ID D3ZSA9_RAT Unreviewed; 1230 AA. AC D3ZSA9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 2. DT 04-NOV-2026, entry version 112. DE SubName: Full=Nodal modulator 1 {ECO:0000313|Ensembl:ENSRNOP00000028680.6}; GN Name=Nomo1 {ECO:0000313|Ensembl:ENSRNOP00000028680.6, GN ECO:0000313|RGD:1305240}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000028680.6, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000028680.6} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000028680.6}; RA Doris P.A., Kalbfleisch T., Li K., Howe K., Wood J.; RT "GRCr8: a new rat reference genome assembly contstructed from accurate long RT reads and long range scaffolding."; RL Submitted (JAN-2024) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSRNOP00000028680.6} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000028680.6}; RG Ensembl; RL Submitted (JUL-2026) to UniProtKB. CC -!- FUNCTION: Component of the multi-pass translocon (MPT) complex that CC mediates insertion of multi-pass membrane proteins into the lipid CC bilayer of membranes. The MPT complex takes over after the SEC61 CC complex: following membrane insertion of the first few transmembrane CC segments of proteins by the SEC61 complex, the MPT complex occludes the CC lateral gate of the SEC61 complex to promote insertion of subsequent CC transmembrane regions. {ECO:0000256|ARBA:ARBA00056484}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004115}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_006229170.1; XM_006229108.5. DR AlphaFoldDB; D3ZSA9; -. DR STRING; 10116.ENSRNOP00000028680; -. DR jPOST; D3ZSA9; -. DR PaxDb; 10116-ENSRNOP00000028680; -. DR PeptideAtlas; D3ZSA9; -. DR Ensembl; ENSRNOT00000028680.7; ENSRNOP00000028680.6; ENSRNOG00000021118.7. DR GeneID; 361578; -. DR UCSC; RGD:1305240; rat. DR AGR; RGD:1305240; -. DR CTD; 23420; -. DR RGD; 1305240; Nomo1. DR VEuPathDB; HostDB:ENSRNOG00000021118; -. DR eggNOG; KOG1948; Eukaryota. DR GeneTree; ENSGT00390000000089; -. DR HOGENOM; CLU_007543_2_0_1; -. DR InParanoid; D3ZSA9; -. DR OMA; AACGELM; -. DR OrthoDB; 10263633at2759; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000021118; Expressed in skeletal muscle tissue and 19 other cell types or tissues. DR ExpressionAtlas; D3ZSA9; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD. DR GO; GO:0160064; C:multi-pass translocon complex; ISO:RGD. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; ISO:RGD. DR GO; GO:0160063; P:multi-pass transmembrane protein insertion into ER membrane; ISO:RGD. DR FunFam; 2.60.40.1120:FF:000001; Nodal modulator 1; 1. DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR013784; Carb-bd-like_fold. DR InterPro; IPR008969; CarboxyPept-like_regulatory. