ID   PGAP3_CRIGR             Reviewed;         320 AA.
AC   A2V7M9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 42.
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   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17314402; DOI=10.1091/mbc.e06-10-0885;
RA   Maeda Y., Tashima Y., Houjou T., Fujita M., Yoko-o T., Jigami Y.,
RA   Taguchi R., Kinoshita T.;
RT   "Fatty acid remodeling of GPI-anchored proteins is required for their raft
RT   association.";
RL   Mol. Biol. Cell 18:1497-1506(2007).
CC   -!- FUNCTION: Involved in the lipid remodeling steps of GPI-anchor
CC       maturation. Lipid remodeling steps consist in the generation of 2
CC       saturated fatty chains at the sn-2 position of GPI-anchors proteins.
CC       Required for phospholipase A2 activity that removes an acyl-chain at
CC       the sn-2 position of GPI-anchors during the remodeling of GPI.
CC       {ECO:0000269|PubMed:17314402}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:17314402}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:17314402}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:17314402}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:17314402}. Note=Mainly localizes to Golgi
CC       apparatus.
CC   -!- SIMILARITY: Belongs to the PGAP3 family. {ECO:0000305}.
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; AB288236; BAF47369.1; -; mRNA.
DR   RefSeq; NP_001233642.1; NM_001246713.1.
DR   AlphaFoldDB; A2V7M9; -.
DR   STRING; 10029.NP_001233642.1; -.
DR   Ensembl; ENSCGRT00001029015; ENSCGRP00001024769; ENSCGRG00001022580.
DR   GeneID; 100689454; -.
DR   KEGG; cge:100689454; -.
DR   CTD; 93210; -.
DR   eggNOG; KOG2970; Eukaryota.
DR   GeneTree; ENSGT00390000001304; -.
DR   OMA; FMIEDCR; -.
DR   OrthoDB; 828384at2759; -.
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; IMP:UniProtKB.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006505; P:GPI anchor metabolic process; IMP:UniProtKB.
DR   InterPro; IPR007217; Per1-like.
DR   PANTHER; PTHR13148; PTHR13148; 1.
DR   Pfam; PF04080; Per1; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   GPI-anchor biosynthesis; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..320
FT                   /note="Post-GPI attachment to proteins factor 3"
FT                   /id="PRO_0000339355"
FT   TOPO_DOM        21..98
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..169
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..223
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..282
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..320
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   320 AA;  36824 MW;  2F53116C7662B1AD CRC64;
     MAERTARLLL LTVTVGLAWG SQGDREPVYR DCVLRCEERN CSGDALKHFR SLQPIYMSLA
     GWTCRDDCKY ECMWITVGLY LQEGHRVPQF HGKWPFSRFL FIQEPASAVA SLLNGLASLV
     MLCRYRASVP ASSPMYHTCM AFAWVSLNAW FWSTVFHTRD TDLTEKMDYF CASAVILHSI
     YLCCVRTVGL QHPSVARAFG ATLLLMLLLH TSYLSLVRFD YSYNMMANVA IGLVNLAWWL
     AWCLRNHRRL PHTRKCVAVV LLLQGLSLLE LLDFPPLFWV LDAHAIWHIS TIPVHVLFFR
     FLEDDSLYLL KESEAKFKLD