NEMP1_MOUSE
ID NEMP1_MOUSE Reviewed; 437 AA.
AC Q6ZQE4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nuclear envelope integral membrane protein 1;
DE Flags: Precursor;
GN Name=Nemp1; Synonyms=Kiaa0286, Tmem194, Tmem194a;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-123.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [3]
RP SUBCELLULAR LOCATION, INTERACTION WITH RAN, PHOSPHORYLATION, AND
RP MUTAGENESIS OF SER-366; SER-376; SER-380; SER-419 AND SER-420.
RX PubMed=25946333; DOI=10.1371/journal.pone.0127271;
RA Shibano T., Mamada H., Hakuno F., Takahashi S., Taira M.;
RT "The inner nuclear membrane protein Nemp1 is a new type of RanGTP-binding
RT protein in eukaryotes.";
RL PLoS ONE 10:E0127271-E0127271(2015).
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with RAN-GTP.
CC {ECO:0000250|UniProtKB:B9X187, ECO:0000269|PubMed:25946333}.
CC -!- INTERACTION:
CC Q6ZQE4; P62827: Ran; NbExp=7; IntAct=EBI-12595939, EBI-286564;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:25946333}; Multi-pass membrane protein
CC {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
CC Nucleus envelope {ECO:0000269|PubMed:25946333}. Note=Colocalizes with
CC lamins and RAN-GTP at the nuclear envelope.
CC {ECO:0000269|PubMed:25946333}.
CC -!- DOMAIN: The transmembrane domains are required and sufficient for its
CC oligomerization. {ECO:0000250|UniProtKB:B9X187}.
CC -!- PTM: Phosphorylated. Phosphorylation may regulate its interaction with
CC RAN-GTP. {ECO:0000269|PubMed:25946333}.
CC -!- SIMILARITY: Belongs to the NEMP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97920.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129110; BAC97920.1; ALT_INIT; mRNA.
DR CCDS; CCDS48720.1; -.
DR RefSeq; NP_001106682.1; NM_001113211.1.
DR AlphaFoldDB; Q6ZQE4; -.
DR BioGRID; 229124; 1.
DR IntAct; Q6ZQE4; 2.
DR STRING; 10090.ENSMUSP00000045988; -.
DR GlyGen; Q6ZQE4; 1 site.
DR iPTMnet; Q6ZQE4; -.
DR PhosphoSitePlus; Q6ZQE4; -.
DR EPD; Q6ZQE4; -.
DR MaxQB; Q6ZQE4; -.
DR PaxDb; Q6ZQE4; -.
DR PRIDE; Q6ZQE4; -.
DR ProteomicsDB; 287372; -.
DR Antibodypedia; 16059; 29 antibodies from 15 providers.
DR DNASU; 210035; -.
DR Ensembl; ENSMUST00000048099; ENSMUSP00000045988; ENSMUSG00000040195.
DR GeneID; 210035; -.
DR KEGG; mmu:210035; -.
DR UCSC; uc007hke.2; mouse.
DR CTD; 23306; -.
DR MGI; MGI:2446113; Nemp1.
DR VEuPathDB; HostDB:ENSMUSG00000040195; -.
DR eggNOG; KOG3817; Eukaryota.
DR GeneTree; ENSGT00390000002174; -.
DR InParanoid; Q6ZQE4; -.
DR OMA; MAGCMKM; -.
DR OrthoDB; 536946at2759; -.
DR PhylomeDB; Q6ZQE4; -.
DR TreeFam; TF314831; -.
DR BioGRID-ORCS; 210035; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Nemp1; mouse.
DR PRO; PR:Q6ZQE4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6ZQE4; protein.
DR Bgee; ENSMUSG00000040195; Expressed in spermatocyte and 165 other tissues.
DR ExpressionAtlas; Q6ZQE4; baseline and differential.
DR Genevisible; Q6ZQE4; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071763; P:nuclear membrane organization; ISO:MGI.
DR InterPro; IPR019358; NEMP_fam.
DR PANTHER; PTHR13598; PTHR13598; 1.
DR Pfam; PF10225; NEMP; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..437
FT /note="Nuclear envelope integral membrane protein 1"
FT /id="PRO_0000050745"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 184..295
FT /note="A; required for its colocalization with lamins at
FT the nuclear envelope"
FT /evidence="ECO:0000269|PubMed:25946333"
FT REGION 334..437
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000269|PubMed:25946333"
FT REGION 334..403
FT /note="B; required for interaction with RAN-GTP"
FT /evidence="ECO:0000269|PubMed:25946333"
FT REGION 415..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14524"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14524"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14524"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT MUTAGEN 366
FT /note="S->A,E: Partial loss of phosphorylation and loss of
FT interaction with RAN-GTP; when associated with A/E-376;
FT A/E-380; A/E-419 and A/E-420."
FT /evidence="ECO:0000269|PubMed:25946333"
FT MUTAGEN 376
FT /note="S->A,E: Partial loss of phosphorylation and loss of
FT interaction with RAN-GTP; when associated with A/E-366;
FT A/E-380; A/E-419 and A/E-420."
FT /evidence="ECO:0000269|PubMed:25946333"
FT MUTAGEN 380
FT /note="S->A,E: Partial loss of phosphorylation and loss of
FT interaction with RAN-GTP; when associated with A/E-366;
FT A/E-376; A/E-419 and A/E-420."
FT /evidence="ECO:0000269|PubMed:25946333"
FT MUTAGEN 419
FT /note="S->A,E: Partial loss of phosphorylation and loss of
FT interaction with RAN; when associated with A/E-366; A/E-
FT 376; A/E-380 and A/E-420."
FT /evidence="ECO:0000269|PubMed:25946333"
FT MUTAGEN 420
FT /note="S->A,E: Partial loss of phosphorylation and loss of
FT interaction with RAN-GTP; when associated with A/E-366;
FT A/E-376; A/E-380 and A/E-419."
FT /evidence="ECO:0000269|PubMed:25946333"
SQ SEQUENCE 437 AA; 49817 MW; F6B25929100CC1D9 CRC64;
MAGGIKVSVW SAVGPGPRCW GAGGGGGATW LLLVVAGCVV CGSADVNVVM LQESQVDMNS
SQQFCYKNVL IPKWHDIWTR IQVRVNSSKL VRVTQVDNEE KLKELEQFSI WNFFSSFLKE
KLNDTYVNVG LYSTKTCLKV EMIEKDTTYS VTVTRRFDPK LFLVFLLGLT LFFCGDLLSR
SQIFYYSTGM SVGIVASLLI VIFMISKFMP KRSPIYVILV GGWSFSLYLI QLVFKNLQEI
WRSYWHYLLS YILTVGFMSF AVCYKYGPLE NERSINLLTW TLQLLGLGLM YSSIQIPHVA
FALIVIALCT KNLEYPIHWL CSTYRRMCKA SGKPVPPRLL TEEEYRIQGE VETQKALQEL
REFCNSPECS AWKTISRIQS PKRFADFVEG SFHLTPNEVS VHEQEYGLGS IFTQDEELSS
EEEGSEYPTF TQNNFLT
