ID   PGAP4_RAT               Reviewed;         403 AA.
AC   Q5EB73;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Post-GPI attachment to proteins factor 4 {ECO:0000305};
DE   AltName: Full=Post-GPI attachment to proteins GalNAc transferase 4 {ECO:0000305};
DE   AltName: Full=Transmembrane protein 246;
GN   Name=Pgap4 {ECO:0000312|RGD:1307218}; Synonyms=Tmem246;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Golgi-resident glycosylphosphatidylinositol (GPI)-N-
CC       acetylgalactosamine transferase involved in the lipid remodeling steps
CC       of GPI-anchor maturation. Lipid remodeling steps consist in the
CC       generation of 2 saturated fatty chains at the sn-2 position of GPI-
CC       anchors proteins. Required for the initial step of GPI-GalNAc
CC       biosynthesis, transfers GalNAc to GPI in the Golgi after fatty acid
CC       remodeling by PGAP2. {ECO:0000250|UniProtKB:Q9BRR3}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9BRR3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9BRR3}.
CC   -!- DOMAIN: Contains three transmembrane domains, including a tandem
CC       transmembrane domain insertion into its glycosyltransferase-A fold.
CC       Transmembrane domain 1 functions as a signal for Golgi targeting.
CC       {ECO:0000250|UniProtKB:Q9BRR3}.
CC   -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC       {ECO:0000250|UniProtKB:Q9BRR3}.
CC   -!- SIMILARITY: Belongs to the PGAP4 family. {ECO:0000305}.
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DR   EMBL; BC089972; AAH89972.1; -; mRNA.
DR   RefSeq; NP_001014212.1; NM_001014190.1.
DR   RefSeq; XP_006238220.1; XM_006238158.3.
DR   RefSeq; XP_006238221.1; XM_006238159.3.
DR   RefSeq; XP_017448961.1; XM_017593472.1.
DR   RefSeq; XP_017448962.1; XM_017593473.1.
DR   RefSeq; XP_017448963.1; XM_017593474.1.
DR   AlphaFoldDB; Q5EB73; -.
DR   STRING; 10116.ENSRNOP00000008883; -.
DR   PaxDb; Q5EB73; -.
DR   Ensembl; ENSRNOT00000008883; ENSRNOP00000008883; ENSRNOG00000006800.
DR   Ensembl; ENSRNOT00000104584; ENSRNOP00000097268; ENSRNOG00000006800.
DR   GeneID; 362518; -.
DR   KEGG; rno:362518; -.
DR   UCSC; RGD:1307218; rat.
DR   CTD; 84302; -.
DR   RGD; 1307218; Pgap4.
DR   eggNOG; ENOG502QT3K; Eukaryota.
DR   GeneTree; ENSGT00500000045018; -.
DR   HOGENOM; CLU_049086_0_0_1; -.
DR   InParanoid; Q5EB73; -.
DR   OMA; RDYVFCL; -.
DR   OrthoDB; 864176at2759; -.
DR   PhylomeDB; Q5EB73; -.
DR   PRO; PR:Q5EB73; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000006800; Expressed in colon and 20 other tissues.
DR   Genevisible; Q5EB73; RN.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR029675; PGAP4.
DR   PANTHER; PTHR31410; PTHR31410; 1.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..403
FT                   /note="Post-GPI attachment to proteins factor 4"
FT                   /id="PRO_0000089734"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRR3"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..264
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRR3"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        286..287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRR3"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..403
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRR3"
FT   MOTIF           211..213
FT                   /note="DXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRR3"
SQ   SEQUENCE   403 AA;  46592 MW;  0F8E8D316C752930 CRC64;
     MTTSTSPAAM LLRRLRRLSW GSTAVQLFIL TVVTFGLLAP LACHRLLHSY FYLRHWHLNQ
     MSQDFLQQSL KEGEAALHYF EELPSANGSV PIVWQATPRP WLVITIITVD RQPGFHYVLQ
     VVSQFHRLLQ QCGPQCEGHQ LFLCNVERSV SHFDAKLLSK YVPVANRYEG TEDDYGDDPS
     TNSFEKEKQD YVYCLESSLQ TYNPDYVLMV EDDAIPEEQI FPVLEHLLRA RFSEPHLQDA
     LYLKLYHPER LQHYINPEPM RILEWVGVGM LLGPVLTWIY MRFACRPGFS WPVMLFFCLY
     SMGLVELVGR HYFLELRRLS PSLYSVVPAS QCCTPAMLFP APAARRTLTY LSQVYCHKGF
     GKDMALYSLL RAKGERAYVV EPNLVKHIGL FSSLRYNFHP SLL