OST4_MOUSE
ID OST4_MOUSE Reviewed; 37 AA.
AC Q99LX8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4 {ECO:0000305};
GN Name=Ost4 {ECO:0000312|MGI:MGI:1914945};
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; TISSUE=Kidney, and Placenta;
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=C57BL/6J, and FVB/N; TISSUE=Brain, and 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: Subunit of the oligosaccharyl transferase (OST) complex that
CC catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. Specifically involved in maintaining stability of
CC STT3A-containing OST complexes. {ECO:0000250|UniProtKB:P0C6T2}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P0C6T2}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex (By
CC similarity). OST exists in two different complex forms which contain
CC common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either
CC STT3A or STT3B as catalytic subunits, and form-specific accessory
CC subunits (By similarity). STT3A complex assembly occurs through the
CC formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258,
CC subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and
CC KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2,
CC DAD1, and OST48. The STT3A complex can form stable complexes with the
CC Sec61 complex or with both the Sec61 and TRAP complexes (By
CC similarity). {ECO:0000250|UniProtKB:P0C6T2,
CC ECO:0000250|UniProtKB:P0CU66}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0C6T2}. Endoplasmic reticulum membrane; Single-
CC pass type III membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the OST4 family. {ECO:0000305}.
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DR EMBL; AK002224; BAE43146.1; -; mRNA.
DR EMBL; AK002453; BAC24992.1; -; mRNA.
DR EMBL; AK003569; BAC25041.1; -; mRNA.
DR EMBL; AK005413; BAC25115.1; -; mRNA.
DR EMBL; AK010297; BAC25288.1; -; mRNA.
DR EMBL; AK019285; BAC25588.1; -; mRNA.
DR EMBL; BC002177; AAH02177.1; -; mRNA.
DR EMBL; BC082316; AAH82316.1; -; mRNA.
DR CCDS; CCDS39049.1; -.
DR RefSeq; NP_001128164.1; NM_001134692.2.
DR RefSeq; NP_077780.3; NM_024460.4.
DR RefSeq; XP_006504134.1; XM_006504071.3.
DR AlphaFoldDB; Q99LX8; -.
DR BMRB; Q99LX8; -.
DR SMR; Q99LX8; -.
DR ComplexPortal; CPX-5821; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5822; Oligosaccharyltransferase complex B.
DR STRING; 10090.ENSMUSP00000128352; -.
DR PaxDb; Q99LX8; -.
DR PRIDE; Q99LX8; -.
DR TopDownProteomics; Q99LX8; -.
DR Antibodypedia; 64138; 15 antibodies from 9 providers.
DR Ensembl; ENSMUST00000132034; ENSMUSP00000126221; ENSMUSG00000038803.
DR Ensembl; ENSMUST00000132253; ENSMUSP00000128352; ENSMUSG00000038803.
DR GeneID; 67695; -.
DR KEGG; mmu:67695; -.
DR UCSC; uc008wwk.2; mouse.
DR CTD; 100128731; -.
DR MGI; MGI:1914945; Ost4.
DR VEuPathDB; HostDB:ENSMUSG00000038803; -.
DR eggNOG; ENOG502SDSY; Eukaryota.
DR GeneTree; ENSGT00390000016516; -.
DR HOGENOM; CLU_186352_2_0_1; -.
DR InParanoid; Q99LX8; -.
DR OrthoDB; 1644285at2759; -.
DR PhylomeDB; Q99LX8; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 67695; 12 hits in 66 CRISPR screens.
DR ChiTaRS; Ost4; mouse.
DR PRO; PR:Q99LX8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR Bgee; ENSMUSG00000038803; Expressed in undifferentiated genital tubercle and 243 other tissues.
DR Genevisible; Q99LX8; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISO:MGI.
DR InterPro; IPR018943; Oligosaccaryltransferase.
DR InterPro; IPR036330; Ost4p_sf.
DR Pfam; PF10215; Ost4; 1.
DR SUPFAM; SSF103464; SSF103464; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..37
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 4"
FT /id="PRO_0000328639"
FT TOPO_DOM 1..4
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 37 AA; 4193 MW; AADA830EA2A3952C CRC64;
MITDVQLAIF ANMLGVSLFL LVVLYHYVAV NNPKKQE
