ID A0A163BCH6_PHYB8 Unreviewed; 927 AA.
AC A0A163BCH6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
DE Flags: Fragment;
GN ORFNames=PHYBLDRAFT_10352 {ECO:0000313|EMBL:OAD80621.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD80621.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; KV440971; OAD80621.1; -; Genomic_DNA.
DR RefSeq; XP_018298661.1; XM_018427770.1.
DR AlphaFoldDB; A0A163BCH6; -.
DR STRING; 763407.A0A163BCH6; -.
DR GeneID; 28988676; -.
DR VEuPathDB; FungiDB:PHYBL_10352; -.
DR InParanoid; A0A163BCH6; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000077315; 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:UP000077315};
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 599..620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 632..656
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 695..716
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 721..743
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 763..789
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 810..835
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 850..867
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 879..900
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OAD80621.1"
FT NON_TER 927
FT /evidence="ECO:0000313|EMBL:OAD80621.1"
SQ SEQUENCE 927 AA; 104921 MW; C07B1C8D999A84B3 CRC64;
LLAIGCIAII LDSFVNHQRD VSGCRDSYTR PLFIQQTGFD SEMTRFAGKY ALYLYREKGI
DTVGQLTGVP VLFIPGHAGS YKQMRSIATE ASYYYYDNYT RQHESWENGK RSLDFFTVDF
NEEFSALHGQ SLLEQAEYLN DCIDYILKLY PQSRKLGPKM NENLPDPNSV IIVGHSMGGI
VARAMFTINN YQPGTINTVL TLSSPHLLPP VPFDWKISKL YDDIYKEWHN GFSHDTSHGV
HSLKDVSLVS IAGGTLDTII CSDSANVATF IPPTNGFTVF STAVPHVWTG TDHNSILSCS
QLIKVVAKAL LDCVDARRAT QTKPLEDRMK IMRKAFLSGL EDRQGNAHVS GISQGAFSIL
TDQSIDTSKQ FDILLCNKLN QQMPDTTRVG CRPARSIAVP VPASSYKDTD SFSGNTFTFA
SIAFAEMLEY EYLAIAHRPS LDGFLIAEAF DMQDTHQTID DPMVSIARHS LKIELEPALF
SSVRIPAIEN PMLAYHLKVS RPQCKQNEGM FAPFLRQSIS TMHESKFHVN LASGNKAETE
VSLHGRTAFS SISINSLKES QQGLVLQVWM DPVCPYPLTI ELEVDWYGSA GRLGFRNGIM
LATFSFVIVI LVLASQIQCY NKTGIFPHFG NGIAYCLCRT LPIVMVLLAV CCYYQPTGYQ
NSPEKSIPLT WNHVWESRSL PVAWNDILIG NTDPFFWWLP LVGVVLSFGT VCLLWIILQL
VLWLGAALCS LFYSVQIPCR IYSRSNETPY QRHQRRAITT LVLFALVATC IPYQFVFVVA
FLVHIITCIR SLLRTWTALP AQEQKRLNRY NYMQSIMFLF ITLLPFNLPI LLVWIRNLSV
HWFVPFSSDH SVMAIAPFML YVELLTGNHK MLPRLNSRYW NWATYLILYS IVVYAFLYGI
KYTHSLYFIS NHLVCWFLLL HFGDSGY
//
