NEMP1_PONAB
ID NEMP1_PONAB Reviewed; 444 AA.
AC Q5RDB4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Nuclear envelope integral membrane protein 1;
DE Flags: Precursor;
GN Name=NEMP1; Synonyms=TMEM194A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homooligomer. Interacts with RAN-GTP.
CC {ECO:0000250|UniProtKB:B9X187, ECO:0000250|UniProtKB:Q6ZQE4}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein
CC {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
CC Nucleus envelope {ECO:0000250|UniProtKB:Q6ZQE4}. Note=Colocalizes with
CC lamins and RAN-GTP at the nuclear envelope.
CC {ECO:0000250|UniProtKB:Q6ZQE4}.
CC -!- DOMAIN: The transmembrane domains are required and sufficient for its
CC oligomerization. {ECO:0000250|UniProtKB:B9X187}.
CC -!- PTM: Phosphorylation may regulate its interaction with RAN-GTP.
CC {ECO:0000250|UniProtKB:Q6ZQE4}.
CC -!- SIMILARITY: Belongs to the NEMP family. {ECO:0000305}.
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DR EMBL; CR858000; CAH90243.1; -; mRNA.
DR RefSeq; NP_001125105.1; NM_001131633.1.
DR AlphaFoldDB; Q5RDB4; -.
DR STRING; 9601.ENSPPYP00000005329; -.
DR GeneID; 100431552; -.
DR KEGG; pon:100431552; -.
DR CTD; 23306; -.
DR eggNOG; KOG3817; Eukaryota.
DR InParanoid; Q5RDB4; -.
DR OrthoDB; 536946at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR019358; NEMP_fam.
DR PANTHER; PTHR13598; PTHR13598; 1.
DR Pfam; PF10225; NEMP; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..444
FT /note="Nuclear envelope integral membrane protein 1"
FT /id="PRO_0000343660"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 186..297
FT /note="A; required for its colocalization with lamins at
FT the nuclear envelope"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQE4"
FT REGION 336..444
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQE4"
FT REGION 336..405
FT /note="B; required for interaction with RAN-GTP"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQE4"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14524"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14524"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14524"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 444 AA; 50724 MW; 777F73250B8BD3E1 CRC64;
MAGGMKVAVS PAVGPGPWGS GVGGGGTVRL LLILSGCLVY GTAEIDVNVV MLQESQVCEK
RASQQFCYTN VLIPKWHDIW TRIQIRVNSS KLVRVTQVEN EQKLKELEQF SIWNFFSSFL
KEKLNDTYVN VGLYSTKTCL KVEIIEKDTK YSVIVIRRFD PKLFLVFLLG LMLFFCGDLL
SRSQIFYYST GMSVGIVASL LIIIFILSKF MPKKSPIYVI LVGGWSFSLY LIQLVFKNLQ
EIWRCYWQYL LSYILTVGFM SFAVCYKYGP LENERSIDLL TWTLQLMGLC FMYSGIQIPH
IALAIIIIAL CTKNLEYPIQ WLYITYRKVC KAAEKPVPPR LLTEEEYRIQ GEVETRKALE
ELREFCNSPD CSAWKTVSRI QSPKRFADFV EGSSHLTPNE VSVHEQEYGL GSIIAQDEIY
EEASSEEEDS YSRCPAITQN NFLT