ID   OSTC_HUMAN              Reviewed;         149 AA.
AC   Q9NRP0; A8MYS2; B2R5H1; D6RH22; Q9P075; Q9P1R4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   22-APR-2020, entry version 139.
DE   RecName: Full=Oligosaccharyltransferase complex subunit OSTC;
DE   AltName: Full=Hydrophobic protein HSF-28;
GN   Name=OSTC; ORFNames=DC2, HDCMD45P, HSPC307;
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 [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RA   Favier A.-L., Harsi C., Chrobozcek J.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Dendritic cell;
RA   Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT   "A novel gene from human dendritic cell.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Umbilical cord blood;
RA   Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA   Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT   "Human partial CDS from CD34+ stem cells.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Dendritic cell;
RA   Peng Y., Li Y., Li N., Gu W., Han Z., Fu G., Chen Z.;
RT   "Novel genes expressed in human dendritic cell.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15146197; DOI=10.1038/nbt971;
RA   Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y.,
RA   Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J.,
RA   Stanton L.W.;
RT   "Transcriptome characterization elucidates signaling networks that control
RT   human ES cell growth and differentiation.";
RL   Nat. Biotechnol. 22:707-716(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mesangial cell;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Urinary bladder;
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSEN1 AND NCSTN.
RX   PubMed=21768116; DOI=10.1074/jbc.m111.249748;
RA   Wilson C.M., Magnaudeix A., Yardin C., Terro F.;
RT   "DC2 and keratinocyte-associated protein 2 (KCP2), subunits of the
RT   oligosaccharyltransferase complex, are regulators of the gamma-secretase-
RT   directed processing of amyloid precursor protein (APP).";
RL   J. Biol. Chem. 286:31080-31091(2011).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13]
RP   VARIANT [LARGE SCALE ANALYSIS] LEU-9.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
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. May be involved in N-glycosylation of APP (amyloid-
CC       beta precursor protein). Can modulate gamma-secretase cleavage of APP
CC       by enhancing endoprotelysis of PSEN1. {ECO:0000269|PubMed:21768116}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
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
CC       (PubMed:21768116). STT3A complex assembly occurs through the formation
CC       of 3 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 (By similarity).
CC       Interacts with PSEN1 and NCSTN; indicative for an association with the
CC       gamma-secretase complex (PubMed:21768116).
CC       {ECO:0000250|UniProtKB:P86218, ECO:0000269|PubMed:21768116}.
CC   -!- INTERACTION:
CC       Q9NRP0; Q92838: EDA; NbExp=3; IntAct=EBI-1044658, EBI-529425;
CC       Q9NRP0; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-1044658, EBI-11988865;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:21768116}. Membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NRP0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NRP0-2; Sequence=VSP_047376;
CC   -!- SIMILARITY: Belongs to the OSTC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF28985.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAF65186.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CN430159; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF343342; AAK69656.1; -; mRNA.
DR   EMBL; AF068297; AAF65186.1; ALT_INIT; mRNA.
DR   EMBL; AF161425; AAF28985.1; ALT_INIT; mRNA.
DR   EMBL; AF201937; AAF86873.1; -; mRNA.
DR   EMBL; CN430159; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK312185; BAG35118.1; -; mRNA.
DR   EMBL; AC107071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471057; EAX06233.1; -; Genomic_DNA.
DR   EMBL; BC016321; AAH16321.1; -; mRNA.
DR   EMBL; BC054857; AAH54857.1; -; mRNA.
DR   CCDS; CCDS3681.1; -. [Q9NRP0-1]
DR   CCDS; CCDS58921.1; -. [Q9NRP0-2]
DR   RefSeq; NP_001254746.1; NM_001267817.1.
DR   RefSeq; NP_001254747.1; NM_001267818.1. [Q9NRP0-2]
DR   RefSeq; NP_067050.1; NM_021227.3. [Q9NRP0-1]
DR   PDB; 6S7O; EM; 3.50 A; H=1-149.
DR   PDBsum; 6S7O; -.
