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Tumor suppressor candidate 3 (Magnesium uptake/transporter TUSC3) (Protein N33)

 TUSC3_HUMAN             Reviewed;         348 AA.
Q13454; A8MSM0; D3DSP2; Q14911; Q14912; Q96FW0;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 155.
RecName: Full=Tumor suppressor candidate 3;
AltName: Full=Magnesium uptake/transporter TUSC3;
AltName: Full=Protein N33;
Flags: Precursor;
Name=TUSC3; Synonyms=N33;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
PubMed=8661104; DOI=10.1006/geno.1996.0322;
Macgrogan D., Levy A., Bova G.S., Isaacs W.B., Bookstein R.;
"Structure and methylation-associated silencing of a gene within a
homozygously deleted region of human chromosome band 8p22.";
Genomics 35:55-65(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND
TISSUE SPECIFICITY.
PubMed=12887896; DOI=10.1016/S1097-2765(03)00243-0;
Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
"Oligosaccharyltransferase isoforms that contain different catalytic
STT3 subunits have distinct enzymatic properties.";
Mol. Cell 12:101-111(2003).
[7]
INVOLVEMENT IN MRT7.
PubMed=18455129; DOI=10.1016/j.ajhg.2008.03.021;
Molinari F., Foulquier F., Tarpey P.S., Morelle W., Boissel S.,
Teague J., Edkins S., Futreal P.A., Stratton M.R., Turner G.,
Matthijs G., Gecz J., Munnich A., Colleaux L.;
"Oligosaccharyltransferase-subunit mutations in nonsyndromic mental
retardation.";
Am. J. Hum. Genet. 82:1150-1157(2008).
[8]
INVOLVEMENT IN MRT7.
PubMed=18452889; DOI=10.1016/j.ajhg.2008.03.018;
Garshasbi M., Hadavi V., Habibi H., Kahrizi K., Kariminejad R.,
Behjati F., Tzschach A., Najmabadi H., Ropers H.H., Kuss A.W.;
"A defect in the TUSC3 gene is associated with autosomal recessive
mental retardation.";
Am. J. Hum. Genet. 82:1158-1164(2008).
[9]
FUNCTION IN MAGNESIUM UPTAKE.
PubMed=19717468; DOI=10.1073/pnas.0908332106;
Zhou H., Clapham D.E.;
"Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake
and vertebrate embryonic development.";
Proc. Natl. Acad. Sci. U.S.A. 106:15750-15755(2009).
[10]
FUNCTION, AND MUTAGENESIS OF CYS-99 AND CYS-102.
PubMed=25135935; DOI=10.1083/jcb.201404083;
Cherepanova N.A., Shrimal S., Gilmore R.;
"Oxidoreductase activity is necessary for N-glycosylation of cysteine-
proximal acceptor sites in glycoproteins.";
J. Cell Biol. 206:525-539(2014).
[11]
X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 44-194, DISULFIDE BOND,
PROPOSED FUNCTION, AND SUBUNIT.
PubMed=24685145; DOI=10.1016/j.str.2014.02.013;
Mohorko E., Owen R.L., Malojcic G., Brozzo M.S., Aebi M.,
Glockshuber R.;
"Structural basis of substrate specificity of human oligosaccharyl
transferase subunit N33/Tusc3 and its role in regulating protein N-
glycosylation.";
Structure 22:590-601(2014).
[12]
VARIANT VAL-247.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- FUNCTION: Acts as accessory component of the N-oligosaccharyl
transferase (OST) complex which catalyzes the transfer of a high
mannose oligosaccharide from a lipid-linked oligosaccharide donor
to an asparagine residue within an Asn-X-Ser/Thr consensus motif
in nascent polypeptide chains. Involved in N-glycosylation of
STT3B-dependent substrates. Specifically required for the
glycosylation of a subset of acceptor sites that are near cysteine
residues; in this function seems to act redundantly with MAGT1. In
its oxidized form proposed to form transient mixed disulfides with
a glycoprotein substrate to facilitate access of STT3B to the
unmodified acceptor site. Has also oxidoreductase-independent
functions in the STT3B-containing OST complex possibly involving
substrate recognition. {ECO:0000269|PubMed:25135935,
ECO:0000305|PubMed:12887896, ECO:0000305|PubMed:24685145}.
-!- FUNCTION: Magnesium transporter. {ECO:0000269|PubMed:19717468}.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Accessory component of the STT3B-containing form of the
oligosaccharyltransferase (OST) complex. OST exists in two
different complex forms which contain common core subunits RPN1,
RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as
catalytic subunits, and form-specific accessory subunits. OST can
form stable complexes with the Sec61 complex or with both the
Sec61 and TRAP complexes. The association of TUSC3 or MAGT1 with
the STT3B-containing complex seems to be mutually exclusvice.
