NOMO3_HUMAN
ID NOMO3_HUMAN Reviewed; 1222 AA.
AC P69849;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Nodal modulator 3;
DE AltName: Full=pM5 protein 3;
DE Flags: Precursor;
GN Name=NOMO3;
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=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-1148.
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [3]
RP INTERACTION WITH NCLN, AND SUBCELLULAR LOCATION.
RX PubMed=17261586; DOI=10.1074/jbc.m611033200;
RA Haffner C., Dettmer U., Weiler T., Haass C.;
RT "The Nicastrin-like protein Nicalin regulates assembly and stability of the
RT Nicalin-nodal modulator (NOMO) membrane protein complex.";
RL J. Biol. Chem. 282:10632-10638(2007).
RN [4]
RP INTERACTION WITH NCLN AND TMEM147.
RX PubMed=20538592; DOI=10.1074/jbc.m110.132548;
RA Dettmer U., Kuhn P.H., Abou-Ajram C., Lichtenthaler S.F., Kruger M.,
RA Kremmer E., Haass C., Haffner C.;
RT "Transmembrane protein 147 (TMEM147) is a novel component of the Nicalin-
RT NOMO protein complex.";
RL J. Biol. Chem. 285:26174-26181(2010).
RN [5]
RP FUNCTION, AND INTERACTION WITH TMCO1; CCDC47; NCLN; TMEM147; SEC61A1;
RP SEC61B AND SEC61G.
RX PubMed=32820719; DOI=10.7554/elife.56889;
RA McGilvray P.T., Anghel S.A., Sundaram A., Zhong F., Trnka M.J.,
RA Fuller J.R., Hu H., Burlingame A.L., Keenan R.J.;
RT "An ER translocon for multi-pass membrane protein biogenesis.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Component of a ribosome-associated endoplasmic reticulum (ER)
CC translocon complex involved in multi-pass membrane protein transport
CC into the ER membrane and biogenesis (PubMed:32820719). May antagonize
CC Nodal signaling and subsequent organization of axial structures during
CC mesodermal patterning, via its interaction with NCLN/Nicalin (By
CC similarity). {ECO:0000250|UniProtKB:Q6NZ07,
CC ECO:0000269|PubMed:32820719}.
CC -!- SUBUNIT: Forms a complex with NCLN/Nicalin and TMEM147, resulting in a
CC stabilization of the 3 proteins, which are otherwise quickly degraded
CC by the proteasome (PubMed:20538592). The ribosome-associated ER
CC translocon complex includes SEC61A1, SEC61B, SEC61G, TMCO1, CCDC47,
CC NCLN/Nicalin, NOMO and TMEM147; in the absence of ribosomes, only the
CC complex forms with NCLN/Nicalin, NOMO and TMEM147 remains intact
CC (PubMed:32820719). Due to the strong similarity between NOMO1, NOMO2
CC and NOMO3, similar interaction pattern probably occur for the three
CC gene copies (PubMed:20538592, PubMed:32820719).
CC {ECO:0000269|PubMed:20538592, ECO:0000269|PubMed:32820719}.
CC -!- INTERACTION:
CC P69849; PRO_0000037315 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-947048, EBI-25487941;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17261586}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17261586}.
CC -!- CAUTION: There are 3 copies of the NOMO gene on chromosome 16p12-p13:
CC NOMO1 (AC Q5JPE7), NOMO2 (AC Q5JPE7) and NOMO3. All 3 are extremely
CC similar, which makes their individual characterization difficult. Thus,
CC most experiments probably do not discriminate between the different
CC members. The results reported in other entries may therefore apply for
CC this protein. {ECO:0000305}.
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DR EMBL; AC136624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U91318; AAC15783.1; -; Genomic_DNA.
DR CCDS; CCDS42123.1; -.
DR RefSeq; NP_001004067.1; NM_001004067.3.
DR AlphaFoldDB; P69849; -.
DR SMR; P69849; -.
DR BioGRID; 135912; 49.
DR IntAct; P69849; 8.
DR MINT; P69849; -.
DR STRING; 9606.ENSP00000382274; -.
DR GlyConnect; 1574; 8 N-Linked glycans (3 sites).
DR GlyGen; P69849; 5 sites, 8 N-linked glycans (3 sites).
DR iPTMnet; P69849; -.
DR MetOSite; P69849; -.
DR PhosphoSitePlus; P69849; -.
DR SwissPalm; P69849; -.
DR BioMuta; NOMO3; -.
DR DMDM; 296439242; -.
DR jPOST; P69849; -.
DR MassIVE; P69849; -.
DR MaxQB; P69849; -.
DR PaxDb; P69849; -.
DR PeptideAtlas; P69849; -.
DR PRIDE; P69849; -.
DR ProteomicsDB; 57544; -.
DR Antibodypedia; 68531; 7 antibodies from 6 providers.
DR DNASU; 408050; -.
DR Ensembl; ENST00000399336.9; ENSP00000382274.4; ENSG00000103226.19.
DR Ensembl; ENST00000611106.4; ENSP00000483234.1; ENSG00000278087.4.
DR Ensembl; ENST00000676846.1; ENSP00000504575.1; ENSG00000103226.19.
DR Ensembl; ENST00000677777.1; ENSP00000504325.1; ENSG00000103226.19.
DR GeneID; 408050; -.
