OST4_HUMAN
ID OST4_HUMAN Reviewed; 37 AA.
AC P0C6T2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4 {ECO:0000305};
GN Name=OST4 {ECO:0000312|HGNC:HGNC:32483};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
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).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX,
RP INTERACTION WITH STT3A; STT3A AND RPN1, MUTAGENESIS OF VAL-23, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23606741; DOI=10.1242/jcs.115410;
RA Dumax-Vorzet A., Roboti P., High S.;
RT "OST4 is a subunit of the mammalian oligosaccharyltransferase required for
RT efficient N-glycosylation.";
RL J. Cell Sci. 126:2595-2606(2013).
RN [4]
RP STRUCTURE BY NMR, AND TRANSMEMBRANE DOMAIN.
RX PubMed=21609714; DOI=10.1016/j.bbrc.2011.05.050;
RA Gayen S., Kang C.;
RT "Solution structure of a human minimembrane protein Ost4, a subunit of the
RT oligosaccharyltransferase complex.";
RL Biochem. Biophys. Res. Commun. 409:572-576(2011).
RN [5] {ECO:0007744|PDB:6S7O, ECO:0007744|PDB:6S7T}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION OF THE
RP OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, FUNCTION, AND PATHWAY.
RX PubMed=31831667; DOI=10.1126/science.aaz3505;
RA Ramirez A.S., Kowal J., Locher K.P.;
RT "Cryo-electron microscopy structures of human oligosaccharyltransferase
RT complexes OST-A and OST-B.";
RL Science 366:1372-1375(2019).
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 (PubMed:31831667). N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61 complex at
CC the channel-forming translocon complex that mediates protein
CC translocation across the endoplasmic reticulum (ER). All subunits are
CC required for a maximal enzyme activity. Specifically involved in
CC maintaining stability of STT3A-containing OST complexes.
CC {ECO:0000269|PubMed:23606741, ECO:0000269|PubMed:31831667}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:31831667}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex
CC (PubMed:31831667). OST exists in two different complex forms which
CC contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258,
CC either STT3A or STT3B as catalytic subunits, and form-specific
CC accessory subunits (PubMed:23606741, PubMed:31831667). STT3A complex
CC assembly occurs through the formation of 3 subcomplexes. Subcomplex 1
CC contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific
CC subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4,
CC and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can
CC form stable complexes with the Sec61 complex or with both the Sec61 and
CC TRAP complexes (By similarity). {ECO:0000250|UniProtKB:P0CU66,
CC ECO:0000269|PubMed:23606741, ECO:0000269|PubMed:31831667}.
CC -!- INTERACTION:
CC P0C6T2; A6NI15: MSGN1; NbExp=3; IntAct=EBI-18397963, EBI-11991020;
CC P0C6T2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-18397963, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000305|PubMed:23606741}. Endoplasmic reticulum membrane; Single-
CC pass type III membrane protein {ECO:0000305}. Note=The single
CC transmembrane helix has a kink in the middle of the transmembrane span.
CC -!- SIMILARITY: Belongs to the OST4 family. {ECO:0000305}.
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DR EMBL; AC013403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015653; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS58703.1; -.
DR RefSeq; NP_001128165.1; NM_001134693.1.
DR PDB; 2LAT; NMR; -; A=1-37.
DR PDB; 6S7O; EM; 3.50 A; B=1-37.
DR PDB; 6S7T; EM; 3.50 A; B=1-37.
DR PDBsum; 2LAT; -.
DR PDBsum; 6S7O; -.
DR PDBsum; 6S7T; -.
DR AlphaFoldDB; P0C6T2; -.
DR BMRB; P0C6T2; -.
DR SMR; P0C6T2; -.
DR BioGRID; 933663; 8.
DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B.
DR IntAct; P0C6T2; 3.
DR STRING; 9606.ENSP00000457935; -.
DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR BioMuta; OST4; -.
DR DMDM; 182894143; -.
DR jPOST; P0C6T2; -.
DR MassIVE; P0C6T2; -.
DR PaxDb; P0C6T2; -.
DR PeptideAtlas; P0C6T2; -.
DR PRIDE; P0C6T2; -.
DR TopDownProteomics; P0C6T2; -.
DR Antibodypedia; 64138; 15 antibodies from 9 providers.
DR DNASU; 100128731; -.
DR Ensembl; ENST00000429985.1; ENSP00000455716.1; ENSG00000228474.6.
DR Ensembl; ENST00000447619.5; ENSP00000454411.1; ENSG00000228474.6.
DR Ensembl; ENST00000456793.2; ENSP00000457935.1; ENSG00000228474.6.
DR GeneID; 100128731; -.
DR KEGG; hsa:100128731; -.
DR MANE-Select; ENST00000456793.2; ENSP00000457935.1; NM_001134693.2; NP_001128165.1.
DR UCSC; uc002rig.4; human.
DR CTD; 100128731; -.
DR DisGeNET; 100128731; -.
DR GeneCards; OST4; -.
DR HGNC; HGNC:32483; OST4.
DR HPA; ENSG00000228474; Low tissue specificity.
DR MIM; 618932; gene.
DR neXtProt; NX_P0C6T2; -.
DR OpenTargets; ENSG00000228474; -.
DR PharmGKB; PA165697090; -.
DR VEuPathDB; HostDB:ENSG00000228474; -.
DR eggNOG; ENOG502TACH; Eukaryota.
DR GeneTree; ENSGT00390000016516; -.
DR HOGENOM; CLU_186352_2_0_1; -.
DR InParanoid; P0C6T2; -.
DR OrthoDB; 1584372at2759; -.
DR PhylomeDB; P0C6T2; -.
DR BRENDA; 2.4.99.18; 2681.
DR PathwayCommons; P0C6T2; -.
DR SignaLink; P0C6T2; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 100128731; 152 hits in 697 CRISPR screens.
DR ChiTaRS; OST4; human.
DR GenomeRNAi; 100128731; -.
DR Pharos; P0C6T2; Tdark.
DR PRO; PR:P0C6T2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR Bgee; ENSG00000228474; Expressed in monocyte and 179 other tissues.
DR Genevisible; P0C6T2; HS.
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; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR InterPro; IPR018943; Oligosaccaryltransferase.
DR InterPro; IPR036330; Ost4p_sf.
DR Pfam; PF10215; Ost4; 1.
DR SUPFAM; SSF103464; SSF103464; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..37
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 4"
FT /id="PRO_0000328638"
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"
FT MUTAGEN 23
FT /note="V->K: Decreases interaction with STT3A, STT3B and
FT RPN1."
FT /evidence="ECO:0000269|PubMed:23606741"
FT HELIX 4..30
FT /evidence="ECO:0007829|PDB:6S7O"
SQ SEQUENCE 37 AA; 4193 MW; AADA830EA2A3952C CRC64;
MITDVQLAIF ANMLGVSLFL LVVLYHYVAV NNPKKQE
