NOMO1_HUMAN
ID NOMO1_HUMAN Reviewed; 1222 AA.
AC Q15155; P78421; Q8IW21; Q96DG0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 5.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Nodal modulator 1;
DE AltName: Full=pM5 protein;
DE Flags: Precursor;
GN Name=NOMO1; Synonyms=PM5;
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 MRNA], AND VARIANT ALA-583.
RC TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 33-1222, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Melanoma;
RX PubMed=1310294; DOI=10.1016/0888-7543(92)90425-r;
RA Templeton N.S., Rodgers L.A., Levy A.T., Ting K.-L., Krutzsch H.C.,
RA Liotta L.A., Stetler-Stevenson W.G.;
RT "Cloning and characterization of a novel human cDNA that has DNA similarity
RT to the conserved region of the collagenase gene family.";
RL Genomics 12:175-176(1992).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-618.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [5]
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 [6]
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 [7]
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).
RN [8]
RP VARIANT LYS-1081.
RX PubMed=10835642; DOI=10.1038/76102;
RA Le Saux O., Urban Z., Tschuch C., Csiszar K., Bacchelli B., Quaglino D.,
RA Pasquali-Ronchetti I., Pope F.M., Richards A., Terry S., Bercovitch L.,
RA de Paepe A., Boyd C.D.;
RT "Mutations in a gene encoding an ABC transporter cause pseudoxanthoma
RT elasticum.";
RL Nat. Genet. 25:223-227(2000).
RN [9]
RP VARIANTS VAL-404; ASN-458; ASP-490; PHE-1141 AND GLY-1195.
RX PubMed=11139250; DOI=10.1002/1098-1004(2001)17:1<74::aid-humu14>3.0.co;2-f;
RA Perdu J., Germain D.P.;
RT "Identification of novel polymorphisms in the pM5 and MRP1 (ABCC1) genes at
RT locus 16p13.1 and exclusion of both genes as responsible for pseudoxanthoma
RT elasticum.";
RL Hum. Mutat. 17:74-75(2001).
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17261586}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in colon tumor tissue and in adjacent
CC normal colonic mucosa. {ECO:0000269|PubMed:1310294}.
CC -!- DEVELOPMENTAL STAGE: No difference between normal colonic mucosa and
CC colon tumor tissue in mRNA expression, whereas the protein is expressed
CC 1.5-fold more in normal colonic mucosa that in colon tumor tissue.
CC {ECO:0000269|PubMed:1310294}.
CC -!- CAUTION: There are 3 copies of the NOMO gene on chromosome 16p12-p13:
CC NOMO1, NOMO2 (AC Q5JPE7) and NOMO3 (AC P69849). 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. Moreover, it does not allow a clear view of which variant
CC belongs to which of the 3 copies. The results reported in other entries
CC may therefore apply for this protein. {ECO:0000305}.
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DR EMBL; AC136443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065535; AAH65535.1; -; mRNA.
DR EMBL; X57398; CAA40655.1; -; mRNA.
DR CCDS; CCDS10556.1; -.
DR PIR; S21977; S21977.
DR RefSeq; NP_055102.3; NM_014287.3.
DR AlphaFoldDB; Q15155; -.
DR BioGRID; 116991; 203.
DR IntAct; Q15155; 28.
DR MINT; Q15155; -.
DR STRING; 9606.ENSP00000287667; -.
DR DrugBank; DB00277; Theophylline.
DR GlyConnect; 1572; 8 N-Linked glycans (3 sites).
DR GlyGen; Q15155; 6 sites, 8 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q15155; -.
DR PhosphoSitePlus; Q15155; -.
DR SwissPalm; Q15155; -.
DR BioMuta; NOMO1; -.
DR DMDM; 296439497; -.
DR EPD; Q15155; -.
DR jPOST; Q15155; -.
DR MassIVE; Q15155; -.
DR MaxQB; Q15155; -.
DR PaxDb; Q15155; -.
DR PeptideAtlas; Q15155; -.
DR PRIDE; Q15155; -.
DR ProteomicsDB; 60474; -.
DR Antibodypedia; 24899; 342 antibodies from 26 providers.
DR DNASU; 23420; -.
DR Ensembl; ENST00000287667.12; ENSP00000287667.7; ENSG00000103512.16.
DR Ensembl; ENST00000619292.4; ENSP00000482008.1; ENSG00000274779.4.
DR GeneID; 23420; -.
