PGAP4_MOUSE
ID PGAP4_MOUSE Reviewed; 403 AA.
AC Q91YV9; Q3TN50; Q9CYX3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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|MGI:MGI:1914313};
GN Synonyms=Tmem246 {ECO:0000312|MGI:MGI:1914313};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, Hypothalamus, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary tumor;
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; BC013800; AAH13800.1; -; mRNA.
DR EMBL; AK013226; BAB28725.1; -; mRNA.
DR EMBL; AK038514; BAC30023.1; -; mRNA.
DR EMBL; AK039788; BAC30454.1; -; mRNA.
DR EMBL; AK042679; BAC31328.1; -; mRNA.
DR EMBL; AK045523; BAC32406.1; -; mRNA.
DR EMBL; AK075994; BAC36105.1; -; mRNA.
DR EMBL; AK165526; BAE38239.1; -; mRNA.
DR CCDS; CCDS18177.1; -.
DR RefSeq; NP_080220.2; NM_025944.3.
DR RefSeq; XP_006538257.1; XM_006538194.3.
DR RefSeq; XP_006538258.1; XM_006538195.3.
DR AlphaFoldDB; Q91YV9; -.
DR STRING; 10090.ENSMUSP00000040885; -.
DR PhosphoSitePlus; Q91YV9; -.
DR MaxQB; Q91YV9; -.
DR PaxDb; Q91YV9; -.
DR PRIDE; Q91YV9; -.
DR ProteomicsDB; 259556; -.
DR Antibodypedia; 54396; 21 antibodies from 9 providers.
DR DNASU; 67063; -.
DR Ensembl; ENSMUST00000042750; ENSMUSP00000040885; ENSMUSG00000039611.
DR GeneID; 67063; -.
DR KEGG; mmu:67063; -.
DR UCSC; uc008svx.2; mouse.
DR CTD; 84302; -.
DR MGI; MGI:1914313; Pgap4.
DR VEuPathDB; HostDB:ENSMUSG00000039611; -.
DR eggNOG; ENOG502QT3K; Eukaryota.
DR GeneTree; ENSGT00500000045018; -.
DR HOGENOM; CLU_049086_0_0_1; -.
DR InParanoid; Q91YV9; -.
DR OMA; RDYVFCL; -.
DR OrthoDB; 864176at2759; -.
DR PhylomeDB; Q91YV9; -.
DR TreeFam; TF313998; -.
DR BioGRID-ORCS; 67063; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tmem246; mouse.
DR PRO; PR:Q91YV9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91YV9; protein.
DR Bgee; ENSMUSG00000039611; Expressed in epithelium of stomach and 258 other tissues.
DR ExpressionAtlas; Q91YV9; baseline and differential.
DR Genevisible; Q91YV9; MM.
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_0000089732"
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"
FT CONFLICT 32
FT /note="V -> G (in Ref. 1; BAB28725)"
FT /evidence="ECO:0000305"
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