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR055075; NOMO-like_N. DR InterPro; IPR055073; NOMO1-like_9th. DR InterPro; IPR056191; NOMO_12th. DR InterPro; IPR056189; NOMO_3rd. DR InterPro; IPR056190; NOMO_5th. DR InterPro; IPR056319; NOMO_7th. DR InterPro; IPR056187; NOMO_8th. DR InterPro; IPR051417; SDr/BOS_complex. DR PANTHER; PTHR23303:SF14; BOS COMPLEX SUBUNIT NOMO1-RELATED; 1. DR PANTHER; PTHR23303; CARBOXYPEPTIDASE REGULATORY REGION-CONTAINING; 1. DR Pfam; PF13620; CarboxypepD_reg; 1. DR Pfam; PF23141; Ig_NOMO; 1. DR Pfam; PF22898; NOMO1-like_1st; 1. DR Pfam; PF22904; NOMO1-like_2nd; 2. DR Pfam; PF22902; NOMO1-like_9th; 1. DR Pfam; PF23192; NOMO_12th; 1. DR Pfam; PF23193; NOMO_3rd; 1. DR Pfam; PF23194; NOMO_5th; 1. DR Pfam; PF23660; NOMO_8th; 1. DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1. DR SUPFAM; SSF49452; Starch-binding domain-like; 3. PE 4: Predicted; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 24..1230 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5053797965" FT TRANSMEM 1164..1183 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 32..116 FT /note="NOMO-like N-terminal beta-sandwich" FT /evidence="ECO:0000259|Pfam:PF22898" FT DOMAIN 217..317 FT /note="NOMO third transthyretin-like" FT /evidence="ECO:0000259|Pfam:PF23193" FT DOMAIN 401..490 FT /note="NOMO fifth transthyretin-like" FT /evidence="ECO:0000259|Pfam:PF23194" FT DOMAIN 584..656 FT /note="NOMO seventh transthyretin-like" FT /evidence="ECO:0000259|Pfam:PF23141" FT DOMAIN 740..790 FT /note="NOMO eighth prealbumin-like" FT /evidence="ECO:0000259|Pfam:PF23660" FT DOMAIN 791..865 FT /note="NOMO-like ninth beta-sandwich" FT /evidence="ECO:0000259|Pfam:PF22902" FT DOMAIN 1046..1139 FT /note="NOMO C-terminal transthyretin-like" FT /evidence="ECO:0000259|Pfam:PF23192" FT REGION 708..733 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1206..1230 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 708..726 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1221..1230 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1230 AA; 135199 MW; 6CB3E1E48C4EE92A CRC64; MRAGRCAAVL LLLLLSGPGR AIGSEDIVVG CGGFVKSDVE INYSLIEIKL YTKHGTLKYQ TDCAPNNGYF MIPLYDKGDF ILKIEPPLGW SFEPTNVELH VDGVSDVCTR GGDINFVFTG FSVNGKVLSK GQPLGPAGVQ VSLRSTGADS KIQSTVTQPG GKFAFFKVLP GDYEILATHP TWALKEASTT VRVTNSNANA AGPLIVAGYN VSGSVRSDGE PMKGVKFLLF SSLVNKEDVL GCNVSPVSGF QPPDESLVYL CYAVSKEDGS FSFYSLPSGG YTVVPFYRGE RITFDVAPSR LDFTVEHDSL RIEPVFHVMG FSVTGRVLNG PDGEGVPEAV VTLNNQIKVR TKADGSFRLE NITTGTYTIH AQKEHLYFDM VTIKIAPNTP QLADLIATGF SICGQISIIR SPDTIKQMNK YKVVLSSQDK DKALVTVETD AHGSFCFKAK PGIYKVQVVV PEAETRAGLM LKPQTFPITV TNKPVMDVAF VQFLASVSGK VSCLDTCGDL LVTLQSLSRQ GEKRSLQLSG KVNSMTFTFD KVLPGKYKIS IMHEDWCWRN KSLEVEVLED DVSAVEFRQT GYMLRCALSH AITLEFHQDG NGPENVGIYN LSRGVNRFCL SKPGVYKVTP RSCHRFEQAF YTYDTSSPSI LTLTAIRHHV LGTIITDKMM DVTVTIKSSI DSEPALVLGP LKSAQELRRE QQLAEIETRR QEREKNGKEE GEEGRARPPG QEMVDELQGP FSYDFSYWAR CGEKITVTPS SKELLFYPPS MEATVSGESC PGKLIEIHGK AGLFLEGQIH PELEGVEIVI SEKGASSPLI TVFTDDKGAY SVGPLHSDLE YTVTSQKEGF 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 NYVVLLDSTL PRSQYDYVLP QVSFAAVGYH KHITLVFSPT WSMSENLQGV TAIPLQRKLP EQDIAQGSYI ALPLTLLLLL AGYNHDKLIP LLLQLTSRLQ GVRALGQAAS DSSGPEDMKR QTKKQKTRRT //