{ECO:0000305|PubMed:12887896, ECO:0000305|PubMed:24685145}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13454-1; Sequence=Displayed;
Name=2;
IsoId=Q13454-2; Sequence=VSP_003776;
-!- TISSUE SPECIFICITY: Expressed in most non-lymphoid cells and
tissues examined, including prostate, lung, liver, colon, heart,
kidney and pancreas. {ECO:0000269|PubMed:12887896}.
-!- DISEASE: Mental retardation, autosomal recessive 7 (MRT7)
[MIM:611093]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. {ECO:0000269|PubMed:18452889,
ECO:0000269|PubMed:18455129}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U42349; AAB18374.1; -; mRNA.
EMBL; U42359; AAB18375.1; -; Genomic_DNA.
EMBL; U42350; AAB18375.1; JOINED; Genomic_DNA.
EMBL; U42351; AAB18375.1; JOINED; Genomic_DNA.
EMBL; U42352; AAB18375.1; JOINED; Genomic_DNA.
EMBL; U42354; AAB18375.1; JOINED; Genomic_DNA.
EMBL; U42355; AAB18375.1; JOINED; Genomic_DNA.
EMBL; U42356; AAB18375.1; JOINED; Genomic_DNA.
EMBL; U42357; AAB18375.1; JOINED; Genomic_DNA.
EMBL; U42358; AAB18375.1; JOINED; Genomic_DNA.
EMBL; U42360; AAB18376.1; -; Genomic_DNA.
EMBL; U42350; AAB18376.1; JOINED; Genomic_DNA.
EMBL; U42351; AAB18376.1; JOINED; Genomic_DNA.
EMBL; U42352; AAB18376.1; JOINED; Genomic_DNA.
EMBL; U42354; AAB18376.1; JOINED; Genomic_DNA.
EMBL; U42355; AAB18376.1; JOINED; Genomic_DNA.
EMBL; U42356; AAB18376.1; JOINED; Genomic_DNA.
EMBL; U42357; AAB18376.1; JOINED; Genomic_DNA.
EMBL; U42358; AAB18376.1; JOINED; Genomic_DNA.
EMBL; BT020002; AAV38805.1; -; mRNA.
EMBL; AC010656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC019292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC100850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471080; EAW63837.1; -; Genomic_DNA.
EMBL; CH471080; EAW63839.1; -; Genomic_DNA.
EMBL; BC010370; AAH10370.1; -; mRNA.
CCDS; CCDS5993.1; -. [Q13454-2]
CCDS; CCDS5994.1; -. [Q13454-1]
PIR; G02297; G02297.
RefSeq; NP_006756.2; NM_006765.3. [Q13454-1]
RefSeq; NP_839952.1; NM_178234.2. [Q13454-2]
UniGene; Hs.426324; -.
UniGene; Hs.600825; -.
PDB; 4M8G; X-ray; 2.00 A; A/B=44-194.
PDB; 4M90; X-ray; 1.60 A; A=44-194.
PDB; 4M91; X-ray; 1.10 A; A=44-194.
PDB; 4M92; X-ray; 1.60 A; A=44-194.
PDBsum; 4M8G; -.
PDBsum; 4M90; -.
PDBsum; 4M91; -.
PDBsum; 4M92; -.
ProteinModelPortal; Q13454; -.
SMR; Q13454; -.
BioGrid; 113701; 26.
CORUM; Q13454; -.
IntAct; Q13454; 1.
MINT; MINT-1192091; -.
STRING; 9606.ENSP00000221167; -.
TCDB; 1.A.76.1.2; the magnesium transporter1 (magt1) family.
iPTMnet; Q13454; -.
PhosphoSitePlus; Q13454; -.
BioMuta; TUSC3; -.
DMDM; 6166601; -.
EPD; Q13454; -.
MaxQB; Q13454; -.
PaxDb; Q13454; -.
PeptideAtlas; Q13454; -.
PRIDE; Q13454; -.
DNASU; 7991; -.
Ensembl; ENST00000382020; ENSP00000371450; ENSG00000104723. [Q13454-2]
Ensembl; ENST00000503731; ENSP00000424544; ENSG00000104723. [Q13454-1]
GeneID; 7991; -.
KEGG; hsa:7991; -.
UCSC; uc003wwt.4; human. [Q13454-1]
CTD; 7991; -.
DisGeNET; 7991; -.
EuPathDB; HostDB:ENSG00000104723.20; -.
GeneCards; TUSC3; -.
GeneReviews; TUSC3; -.
HGNC; HGNC:30242; TUSC3.
HPA; HPA049851; -.
HPA; HPA049974; -.
MalaCards; TUSC3; -.
MIM; 601385; gene.
MIM; 611093; phenotype.
neXtProt; NX_Q13454; -.
OpenTargets; ENSG00000104723; -.
Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
PharmGKB; PA128394537; -.
eggNOG; KOG2603; Eukaryota.
eggNOG; ENOG410XR1F; LUCA.