DR   BioGrid; 121833; 15.
DR   IntAct; Q9NRP0; 21.
DR   MINT; Q9NRP0; -.
DR   STRING; 9606.ENSP00000426167; -.
DR   TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR   iPTMnet; Q9NRP0; -.
DR   PhosphoSitePlus; Q9NRP0; -.
DR   SwissPalm; Q9NRP0; -.
DR   BioMuta; OSTC; -.
DR   DMDM; 74734324; -.
DR   EPD; Q9NRP0; -.
DR   jPOST; Q9NRP0; -.
DR   MassIVE; Q9NRP0; -.
DR   MaxQB; Q9NRP0; -.
DR   PaxDb; Q9NRP0; -.
DR   PeptideAtlas; Q9NRP0; -.
DR   PRIDE; Q9NRP0; -.
DR   ProteomicsDB; 14790; -.
DR   ProteomicsDB; 82398; -. [Q9NRP0-1]
DR   TopDownProteomics; Q9NRP0-1; -. [Q9NRP0-1]
DR   Antibodypedia; 26281; 87 antibodies.
DR   DNASU; 58505; -.
DR   Ensembl; ENST00000361564; ENSP00000354676; ENSG00000198856. [Q9NRP0-1]
DR   Ensembl; ENST00000512478; ENSP00000426167; ENSG00000198856. [Q9NRP0-2]
DR   GeneID; 58505; -.
DR   KEGG; hsa:58505; -.
DR   UCSC; uc003hzb.3; human. [Q9NRP0-1]
DR   CTD; 58505; -.
DR   DisGeNET; 58505; -.
DR   GeneCards; OSTC; -.
DR   HGNC; HGNC:24448; OSTC.
DR   HPA; ENSG00000198856; Low tissue specificity.
DR   neXtProt; NX_Q9NRP0; -.
DR   OpenTargets; ENSG00000198856; -.
DR   PharmGKB; PA164724280; -.
DR   eggNOG; KOG3356; Eukaryota.
DR   eggNOG; ENOG4111G0G; LUCA.
DR   GeneTree; ENSGT00390000001376; -.
DR   HOGENOM; CLU_109136_1_0_1; -.
DR   InParanoid; Q9NRP0; -.
DR   OMA; MRMKLPF; -.
DR   OrthoDB; 1575260at2759; -.
DR   PhylomeDB; Q9NRP0; -.
DR   TreeFam; TF323315; -.
DR   UniPathway; UPA00378; -.
DR   ChiTaRS; OSTC; human.
DR   GenomeRNAi; 58505; -.
DR   Pharos; Q9NRP0; Tbio.
DR   PRO; PR:Q9NRP0; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9NRP0; protein.
DR   Bgee; ENSG00000198856; Expressed in kidney and 199 other tissues.
DR   ExpressionAtlas; Q9NRP0; baseline and differential.
DR   Genevisible; Q9NRP0; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:HGNC.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IC:HGNC-UCL.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR042416; OSTC.
DR   PANTHER; PTHR13160; PTHR13160; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Endoplasmic reticulum; Membrane;
KW   Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..149
FT                   /note="Oligosaccharyltransferase complex subunit OSTC"
FT                   /id="PRO_0000320602"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..83
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..117
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..149
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         145..149
FT                   /note="GYLMG -> RSLALLPRLECSGVISAHYKLCLPGAI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15146197"
FT                   /id="VSP_047376"
FT   VARIANT         9
FT                   /note="F -> L (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_039231"
FT   CONFLICT        119
FT                   /note="L -> P (in Ref. 2; AAF65186)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   149 AA;  16829 MW;  E59289BB927442B4 CRC64;
     METLYRVPFL VLECPNLKLK KPPWLHMPSA MTVYALVVVS YFLITGGIIY DVIVEPPSVG
     SMTDEHGHQR PVAFLAYRVN GQYIMEGLAS SFLFTMGGLG FIILDRSNAP NIPKLNRFLL
     LFIGFVCVLL SFFMARVFMR MKLPGYLMG
//