ID U5GZV3_USTV1 Unreviewed; 1187 AA.
AC U5GZV3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 28-JUN-2023, entry version 41.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=MVLG_00698 {ECO:0000313|EMBL:KDE08975.1};
OS Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE08975.1};
RN [1] {ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KDE08975.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE08975.1};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KDE08975.1, ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE08975.1}, and p1A1 Lamole
RC {ECO:0000313|Proteomes:UP000017200};
RX PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA Hood M.E., Schultz D.J., Cuomo C.A.;
RT "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT fungus.";
RL BMC Genomics 16:461-461(2015).
RN [4] {ECO:0000313|EnsemblFungi:MVLG_00698T0}
RP IDENTIFICATION.
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU365011}.
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DR EMBL; AEIJ01000063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL541646; KDE08975.1; -; Genomic_DNA.
DR AlphaFoldDB; U5GZV3; -.
DR STRING; 683840.U5GZV3; -.
DR EnsemblFungi; MVLG_00698T0; MVLG_00698T0; MVLG_00698.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; U5GZV3; -.
DR OMA; WVRNLAV; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000017200; 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:UP000017200};
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 59..82
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 804..825
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1024..1047
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1091..1111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 128847 MW; FD7E08350DE22FA8 CRC64;
MPDPAGVASQ EPGLLSSTRS TIAPDALDAA TTATTARPKS AGYVVHAATN RSSFGRTPLA
GFVAIVLVSL VALVTVLLAH VASPPRYPPG SLPPDAKGGG AGACRQSWMS PSYLHISGTS
LPLFRLWSSR VPEAHARFFV ARSPSPSPLT SPAPNPDSTA FGREYSRLGA GPWGLYLYRE
EGWDDDPFEP HVGHGAASTD PTPRAFALTG IPVIFVPGNA GSFRQVRSLA SAASRAYYEL
PGVRRKGMGS KEGGRPLDFF TLDFNDDFSA FHGQTLLDQA EYLADSIRYI LSLYHQESNA
KQGRPDPTSV IVIGHSMGGI VARAALLHPH YQSGSISTLV TIATPHAVPP VTVDRGVDRV
YDNINSYWRR AHHLEAMSSP PSRRDLRGEA ELSNLVLVSI SGGISDTTIA SESASLTSIM
PLNDSHGFTV FTTAIPGVQT PIDHLAMLWC RQLMETVATA LLVIVDVRSP LGVLPREARV
GKLAERLLGA IESHPVKPEG RKSTLESLER GQHGRELAIG ERLSLRGHGD KRSTFVLPIP
PRRTYGSARV FSLLTSANIG RSLDSLVEVY ACGKNESAPE STHSSSCTSL FPSFVTTIPI
SPHSAQSPIL PAPAEDGTMA FLDVDVSQLE SQDVIVVVVK PGNAWLLAEF GDKDRRVHTV
DKSAFQLMLG GFKIENFPTT PSLISELWLP TLDSSLLTFK MKVFRSDCQD SSTVLFAPLL
RQYSSLLHET KYFPNVREAS LYTHASGPYL PAPASPFVSP GARLQLIVDP TCARENSRAS
ADVAIEIKLD LWASLGNLAM RYRMAVVAFP FALILLVFAC QLRDYNSGHC FPPFATALGT
FTRHHLMPLL GSLVALSFLQ SVMLGTRLSF VEAKLASADA HVLPSLPPRW ISEMLLGNQG
PFFAFLGAFI LFTMLSVVVL EYAALYLLVT VLARLVRLIR QRGPSQMRSF VTLVEPRETL
PLQRIVTMGA LVLFVLFFAP YQFAFLVLFL VHLLSTVRAL LLAQDASAPS TPASTRRLWD
RYHYSFVSLL VMIGLLPINA MILAVWVRNL AVGWLAPFST DHNVLNILGF LLNVEALHSG
KMLQRTPGPT ASTVSIALPL IAAGFALLYG IRWTYNIYPL ANAFFLWLAS NHSHHLVGAL
NEAVKAKRRL SISTAGQHVQ SNSVKQLSSS ALSPSPAPRT PTKRQFL
//
