OST4_CANLF
ID OST4_CANLF Reviewed; 37 AA.
AC P0CU66;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4 {ECO:0000250|UniProtKB:P0C6T2};
GN Name=OST4 {ECO:0000250|UniProtKB:P0C6T2};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 1-34.
RX PubMed=29519914; DOI=10.1126/science.aar7899;
RA Braunger K., Pfeffer S., Shrimal S., Gilmore R., Berninghausen O.,
RA Mandon E.C., Becker T., Foerster F., Beckmann R.;
RT "Structural basis for coupling protein transport and N-glycosylation at the
RT mammalian endoplasmic reticulum.";
RL Science 360:215-219(2018).
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. OST
CC exists in two different complex forms which contain common core
CC subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or
CC STT3B as catalytic subunits, and form-specific accessory subunits (By
CC similarity). STT3A complex assembly occurs through the formation of 3
CC subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2
CC contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well
CC as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and
CC OST48. The STT3A complex can form stable complexes with the Sec61
CC complex or with both the Sec61 and TRAP complexes (PubMed:29519914).
CC {ECO:0000250|UniProtKB:P0C6T2, ECO:0000269|PubMed:29519914}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P0C6T2}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:29519914}.
CC -!- SIMILARITY: Belongs to the OST4 family. {ECO:0000305}.
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DR EMBL; JH373195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003432220.1; XM_003432172.3.
DR PDB; 6FTG; EM; 9.10 A; 4=1-34.
DR PDB; 6FTI; EM; 4.20 A; 4=1-34.
DR PDB; 6FTJ; EM; 4.70 A; 4=1-34.
DR PDBsum; 6FTG; -.
DR PDBsum; 6FTI; -.
DR PDBsum; 6FTJ; -.
DR AlphaFoldDB; P0CU66; -.
DR SMR; P0CU66; -.
DR GeneID; 100684900; -.
DR KEGG; cfa:100684900; -.
DR CTD; 100128731; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
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_0000445977"
FT TOPO_DOM 1..4
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29519914"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29519914"
FT TOPO_DOM 26..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29519914"
SQ SEQUENCE 37 AA; 4193 MW; AADA830EA2A3952C CRC64;
MITDVQLAIF ANMLGVSLFL LVVLYHYVAV NNPKKQE