DR KEGG; hsa:408050; -.
DR MANE-Select; ENST00000399336.9; ENSP00000382274.4; NM_001004067.4; NP_001004067.1.
DR UCSC; uc002deq.4; human.
DR CTD; 408050; -.
DR DisGeNET; 408050; -.
DR GeneCards; NOMO3; -.
DR HGNC; HGNC:25242; NOMO3.
DR HPA; ENSG00000103226; Tissue enhanced (pancreas).
DR MIM; 609159; gene.
DR neXtProt; NX_P69849; -.
DR OpenTargets; ENSG00000103226; -.
DR PharmGKB; PA134950400; -.
DR VEuPathDB; HostDB:ENSG00000103226; -.
DR eggNOG; KOG1948; Eukaryota.
DR GeneTree; ENSGT00390000000089; -.
DR HOGENOM; CLU_007543_2_0_1; -.
DR InParanoid; P69849; -.
DR OMA; NQYTIHA; -.
DR OrthoDB; 839381at2759; -.
DR PhylomeDB; P69849; -.
DR TreeFam; TF313696; -.
DR PathwayCommons; P69849; -.
DR SignaLink; P69849; -.
DR BioGRID-ORCS; 408050; 22 hits in 612 CRISPR screens.
DR ChiTaRS; NOMO3; human.
DR GenomeRNAi; 408050; -.
DR Pharos; P69849; Tdark.
DR PRO; PR:P69849; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P69849; protein.
DR Bgee; ENSG00000103226; Expressed in body of pancreas and 98 other tissues.
DR ExpressionAtlas; P69849; baseline and differential.
DR Genevisible; P69849; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:1900108; P:negative regulation of nodal signaling pathway; ISS:FlyBase.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041033; Prealbumin-like.
DR Pfam; PF17802; SpaA; 1.
DR SUPFAM; SSF49452; SSF49452; 3.
DR SUPFAM; SSF49464; SSF49464; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1222
FT /note="Nodal modulator 3"
FT /id="PRO_0000021821"
FT TOPO_DOM 32..1155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1156..1176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1177..1222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1198..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 726
FT /note="N -> K (in Ref. 2; AAC15783)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141
FT /note="I -> F (in Ref. 2; AAC15783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1222 AA; 134134 MW; 2142BE9860A76722 CRC64;
MLVGQGAGPL GPAVVTAAVV LLLSGVGPAH GSEDIVVGCG GFVKSDVEIN YSLIEIKLYT
KHGTLKYQTD CAPNNGYFMI PLYDKGDFIL KIEPPLGWSF EPTTVELHVD GVSDICTKGG
DINFVFTGFS VNGKVLSKGQ PLGPAGVQVS LRNTGTEAKI QSTVTQPGGK FAFFKVLPGD
YEILATHPTW ALKEASTTVR VTNSNANAAS PLIVAGYNVS GSVRSDGEPM KGVKFLLFSS
LVTKEDVLGC NVSPVPGFQP QDESLVYLCY TVSREDGSFS FYSLPSGGYT VIPFYRGERI
TFDVAPSRLD FTVEHDSLKI EPVFHVMGFS VTGRVLNGPE GDGVPEAVVT LNNQIKVKTK
ADGSFRLENI TTGTYTIHAQ KEHLYFETVT IKIAPNTPQL ADIVATGFSV CGQISIIRFP
DTVKQMNKYK VVLSSQDKDK SLVTVETDAH GSFCFKANPG TYKVQVMVPE AETRAGLTLK
PQTFPLTVTD RPVMDVAFVQ FLASVSGKVS CLDTCGDLLV TLQSLSRQGE KRSLQLSGKV
NAMTFTFDNV LPGKYKISIM HEDWCWKNKS LEVEVLEDDV SAVEFRQTGY MLRCSLSHAI
TLEFYQDGNG RENVGIYNLS KGVNRFCLSK PGVYKVTPRS CHRFEQAFYT YDTSSPSILT
LTAIRHHVLG TITTDKMMDV TVTIKSSIDS EPALVLGPLK SVQELRREQQ LAEIEARRQE
REKNGNEEGE ERMTKPPVQE MVDELQGPFS YDFSYWARSG EKITVTPSSK ELLFYPPSME
AVVSGESCPG KLIEIHGKAG LFLEGQIHPE LEGVEIVISE KGASSPLITV FTDDKGAYSV
GPLHSDLEYT VTSQKEGYVL TAVEGTIGDF KAYALAGVSF EIKAEDDQPL PGVLLSLSGG
LFRSNLLTQD NGILTFSNLS PGQYYFKPMM KEFRFEPSSQ MIEVQEGQNL KITITGYRTA
YSCYGTVSSL NGEPEQGVAM EAVGQNDCSI YGEDTVTDEE GKFRLRGLLP GCVYHVQLKA
EGNDHIERAL PHHRVIEVGN NDIDDVNIIV FRQINQFDLS GNVITSSEYL PTLWVKLYKS
ENLDNPIQTV SLGQSLFFHF PPLLRDGENY VVLLDSTLPR SQYDYILPQV SFTAVGYHKH
ITLIFNPTRK LPEQDIAQGS YIALPLTLLV LLAGYNHDKL IPLLLQLTSR LQGVGALGQA
ASDNSGPEDA KRQAKKQKTR RT
