ID A0A0A2L3H4_PENIT Unreviewed; 730 AA.
AC A0A0A2L3H4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=PITC_039070 {ECO:0000313|EMBL:KGO73696.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73696.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO73696.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73696.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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|ARBA:ARBA00003496,
CC ECO:0000256|RuleBase:RU365011}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU365011}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|RuleBase:RU365011}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO73696.1}.
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DR EMBL; JQGA01000780; KGO73696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L3H4; -.
DR HOGENOM; CLU_010646_0_0_1; -.
DR OMA; WKWDDAR; -.
DR OrthoDB; 70376at2759; -.
DR PhylomeDB; A0A0A2L3H4; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR48182; PROTEIN SERAC1; 1.
DR PANTHER; PTHR48182:SF2; PROTEIN SERAC1; 1.
DR Pfam; PF07819; PGAP1; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365011}; Hydrolase {ECO:0000256|RuleBase:RU365011};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protein transport {ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|RuleBase:RU365011}.
FT REGION 293..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 81796 MW; FF4D2741F4298D3A CRC64;
MDTEYELPFL QEVFSPESHK VDIIFVHGLN PSGRNDHPFQ TWTHSNGKFW PRDFLAEDIS
YARVFVYGYN SNITHPQTMS TASIKDHANT LLNLLDMERG PQMGSIPPKV IFIGHSLGGL
VIKQALLNAK EDPKYTSIRS ATSGLVFFGT PHRGAKAVEL GKIAARVARF VSKGHASNDL
LNCLEHNSLF TRQMTDRFRH QLEDYRVVSF IEGKEVQIGG VGPASVSHLV VDEESAVLGL
SGLRETQLKL DADHSQMCKV GARGPMYRLI KGNIKQLVDQ ALLSEQGFIP QSIPPSIVSS
PPPVPPRIHS NSSTPYQGQS RPSPAAQRVT GVMFNALDND PRSVRSAELK NRARWDEART
VEYEIFQEHL RSLGPDHFST LSVGYNLAEV ELETSYLEKA GEWCHWVSEN AQRVFGTKHP
LAMKTESLAA EVLCQQGKYQ EAESVCANVL ARQQMTIGED HLDTCDTRRR LGMTYNALGH
RQNAVMTAEK LTETLKRLLG ETHIRVFGSV LDALEYIISN QSRDANIQIV MRFQPDVQRA
VEMLFQIYQE LRNALGHGHP STIRALCLHG RAQSFVQQSI EASETLRRAL ASAEEALGPD
HPLTMDIVGN IGVMYALQNG YARGLLTNGP AAEAFPWLIR YLNWVEHRKG KDNPETQATL
ELLANLHFNA KEYEPAQQYY ERLVANMRRT DSNVTQRIDT QLQLCRANTK YTRRGLGSGI
GGFLSNLQRY
//
