ID   PGAP3_BOVIN             Reviewed;         319 AA.
AC   A7YWP2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Mainly
CC       localizes to Golgi apparatus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PGAP3 family. {ECO:0000305}.
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DR   EMBL; BC134683; AAI34684.1; -; mRNA.
DR   RefSeq; NP_001098833.1; NM_001105363.1.
DR   AlphaFoldDB; A7YWP2; -.
DR   STRING; 9913.ENSBTAP00000034758; -.
DR   PaxDb; A7YWP2; -.
DR   PRIDE; A7YWP2; -.
DR   Ensembl; ENSBTAT00000034874; ENSBTAP00000034758; ENSBTAG00000011732.
DR   GeneID; 513258; -.
DR   KEGG; bta:513258; -.
DR   CTD; 93210; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011732; -.
DR   VGNC; VGNC:32783; PGAP3.
DR   eggNOG; KOG2970; Eukaryota.
DR   GeneTree; ENSGT00390000001304; -.
DR   HOGENOM; CLU_032917_1_0_1; -.
DR   InParanoid; A7YWP2; -.
DR   OMA; FMIEDCR; -.
DR   OrthoDB; 828384at2759; -.
DR   TreeFam; TF300031; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000011732; Expressed in pigment epithelium of eye and 105 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; IBA:GO_Central.
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   Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   GPI-anchor biosynthesis; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..319
FT                   /note="Post-GPI attachment to proteins factor 3"
FT                   /id="PRO_0000339354"
FT   TOPO_DOM        24..101
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..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..200
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..224
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..257
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..281
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..319
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   319 AA;  36056 MW;  F603E7201AF72979 CRC64;
     MAGRTARLVL LAGAAALASG SQGDREPVYR DCVLRCEERN CSGGALKHFR SRQPIYMSLA
     GWTCRDDCKY ECMWVTVGLY LQEGQKVPQF HGKWPFSRFL CFQEPASAVA SFLNGLASLV
     MLCRYRTSVP ASSPMYPTCV AFAWVSLNAW FWSTVFHTRD TDLTEKMDYF CASTVILHSI
     YLCCVRTVGL QHPAMASAFR ALLLLLLTAH VSYLSLIHFD YGYNMAANVA IGLLNAAWWL
     AWCLWNQRLP HVHKCVAVVL LLQGLSLLEL LDFPPLFWVL DAHAIWHIST IPVHVLFFSF
     LEDDSLYLLK ESEAKVKLD