ID W5MD90_LEPOC Unreviewed; 944 AA.
AC W5MD90;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN Name=PGAP1 {ECO:0000313|Ensembl:ENSLOCP00000006349.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000006349.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000006349.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins.
CC GPI inositol deacylation may important for efficient transport of GPI-
CC anchored proteins from the endoplasmic reticulum to the Golgi.
CC {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; AHAT01028899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01028900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MD90; -.
DR STRING; 7918.ENSLOCP00000006349; -.
DR Ensembl; ENSLOCT00000006357.1; ENSLOCP00000006349.1; ENSLOCG00000005267.1.
DR eggNOG; KOG3724; Eukaryota.
DR GeneTree; ENSGT00390000016484; -.
DR HOGENOM; CLU_013735_1_0_1; -.
DR InParanoid; W5MD90; -.
DR OMA; YGLYYYY; -.
DR Proteomes; UP000018468; Linkage group LG12.
DR Bgee; ENSLOCG00000005267; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050185; F:phosphatidylinositol deacylase activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central.
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:UP000018468};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..944
FT /note="GPI inositol-deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004867633"
FT TRANSMEM 329..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 698..722
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 750..778
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 839..861
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 873..889
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 901..921
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
SQ SEQUENCE 944 AA; 105371 MW; 53F5DF6FD330994B CRC64;
MRFVAVAFYG CLLALLAVGL RDLLLGYEEN RCSMTYMFEY PEYLRIQLPH RVSQRYPGYG
LYLYGEGLYA QHSHSLKLSG VPVLFLPGNA GSYKQARSLG SIALRKAEDI DNGFHLNVFT
IDFSEELVAL YGGSLQRQTR FVHESIKAIL RLYKDQETPP RSVAVVGHSM GGIVARALFT
LPKFSPHLVS LILTQASPHQ GPVLPLDRHL LEFYSAVRRR WSLGTGDLRN VTVLSVGGGY
RDYQVRSGLT ALPCPPNDPN KLSLVSTAVP RTWVSTDHLS IVCVCCWCKF LLCARAVNVF
IFGNPDSAQI FAFSYKNLSI IYYNYYNKAF VYLLGSPWLN FFFYFFHSVQ EPRARYFIFP
LSSRRKSHSH FHCQNSNLEM TSWLFGCTQS NGSMCRQAVD LSWDTELLPA YKVVTVKLSD
LSSFSHLVLS ASSLNGGQFS VECEWFSEDS RTASVPVPHI LSFGMSIREV TLSSPALFHT
VELLDFHQVY QAFKVTIESQ CKGTRGKDFF TLSDSSELVI EGRLPSVYRL QVPWFREDSF
TAASVPSVTE IFAKLHTSRP DNSSSAILQL HTSPDCQYKV SVQTSFFQVL GQVLRFCGPV
LPVYMAVCIL LACEGQVYSL IHTGRPVELA EALGESTQLH RVELLVSLLH LLLRLSWFRA
GWSALCLPLV DTLPLTALDH GVLESSEPLS PAEGWTRLVS LFLLLLGAAV AFWGGALFRL
SLELLSWILS PLHRPSIIQD NGHPLTRSRI ILIVTLGLVA WATCGALALV AVYFLYLYKV
MRLQMSERTL KHVLNLAPRE KVREAGGSAG QGEAHPAGSN SLITVSALEK VQDNLQLHLS
LSVLLTLPVM LSAPSLIHWL RSLRHSLQLN PDPCWPVVLP LIVSSTILMN SNTHTLCCSK
LLAVICRLQL PVCVSMVTFS LMHLYRVTYF LSLSLALHAL CCLI
//
