ID G1SH11_RABIT Unreviewed; 882 AA.
AC G1SH11;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN Name=PGAP1 {ECO:0000313|Ensembl:ENSOCUP00000001895.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000001895.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000001895.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000001895.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000001895.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001895.3};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU365011}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAGW02003273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02003274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SH11; -.
DR Ensembl; ENSOCUT00000002196.4; ENSOCUP00000001895.3; ENSOCUG00000002192.4.
DR eggNOG; KOG3724; Eukaryota.
DR GeneTree; ENSGT00390000016484; -.
DR HOGENOM; CLU_013735_1_0_1; -.
DR TreeFam; TF314565; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000002192; Expressed in prefrontal cortex and 16 other cell types or tissues.
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:UP000001811};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 667..689
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 734..758
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 819..838
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 777..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 100698 MW; A85C4209F0A26E2C CRC64;
MFLHSVNLWN LAFYVFMVFM ATVGLWDVFF GFEENKCSMS YMFEYPEYQK IELPKKLAKR
YPAYELYLYG EGSYAEEHKI LPLTGIPVLF LPGNAGSYKQ VRSIGSIALR KAEDIDFKYH
FDFFSVNFNE ELVALYGGSL QKQTKFVHEC IKTILKLYKG QEFAPKSVAI IGHSMGGLVA
RALLTLKNFK QDLINLLITQ ATPHVAPVMP LDRFITDFYM TVNNYWILNA RHINLTTLSV
AGGFRDYQVR SGLTFLPKLS HHTSALSVVS SAVPKTWVST DHLSIVWCKQ LQLTTIRAFF
DLIDADTKQI TQNPKKKLSV LNHHFIRHPA KHFEENPSII SDLTGTSMWV PVKVSRWTYV
AYNESDKIYF TFPLANHRKI YTHVYCQSTM LDTNSWIFGC INSTSMCRQG VDLSWKAELL
PTIKFLTLRL QDYPSLSHLV VYVPSIHGSK FVVDCEFFKK ETRSIQLPVT HLFSFGLSSR
KVVLNTSGLY YNIELLNFGQ IYQAFKINVV SKCSGVREEI TSIYKLHIPW SYEDSLTIAQ
VPSSTEISLK LHIAQPENDS HVALLKMYTS SDCQYEVTVK TSFSQILGQV VRFHGGALPA
YVISSILLAY GGQLYSLFST GSCLEYAVML DKEAKPYKVD PFVIMVKFLL GYKWFKELWD
ALMLPELDAI VLTSQSMCFP LVSLILFLFG TCTAYWSGLV SSTSVRLLSS LWLAMKRPSE
LPKDIKMLSP DLPFLTIVLI IVSWTTCGAL AILLSYFYYV FKIVHLQACL TTFKNNQPVN
PKHSRRSEKK SNHHKDSAVH HLRLSANDAE DSLRMHSTVI NLLTWIVLLS MPSLIYWLKN
LKYYFKLNPD PCKPLAFILI PTMAILGNTY TVSVKSRKQD TL
//
