ID   NEMP1_XENTR             Reviewed;         431 AA.
AC   Q28EH9; Q5BJ84;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Nuclear envelope integral membrane protein 1;
DE   Flags: Precursor;
GN   Name=nemp1; Synonyms=tmem194a; ORFNames=TTpA010p19.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Embryo, and Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In concert with ran, required for proper eye development. May
CC       be involved in the expression of early eye marker genes.
CC       {ECO:0000250|UniProtKB:B9X187}.
CC   -!- SUBUNIT: Homooligomer. Interacts with banf1-a and banf1-b. Interacts
CC       with ran-gtp. {ECO:0000250|UniProtKB:B9X187}.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC       {ECO:0000250|UniProtKB:B9X187}; Multi-pass membrane protein
CC       {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
CC       Nucleus envelope {ECO:0000250|UniProtKB:B9X187}. Note=Localization in
CC       the nuclear membrane is essential for its function. Colocalizes with
CC       and lamins and banf1-a/b at the nuclear envelope.
CC       {ECO:0000250|UniProtKB:B9X187}.
CC   -!- DOMAIN: The transmembrane domains are required and sufficient for its
CC       oligomerization. {ECO:0000250|UniProtKB:B9X187}.
CC   -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:B9X187}.
CC   -!- SIMILARITY: Belongs to the NEMP family. {ECO:0000305}.
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DR   EMBL; CR848245; CAJ82959.1; -; mRNA.
DR   EMBL; BC091583; AAH91583.2; -; mRNA.
DR   EMBL; BC121559; AAI21560.1; -; mRNA.
DR   RefSeq; NP_001034832.1; NM_001039743.1.
DR   AlphaFoldDB; Q28EH9; -.
DR   STRING; 8364.ENSXETP00000009646; -.
DR   PaxDb; Q28EH9; -.
DR   GeneID; 594887; -.
DR   KEGG; xtr:594887; -.
DR   CTD; 23306; -.
DR   Xenbase; XB-GENE-974573; nemp1.
DR   eggNOG; KOG3817; Eukaryota.
DR   HOGENOM; CLU_025225_0_0_1; -.
DR   InParanoid; Q28EH9; -.
DR   OMA; INILNWT; -.
DR   OrthoDB; 536946at2759; -.
DR   PhylomeDB; Q28EH9; -.
DR   TreeFam; TF314831; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; 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; ISS:UniProtKB.
DR   GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR   InterPro; IPR019358; NEMP_fam.
DR   PANTHER; PTHR13598; PTHR13598; 1.
DR   Pfam; PF10225; NEMP; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Membrane; Nucleus; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..431
FT                   /note="Nuclear envelope integral membrane protein 1"
FT                   /id="PRO_0000332242"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          176..287
FT                   /note="A; required for its colocalization with lamins at
FT                   the nuclear envelope"
FT                   /evidence="ECO:0000250|UniProtKB:B9X187"
FT   REGION          326..431
FT                   /note="Interaction with banf1-a and banf1-b"
FT                   /evidence="ECO:0000250|UniProtKB:B9X187"
FT   REGION          326..395
FT                   /note="B; required for interaction with ran"
FT                   /evidence="ECO:0000250|UniProtKB:B9X187"
FT   REGION          368..375
FT                   /note="BAF-binding site (BBS); essential for interaction
FT                   with banf1-a, banf1-b and ran"
FT                   /evidence="ECO:0000250|UniProtKB:B9X187"
FT   MOTIF           317..325
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:B9X187"
SQ   SEQUENCE   431 AA;  49962 MW;  28862C07383BDD30 CRC64;
     MAGEVEGEGC RVSWGVLVAL LLLPLPSLCS LTAGKQLQVI KLFEGRVVRY NESKNFCYQR
     TYEPKWSDVW TKIQIRVNST KMIRVTQVEN EEKLKEMETF NMFDFFSSFL KEKLNDSFIY
     VDLYNNKTCI KVHVSDTDTY YSVALSRGFD PRLFFVFLCG LLLFFYGDTL SRSQIFYYST
     GITVGMLASM LILVFMLSKL MPKKSPFVAL LLGGWSVSIY VIQLVFKNLQ AICTEYWQYL
     LGYLGIVGFV SFAFCYKYGP LENERSINIL NWTLQLIGLL LMYISVQIRH IAVTMVVIAF
     CTKQIEYPVR WIYILYRKIK LKRGKPSPPR LLTEEEYRKQ GDVETRKALE ELRGYCSSPD
     FAAWKTVSRI QSPKRFADFV EGSSHLTPNE VSVHEHEYGF GGSFLEDELF GEDSDVEEEM
     EIEPVLYQDL R