PGAP3_XENLA
ID PGAP3_XENLA Reviewed; 317 AA.
AC Q68EV0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Post-GPI attachment to proteins factor 3;
DE AltName: Full=PER1-like domain-containing protein 1;
DE Flags: Precursor;
GN Name=pgap3; Synonyms=perld1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the lipid remodeling steps of GPI-anchor
CC maturation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PGAP3 family. {ECO:0000305}.
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DR EMBL; BC080100; AAH80100.1; -; mRNA.
DR RefSeq; NP_001087556.1; NM_001094087.1.
DR AlphaFoldDB; Q68EV0; -.
DR DNASU; 447380; -.
DR GeneID; 447380; -.
DR KEGG; xla:447380; -.
DR CTD; 447380; -.
DR Xenbase; XB-GENE-947222; pgap3.L.
DR OrthoDB; 828384at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 447380; Expressed in testis and 19 other tissues.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; ISS:UniProtKB.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006505; P:GPI anchor metabolic process; ISS:UniProtKB.
DR InterPro; IPR007217; Per1-like.
DR PANTHER; PTHR13148; PTHR13148; 1.
DR Pfam; PF04080; Per1; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..317
FT /note="Post-GPI attachment to proteins factor 3"
FT /id="PRO_0000339359"
FT TOPO_DOM 19..93
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..163
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..219
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 317 AA; 37085 MW; B689D53CB7F82041 CRC64;
MAPFLVLFLA GVVSASRGDR EPVYRDCVTV CDQNNCTGFR LRDFRAQQPL YMRLTGWTCL
DDCRYKCMWY TVSLYLKEGH EVPQFHGKWP FSRFLFFQEP ASALASFLNG VASLLMLFRY
RSSVPSSCQM YRTCLAFSMV SVNAWFWSTI FHTRDTALTE KMDYFCASSV ILHSIYLCCM
RTFGLQYPSI ANAFGAFLVL LFACHISYLT LGRFDYSYNM AANTSFGIVN LMWWLAWCMW
RRFHQPYLWK CVLVVVLLQS LALLELLDFP PVMWILDAHA LWHFSTIPLH FLFYSFLRDD
SLYLLKVNHD DDIPKLD