NOMO1_MOUSE
ID NOMO1_MOUSE Reviewed; 1214 AA.
AC Q6GQT9; Q3TKZ1; Q8BJM1; Q8BJM8; Q8BLS9; Q8K074; Q8R1I7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Nodal modulator 1 {ECO:0000312|EMBL:AAH72630.1};
DE Flags: Precursor;
GN Name=Nomo1 {ECO:0000312|MGI:MGI:2385850};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAC38508.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38508.1};
RC TISSUE=Blastocyst {ECO:0000312|EMBL:BAE39002.1},
RC Cerebellum {ECO:0000312|EMBL:BAC38508.1}, and
RC Embryonic spinal cord {ECO:0000312|EMBL:BAC38713.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|EMBL:AAH72630.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH72630.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH33923.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH72630.1},
RC Colon {ECO:0000312|EMBL:AAH24503.1}, and
RC Liver {ECO:0000312|EMBL:AAH33923.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196 AND SER-1197, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). 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:Q15155,
CC ECO:0000250|UniProtKB:Q6NZ07}.
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. The ribosome-associated ER translocon complex
CC includes SEC61A1, SEC61B, SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and
CC TMEM147; in the absence of ribosomes, only the complex forms with
CC NCLN/Nicalin, NOMO and TMEM147 remains intact. Due to the strong
CC similarity between NOMO1, NOMO2 and NOMO3, similar interaction pattern
CC probably occur for the three gene copies.
CC {ECO:0000250|UniProtKB:Q15155}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15155}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24503.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH33923.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC38713.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK043279; BAC31513.1; -; mRNA.
DR EMBL; AK082495; BAC38508.1; -; mRNA.
DR EMBL; AK082963; BAC38713.1; ALT_INIT; mRNA.
DR EMBL; AK166764; BAE39002.1; -; mRNA.
DR EMBL; BC024503; AAH24503.1; ALT_INIT; mRNA.
DR EMBL; BC033923; AAH33923.1; ALT_INIT; mRNA.
DR EMBL; BC072630; AAH72630.1; -; mRNA.
DR CCDS; CCDS21273.1; -.
DR RefSeq; NP_694697.3; NM_153057.4.
DR AlphaFoldDB; Q6GQT9; -.
DR BioGRID; 229243; 8.
DR STRING; 10090.ENSMUSP00000033121; -.
DR GlyConnect; 2564; 4 N-Linked glycans (3 sites).
DR GlyGen; Q6GQT9; 4 sites, 4 N-linked glycans (3 sites).
DR iPTMnet; Q6GQT9; -.
DR PhosphoSitePlus; Q6GQT9; -.
DR SwissPalm; Q6GQT9; -.
DR EPD; Q6GQT9; -.
DR jPOST; Q6GQT9; -.
DR MaxQB; Q6GQT9; -.
DR PaxDb; Q6GQT9; -.
DR PeptideAtlas; Q6GQT9; -.
DR PRIDE; Q6GQT9; -.
DR ProteomicsDB; 293701; -.
DR DNASU; 211548; -.
DR Ensembl; ENSMUST00000033121; ENSMUSP00000033121; ENSMUSG00000030835.
DR GeneID; 211548; -.
DR KEGG; mmu:211548; -.
DR UCSC; uc009gyb.2; mouse.
DR CTD; 23420; -.
DR MGI; MGI:2385850; Nomo1.
DR VEuPathDB; HostDB:ENSMUSG00000030835; -.
DR eggNOG; KOG1948; Eukaryota.
DR GeneTree; ENSGT00390000000089; -.
DR HOGENOM; CLU_007543_2_0_1; -.
DR InParanoid; Q6GQT9; -.
DR OMA; GWSFEPE; -.
DR OrthoDB; 839381at2759; -.
DR PhylomeDB; Q6GQT9; -.
DR TreeFam; TF313696; -.
DR BioGRID-ORCS; 211548; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Nomo1; mouse.
DR PRO; PR:Q6GQT9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6GQT9; protein.
DR Bgee; ENSMUSG00000030835; Expressed in otic placode and 262 other tissues.
