KYILTQSKLI KRFAQSKYFF FLNAITLFMP
LIFLTNYYLK WIILFAVFWI LLGVLQGNKT DYGHSNNILH GFAYLMFLYF ILNIHNLLAG
QIQLQNSHKL FKNLMFTEEF TSEFFTMVCW FFILTRLENL IGNLRTPLQI IFILLSLFLF
FFLFQSVQHA NYYLCNLSYL LMFFAIYYHN QKAPIVAQIP QNQQY
//