GeneTree; ENSGT00390000012030; -.
HOGENOM; HOG000231301; -.
HOVERGEN; HBG002493; -.
InParanoid; Q13454; -.
KO; K12669; -.
OMA; WIGERTD; -.
OrthoDB; EOG091G0ERM; -.
PhylomeDB; Q13454; -.
TreeFam; TF314850; -.
Reactome; R-HSA-446203; Asparagine N-linked glycosylation.
Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
UniPathway; UPA00378; -.
ChiTaRS; TUSC3; human.
GeneWiki; TUSC3; -.
GenomeRNAi; 7991; -.
PRO; PR:Q13454; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104723; -.
CleanEx; HS_TUSC3; -.
ExpressionAtlas; Q13454; baseline and differential.
Genevisible; Q13454; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:HGNC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0050890; P:cognition; IMP:UniProtKB.
GO; GO:0015693; P:magnesium ion transport; IMP:UniProtKB.
GO; GO:0006487; P:protein N-linked glycosylation; NAS:UniProtKB.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF04756; OST3_OST6; 1.
SUPFAM; SSF52833; SSF52833; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Magnesium; Membrane; Mental retardation;
Polymorphism; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 41 {ECO:0000255}.
CHAIN 42 348 Tumor suppressor candidate 3.
/FTId=PRO_0000215300.
TOPO_DOM 42 196 Lumenal. {ECO:0000255}.
TRANSMEM 197 217 Helical. {ECO:0000255}.
TOPO_DOM 218 221 Cytoplasmic. {ECO:0000255}.
TRANSMEM 222 242 Helical. {ECO:0000255}.
TOPO_DOM 243 276 Lumenal. {ECO:0000255}.
TRANSMEM 277 297 Helical. {ECO:0000255}.
TOPO_DOM 298 312 Cytoplasmic. {ECO:0000255}.
TRANSMEM 313 333 Helical. {ECO:0000255}.
TOPO_DOM 334 348 Lumenal. {ECO:0000255}.
DOMAIN 59 187 Thioredoxin.
DISULFID 99 102 Redox-active. {ECO:0000244|PDB:4M8G,
ECO:0000244|PDB:4M90,
ECO:0000269|PubMed:24685145}.
VAR_SEQ 344 348 DLDFE -> FLIK (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8661104}.
/FTId=VSP_003776.
VARIANT 65 65 I -> V (in dbSNP:rs11545035).
/FTId=VAR_045836.
VARIANT 247 247 M -> V. {ECO:0000269|PubMed:23033978}.
/FTId=VAR_069369.
MUTAGEN 99 99 C->S: Reduces N-glycosylation of
cysteine-proximal acceptor sites; when
associated with S-102.
{ECO:0000269|PubMed:25135935}.
MUTAGEN 102 102 C->S: Reduces N-glycosylation of
cysteine-proximal acceptor sites; when
associated with S-99.
{ECO:0000269|PubMed:25135935}.
HELIX 44 62 {ECO:0000244|PDB:4M91}.
STRAND 64 67 {ECO:0000244|PDB:4M91}.
HELIX 70 76 {ECO:0000244|PDB:4M91}.
STRAND 84 91 {ECO:0000244|PDB:4M91}.
HELIX 95 97 {ECO:0000244|PDB:4M91}.
HELIX 100 118 {ECO:0000244|PDB:4M91}.
STRAND 126 132 {ECO:0000244|PDB:4M91}.
TURN 133 135 {ECO:0000244|PDB:4M91}.
HELIX 137 142 {ECO:0000244|PDB:4M91}.
STRAND 150 154 {ECO:0000244|PDB:4M91}.
STRAND 156 158 {ECO:0000244|PDB:4M91}.
HELIX 162 164 {ECO:0000244|PDB:4M91}.
HELIX 168 171 {ECO:0000244|PDB:4M91}.
HELIX 175 186 {ECO:0000244|PDB:4M91}.
SEQUENCE 348 AA; 39676 MW; 16D97CB1E00C5190 CRC64;
MGARGAPSRR RQAGRRLRYL PTGSFPFLLL LLLLCIQLGG GQKKKENLLA EKVEQLMEWS
SRRSIFRMNG DKFRKFIKAP PRNYSMIVMF TALQPQRQCS VCRQANEEYQ ILANSWRYSS
AFCNKLFFSM VDYDEGTDVF QQLNMNSAPT FMHFPPKGRP KRADTFDLQR IGFAAEQLAK
WIADRTDVHI RVFRPPNYSG TIALALLVSL VGGLLYLRRN NLEFIYNKTG WAMVSLCIVF
AMTSGQMWNH IRGPPYAHKN PHNGQVSYIH GSSQAQFVAE SHIILVLNAA ITMGMVLLNE
AATSKGDVGK RRIICLVGLG LVVFFFSFLL SIFRSKYHGY PYSDLDFE


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