DR KEGG; hsa:23420; -.
DR MANE-Select; ENST00000287667.12; ENSP00000287667.7; NM_014287.4; NP_055102.3.
DR UCSC; uc002dcv.4; human.
DR CTD; 23420; -.
DR DisGeNET; 23420; -.
DR GeneCards; NOMO1; -.
DR HGNC; HGNC:30060; NOMO1.
DR HPA; ENSG00000103512; Tissue enhanced (pancreas).
DR MIM; 609157; gene.
DR neXtProt; NX_Q15155; -.
DR OpenTargets; ENSG00000103512; -.
DR PharmGKB; PA134934458; -.
DR VEuPathDB; HostDB:ENSG00000103512; -.
DR eggNOG; KOG1948; Eukaryota.
DR GeneTree; ENSGT00390000000089; -.
DR HOGENOM; CLU_007543_2_0_1; -.
DR InParanoid; Q15155; -.
DR OrthoDB; 839381at2759; -.
DR PhylomeDB; Q15155; -.
DR TreeFam; TF313696; -.
DR PathwayCommons; Q15155; -.
DR SignaLink; Q15155; -.
DR BioGRID-ORCS; 23420; 46 hits in 990 CRISPR screens.
DR ChiTaRS; NOMO1; human.
DR GeneWiki; NOMO1; -.
DR GenomeRNAi; 23420; -.
DR Pharos; Q15155; Tbio.
DR PRO; PR:Q15155; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q15155; protein.
DR Bgee; ENSG00000103512; Expressed in islet of Langerhans and 98 other tissues.
DR ExpressionAtlas; Q15155; baseline and differential.
DR Genevisible; Q15155; 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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
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; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1222
FT /note="Nodal modulator 1"
FT /id="PRO_0000021819"
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 MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GQT9"
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:0000269|PubMed:19159218"
FT VARIANT 404
FT /note="I -> V (in dbSNP:rs2561962)"
FT /evidence="ECO:0000269|PubMed:11139250"
FT /id="VAR_013312"
FT VARIANT 458
FT /note="K -> N (in dbSNP:rs1345150579)"
FT /evidence="ECO:0000269|PubMed:11139250"
FT /id="VAR_013313"
FT VARIANT 490
FT /note="N -> D (in dbSNP:rs1062412)"
FT /evidence="ECO:0000269|PubMed:11139250"
FT /id="VAR_013314"
FT VARIANT 493
FT /note="M -> V (in dbSNP:rs141860762)"
FT /id="VAR_022551"
FT VARIANT 580
FT /note="M -> V (in dbSNP:rs17356851)"
FT /id="VAR_056956"
FT VARIANT 583
FT /note="V -> A (in dbSNP:rs17855981)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060370"
FT VARIANT 1081
FT /note="E -> K (in dbSNP:rs200317822)"
FT /evidence="ECO:0000269|PubMed:10835642"
FT /id="VAR_011496"
FT VARIANT 1141
FT /note="I -> F (in dbSNP:rs376397163)"
FT /evidence="ECO:0000269|PubMed:11139250"
FT /id="VAR_013315"
FT VARIANT 1195
FT /note="R -> G (in dbSNP:rs9330)"
FT /evidence="ECO:0000269|PubMed:11139250"
FT /id="VAR_013316"
FT CONFLICT 33..35
FT /note="EDI -> RDL (in Ref. 3; CAA40655)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="R -> S (in Ref. 3; CAA40655)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="D -> N (in Ref. 3; CAA40655)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="N -> S (in Ref. 3; CAA40655)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="S -> F (in Ref. 3; CAA40655)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="T -> I (in Ref. 3; CAA40655)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="L -> F (in Ref. 3; CAA40655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141
FT /note="I -> T (in Ref. 3; CAA40655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1196
FT /note="A -> V (in Ref. 2; AAH65535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1222 AA; 134324 MW; EE0A3BB552BAB72B 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 ADIIATGFSV CGQISIIRFP
DTVKQMNKYK VVLSSQDKDK SLVTVETDAH GSFCFKAKPG TYKVQVMVPE AETRAGLTLK
PQTFPLTVTN RPMMDVAFVQ FLASVSGKVS CLDTCGDLLV TLQSLSRQGE KRSLQLSGKV
NAMTFTFDNV LPGKYKISIM HEDWCWKNKS LEVEVLEDDM 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 LQGVRALGQA
ASDNSGPEDA KRQAKKQKTR RT
