NMP1B_XENLA
ID NMP1B_XENLA Reviewed; 434 AA.
AC A1L3G9; B9X188;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Nuclear envelope integral membrane protein 1b;
DE Flags: Precursor;
GN Name=nemp1b; Synonyms=tmem194a-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL
RP STAGE, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH BANF1-A AND
RP BANF1-B.
RX PubMed=19167377; DOI=10.1016/j.ydbio.2008.12.038;
RA Mamada H., Takahashi N., Taira M.;
RT "Involvement of an inner nuclear membrane protein, Nemp1, in Xenopus neural
RT development through an interaction with the chromatin protein BAF.";
RL Dev. Biol. 327:497-507(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL,
RP INTERACTION WITH RAN, AND PHOSPHORYLATION.
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 -!- FUNCTION: In concert with ran, required for proper eye development
CC (PubMed:25946333). May be involved in the expression of early eye
CC marker genes (PubMed:19167377). {ECO:0000269|PubMed:19167377,
CC ECO:0000269|PubMed:25946333}.
CC -!- SUBUNIT: Interacts with banf1-a and banf1-b. Interacts with ran-gtp.
CC {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}; Multi-pass
CC membrane protein {ECO:0000255}; Nucleoplasmic side
CC {ECO:0000269|PubMed:19167377}. Nucleus envelope
CC {ECO:0000269|PubMed:19167377}. Note=Localization in the nuclear
CC membrane is essential for its function. Colocalizes with lamins and
CC banf1-a/b at the nuclear envelope. {ECO:0000269|PubMed:19167377,
CC ECO:0000269|PubMed:25946333}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. At the
CC early gastrula stage, expressed mainly in the entire animal hemisphere.
CC During neurulation, its expression becomes restricted to the anterior
CC neuroectoderm. At the tailbud stage, expressed in various anterior
CC regions including the anterior central nervous system (CNS), otic
CC vesicles, and branchial arches. {ECO:0000269|PubMed:19167377}.
CC -!- DOMAIN: The transmembrane domains are required and sufficient for its
CC oligomerization. {ECO:0000269|PubMed:25946333}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:25946333}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in defects in eye
CC development, reduced expression of early eye marker genes rax, tbx3,
CC six3 and pax6 and reduction of cell density at the neurula stage. Co-
CC knockdown of nemp1b and ran elicits reduction of cell density and eye
CC defects more significantly than the individual knockdown of either one.
CC {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}.
CC -!- SIMILARITY: Belongs to the NEMP family. {ECO:0000305}.
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DR EMBL; AB474920; BAH24056.1; -; mRNA.
DR EMBL; BC130092; AAI30093.1; -; mRNA.
DR RefSeq; NP_001091224.1; NM_001097755.1.
DR AlphaFoldDB; A1L3G9; -.
DR BioGRID; 674282; 3.
DR IntAct; A1L3G9; 3.
DR DNASU; 100037004; -.
DR GeneID; 100037004; -.
DR KEGG; xla:100037004; -.
DR CTD; 100037004; -.
DR Xenbase; XB-GENE-974580; nemp1.L.
DR OrthoDB; 536946at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 100037004; Expressed in egg cell and 18 other tissues.
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; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR InterPro; IPR019358; NEMP_fam.
DR PANTHER; PTHR13598; PTHR13598; 1.
DR Pfam; PF10225; NEMP; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Membrane; Nucleus; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..434
FT /note="Nuclear envelope integral membrane protein 1b"
FT /id="PRO_0000332241"
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 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
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:0000269|PubMed:25946333"
FT REGION 326..434
FT /note="Interaction with banf1-a and banf1-b"
FT /evidence="ECO:0000269|PubMed:19167377"
FT REGION 326..395
FT /note="B; interaction with ran"
FT /evidence="ECO:0000269|PubMed:25946333"
FT REGION 368..375
FT /note="BAF-binding site (BBS); essential for interaction
FT with banf1-a, banf1-b and ran"
FT /evidence="ECO:0000269|PubMed:19167377,
FT ECO:0000269|PubMed:25946333"
FT MOTIF 317..325
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:25946333"
SQ SEQUENCE 434 AA; 50327 MW; 258089C9B16BA011 CRC64;
MAGEVEGRGC GFSLGVLVTL LVLPLPSLCT LSTEKELHVI KLYEGRMVRY NESRNFCYQR
TYEPKWSDVW TKIQIRINST KMIRVTQVDN EEKLKEMETF NMFDFFSSFL KEKLNDTFIY
VNLYSNKTCV KVHLTDTDTY YSVALSRGFD PRLFFVFLCG LLLFFYGDTL SRSQLFFYST
GITVGMLASM LILVFMLSKL MPKKSPFFAL LLGGWSVSIY VIQLVFRNLQ AICSEYWQYL
IVYLGIVGFV SFAFCYIYGP LENERSINIL NWTLQLIGLL LMYVSVQIQH IAVTIVVIAF
CTKQIEYPVQ WIYILYRKIK LKRAKPGPPR LLTEEEYRKQ ADVETRKALE ELRECCSSPD
FAAWKTISRI QSPKRFADFV EGSSHLTPNE VSVHEHEYGL GGSFLEDELF GEDSDVEEEM
EIEPPLYPIP RSVF