DR Genevisible; Q6GQT9; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
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 Coiled coil; Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1214
FT /note="Nodal modulator 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396822"
FT TOPO_DOM 24..1150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1151..1167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1168..1214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 708..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 692..720
FT /evidence="ECO:0000255"
FT COMPBIAS 708..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 6
FT /note="C -> G (in Ref. 1; BAC38508)"
FT /evidence="ECO:0000305"
FT CONFLICT 62..63
FT /note="DC -> GW (in Ref. 1; BAC38508)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="Y -> V (in Ref. 1; BAC38508)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..97
FT /note="TNV -> PHG (in Ref. 1; BAC38508)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="V -> G (in Ref. 1; BAC38508)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="T -> A (in Ref. 1; BAC38508)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="D -> G (in Ref. 1; BAC38508)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="P -> T (in Ref. 1; BAC38508)"
FT /evidence="ECO:0000305"
FT CONFLICT 875..878
FT /note="KAED -> GRVG (in Ref. 2; AAH24503)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="E -> G (in Ref. 1; BAC31513)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176
FT /note="L -> V (in Ref. 1; BAC31513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1214 AA; 133420 MW; 0F71587617C444A7 CRC64;
MRAGRCAAAL LLLLLSGAGR AIGSEDIVVG CGGFVKSDVE INYSLIEIKL YTKHGTLKYQ
TDCAPNNGYF MIPLYDKGDF ILKIEPPLGW SFEPTNVELR VDGVSDICTK GGDINFLFTG
FSVNGKVLSK GQPLGPAGVQ VSLRSTGADS KIQSTVTQPG GKFAFFKVLP GDYEILATHP
TWALKEASTT VRVTNSNANA AGPLIVAGYN VSGSVRSDGE PMKGVKFLLF SSLVNKEDVL
GCNVSPVSGF QPPDESLVYL CYAVSKEDGS FSFYSLPSGG YTVVPFYRGE RITFDVAPSR
LDFTVEHDSL RIEPVFHVMG FSVTGRVLNG PDGEGVPEAV VTLNNQIKVK TKADGSFRLE
NITTGTYTIH AQKEHLYFEM VTIKIAPNTP QLADLIATGF SICGQIAIVR SPDTIKQMSK
YRVVLSSQDK DKALLTVDSD AHGSFCFKAK PGAYKVQVVV PEAETRAGLM LKPQVFPLTV
TNRPVMDVAF VQFLASVSGK VSCLDTCGDL LVTLQSLSRQ GEKRSLQLSG KVNSMTFTFD
KVLPGRYKIS IMHEDWCWRN KSLEVEVLED DVSAVEFRQT GYMLRCALSH AITLEFHQDG
NGPENVGIYN LSRGVNRFCL SKPGVYKVTP RSCHRFEQAF YTYDTSSPSI LTLTAIRHHV
LGTIITDKMM DVTVTIKSSI DSEPALVLGP LKSAQELRRE QQLAEIETRR QEREKNGKEE
GEEGRARPPG QEMVDELQGP FSYDFSYWAR SGEKITVTPS SKELLFYPPS MEATVSGESC
PGKLIEIHGK AGLFLEGQIH PELEGVEIVI SEKGASSPLI TVFTDDKGAY SVGPLHSDLE
YTVNSQKEGY VLTAVEGTVG DFKAYALAGV SFEIKAEDDQ PLPGVLLSLS GGVFRSNLLT
QDNGILTFSN LSPGQYYFKP MMKEFRFEPS SQMIEVQEGQ NLRITITGFR TAYSCYGTVS
SLNGEPEQGV AVEAVGQKDC SIYGEDTVTD EEGKFRLRGL LPGCMYHVQL KAEGNDHIER
ALPHHRVIEV GNNDVDDVNI IVFRQINQFD LSGNVITSSE YLSTLWVKLY KSESLDNPIQ
TVSLGQSLFF HFPPLLRDGE NYVVLLDTTL PRSQYDYVLP QVSFTAVGYH KHITLVFSPT
RKLPEQDIAQ GSYIALPLTL LLLLAGYNHD KLIPLLLQLT SRLQGVRALG QAASDSSGPE
DMKRQTKKQK TRRT
