ERG28_MOUSE
ID ERG28_MOUSE Reviewed; 140 AA.
AC Q9ERY9; Q3U8G1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ergosterol biosynthetic protein 28 homolog;
GN Name=Erg28 {ECO:0000312|MGI:MGI:1915571}; Synonyms=Orf11;
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 [MRNA].
RX PubMed=10967139; DOI=10.1007/s003350010148;
RA Ottolenghi C., Daizadeh I., Ju A., Kossida S., Renault G., Jacquet M.,
RA Fellous A., Gilbert W., Veitia R.A.;
RT "The genomic structure of c14orf1 is conserved across eukarya.";
RL Mamm. Genome 11:786-788(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ERG28 family. {ECO:0000305}.
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DR EMBL; AF270646; AAG17664.1; -; mRNA.
DR EMBL; AK004480; BAB23325.1; -; mRNA.
DR EMBL; AK152230; BAE31057.1; -; mRNA.
DR EMBL; BC004591; AAH04591.1; -; mRNA.
DR CCDS; CCDS26063.1; -.
DR RefSeq; NP_067421.1; NM_021446.2.
DR RefSeq; XP_006516180.1; XM_006516117.2.
DR AlphaFoldDB; Q9ERY9; -.
DR BioGRID; 208424; 2.
DR STRING; 10090.ENSMUSP00000021676; -.
DR PhosphoSitePlus; Q9ERY9; -.
DR SwissPalm; Q9ERY9; -.
DR EPD; Q9ERY9; -.
DR jPOST; Q9ERY9; -.
DR MaxQB; Q9ERY9; -.
DR PaxDb; Q9ERY9; -.
DR PeptideAtlas; Q9ERY9; -.
DR PRIDE; Q9ERY9; -.
DR ProteomicsDB; 275770; -.
DR Antibodypedia; 51644; 65 antibodies from 15 providers.
DR DNASU; 58520; -.
DR Ensembl; ENSMUST00000021676; ENSMUSP00000021676; ENSMUSG00000021252.
DR GeneID; 58520; -.
DR KEGG; mmu:58520; -.
DR UCSC; uc007ohf.1; mouse.
DR CTD; 11161; -.
DR MGI; MGI:1915571; Erg28.
DR VEuPathDB; HostDB:ENSMUSG00000021252; -.
DR eggNOG; KOG3455; Eukaryota.
DR GeneTree; ENSGT00390000010925; -.
DR HOGENOM; CLU_114589_2_0_1; -.
DR InParanoid; Q9ERY9; -.
DR OMA; SEWLIFG; -.
DR OrthoDB; 1590576at2759; -.
DR PhylomeDB; Q9ERY9; -.
DR TreeFam; TF300191; -.
DR BioGRID-ORCS; 58520; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Erg28; mouse.
DR PRO; PR:Q9ERY9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9ERY9; protein.
DR Bgee; ENSMUSG00000021252; Expressed in undifferentiated genital tubercle and 234 other tissues.
DR ExpressionAtlas; Q9ERY9; baseline and differential.
DR Genevisible; Q9ERY9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005352; Erg28.
DR PANTHER; PTHR15451; PTHR15451; 1.
DR Pfam; PF03694; Erg28; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..140
FT /note="Ergosterol biosynthetic protein 28 homolog"
FT /id="PRO_0000193904"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 140 AA; 15806 MW; BDD082A4916E9E50 CRC64;
MSRFLNVLRS WLVMVSIIAM GNTLQSFRDH TFLYEKLYTG KPNLVNGLQA RTFGIWTLLS
SVIRCLCAID IHNKTLYHIT LWTFLLALGH FLSELFVFGT AAPTVGVLAP LMVASFSILG
MLVGLRYLEA EPVSRQKKRN
