NOMO2_HUMAN
ID NOMO2_HUMAN Reviewed; 1267 AA.
AC Q5JPE7; Q4G177;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Nodal modulator 2;
DE AltName: Full=pM5 protein 2;
DE Flags: Precursor;
GN Name=NOMO2;
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 MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Leukocyte, and Testis;
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 [4]
RP INTERACTION WITH NCLN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15257293; DOI=10.1038/sj.emboj.7600307;
RA Haffner C., Frauli M., Topp S., Irmler M., Hofmann K., Regula J.T.,
RA Bally-Cuif L., Haass C.;
RT "Nicalin and its binding partner Nomo are novel Nodal signaling
RT antagonists.";
RL EMBO J. 23:3041-3050(2004).
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).
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:15257293, ECO:0000269|PubMed:17261586}; Single-pass
CC membrane protein {ECO:0000269|PubMed:15257293,
CC ECO:0000269|PubMed:17261586}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5JPE7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JPE7-2; Sequence=VSP_013850;
CC Name=3;
CC IsoId=Q5JPE7-3; Sequence=VSP_053928, VSP_053929;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and skeletal muscle
CC and, at lower levels, in heart. {ECO:0000269|PubMed:15257293}.
CC -!- CAUTION: There are 3 copies of the NOMO gene on chromosome 16p12-p13:
CC NOMO1 (AC Q15155), NOMO2 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. The results reported in other entries may therefore apply for
CC this protein. {ECO:0000305}.
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DR EMBL; AL832855; CAI46162.1; -; mRNA.
DR EMBL; AC126755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028389; AAH28389.1; -; mRNA.
DR EMBL; BC041131; AAH41131.1; -; mRNA.
DR CCDS; CCDS10570.1; -. [Q5JPE7-2]
DR CCDS; CCDS32394.1; -. [Q5JPE7-1]
DR RefSeq; NP_001004060.1; NM_001004060.1. [Q5JPE7-1]
DR RefSeq; NP_775885.1; NM_173614.2. [Q5JPE7-2]
DR AlphaFoldDB; Q5JPE7; -.
DR BioGRID; 129677; 26.
DR IntAct; Q5JPE7; 10.
DR MINT; Q5JPE7; -.
DR STRING; 9606.ENSP00000477502; -.
DR TCDB; 8.A.146.1.1; the nodal modulator (nomo) family.
DR GlyConnect; 1573; 8 N-Linked glycans (3 sites).
DR GlyGen; Q5JPE7; 5 sites, 8 N-linked glycans (3 sites).
DR iPTMnet; Q5JPE7; -.
DR PhosphoSitePlus; Q5JPE7; -.
DR SwissPalm; Q5JPE7; -.
DR BioMuta; NOMO2; -.
DR DMDM; 67460998; -.
DR EPD; Q5JPE7; -.
DR jPOST; Q5JPE7; -.
DR MassIVE; Q5JPE7; -.
DR MaxQB; Q5JPE7; -.
DR PaxDb; Q5JPE7; -.
DR PeptideAtlas; Q5JPE7; -.
DR PRIDE; Q5JPE7; -.
DR ProteomicsDB; 62158; -.
DR ProteomicsDB; 63010; -. [Q5JPE7-1]
DR ProteomicsDB; 63011; -. [Q5JPE7-2]
DR Antibodypedia; 42898; 40 antibodies from 17 providers.
DR DNASU; 283820; -.
DR Ensembl; ENST00000330537.10; ENSP00000331851.6; ENSG00000185164.15. [Q5JPE7-2]
DR Ensembl; ENST00000381474.7; ENSP00000370883.3; ENSG00000185164.15. [Q5JPE7-1]
DR Ensembl; ENST00000543392.5; ENSP00000439970.1; ENSG00000185164.15. [Q5JPE7-3]
DR Ensembl; ENST00000621364.4; ENSP00000477502.1; ENSG00000185164.15. [Q5JPE7-1]
DR Ensembl; ENST00000622306.5; ENSP00000478653.1; ENSG00000185164.15. [Q5JPE7-2]
DR GeneID; 283820; -.
DR KEGG; hsa:283820; -.
DR MANE-Select; ENST00000622306.5; ENSP00000478653.1; NM_173614.4; NP_775885.1. [Q5JPE7-2]
DR UCSC; uc032dtj.2; human. [Q5JPE7-1]
DR CTD; 283820; -.
DR GeneCards; NOMO2; -.
DR HGNC; HGNC:22652; NOMO2.
DR HPA; ENSG00000185164; Tissue enhanced (pancreas).
DR MIM; 609158; gene.
DR neXtProt; NX_Q5JPE7; -.
DR PharmGKB; PA134958124; -.
DR VEuPathDB; HostDB:ENSG00000185164; -.
DR eggNOG; KOG1948; Eukaryota.
DR GeneTree; ENSGT00390000000089; -.
DR HOGENOM; CLU_007543_2_0_1; -.
DR InParanoid; Q5JPE7; -.
DR OMA; GWSFEPE; -.
DR OrthoDB; 839381at2759; -.
DR PhylomeDB; Q5JPE7; -.
DR TreeFam; TF313696; -.
DR PathwayCommons; Q5JPE7; -.
DR SignaLink; Q5JPE7; -.
DR BioGRID-ORCS; 283820; 22 hits in 956 CRISPR screens.
DR ChiTaRS; NOMO2; human.
DR GenomeRNAi; 283820; -.
DR Pharos; Q5JPE7; Tdark.
DR PRO; PR:Q5JPE7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q5JPE7; protein.
DR Bgee; ENSG00000185164; Expressed in body of pancreas and 95 other tissues.
DR ExpressionAtlas; Q5JPE7; baseline and differential.
DR Genevisible; Q5JPE7; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA: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 Alternative splicing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1267
FT /note="Nodal modulator 2"
FT /id="PRO_0000021820"
FT TOPO_DOM 32..1155
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1156..1176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1177..1267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1198..1219
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 VAR_SEQ 1..3
FT /note="MLV -> MAR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053928"
FT VAR_SEQ 4..170
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053929"
FT VAR_SEQ 1223..1267
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013850"
FT VARIANT 493
FT /note="V -> M (in dbSNP:rs1062413)"
FT /id="VAR_034139"
FT VARIANT 580
FT /note="V -> M (in dbSNP:rs15984)"
FT /id="VAR_016104"
SQ SEQUENCE 1267 AA; 139439 MW; 593D2AE67A46F5B0 CRC64;
MLVGQGAGLL 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 CGRISIIRFP
DTVKQMNKYK VVLSSQDKDK SLVTVETDAH GSFCFKAKPG 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 RTLRLQEEFQ LMWCLVPWRG TLGIHLFSSL PFASEILLET
TATCIHY
