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NEMP1_BOVIN
ID   NEMP1_BOVIN             Reviewed;         445 AA.
AC   A7MBC7;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Nuclear envelope integral membrane protein 1;
DE   Flags: Precursor;
GN   Name=NEMP1; Synonyms=TMEM194A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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; BC151486; AAI51487.1; -; mRNA.
DR   RefSeq; NP_001095631.1; NM_001102161.1.
DR   AlphaFoldDB; A7MBC7; -.
DR   STRING; 9913.ENSBTAP00000019519; -.
DR   PaxDb; A7MBC7; -.
DR   PRIDE; A7MBC7; -.
DR   Ensembl; ENSBTAT00000019519; ENSBTAP00000019519; ENSBTAG00000014659.
DR   GeneID; 533988; -.
DR   KEGG; bta:533988; -.
DR   CTD; 23306; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014659; -.
DR   VGNC; VGNC:56223; NEMP1.
DR   eggNOG; KOG3817; Eukaryota.
DR   GeneTree; ENSGT00390000002174; -.
DR   HOGENOM; CLU_025225_0_0_1; -.
DR   InParanoid; A7MBC7; -.
DR   OMA; MAGCMKM; -.
DR   OrthoDB; 536946at2759; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000014659; Expressed in oocyte and 103 other tissues.
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   GO; GO:0071763; P:nuclear membrane organization; IEA:Ensembl.
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..44
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..445
FT                   /note="Nuclear envelope integral membrane protein 1"
FT                   /id="PRO_0000343659"
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..445
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   REGION          418..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   445 AA;  50958 MW;  7DD73BB3322BA8A4 CRC64;
     MAGGMKVAVL PAVGAGPWSW GAGGCGAVRL LLVLFGCFVC GSAGIDLNVV TLRESEILFM
     NTSRQSCYKN VLIPKWHDIW TRIQIRVNSS KLVRVTQVEN EDKLKELEQF SIWNFFSSFL
     KEKLNDTYIN VGLYSTKTCL KVEILEEDTK YSVIVTRRFD PKLFLIFLLG LTLFFCGDLL
     SRSQIFYYST GMSVGIVASL LIIIFIVSKF MPKKSPIYII LVGGWSFSLY LIQLVFKNLQ
     EIWRCYWQYL LSYVLAVGFM SFAVCYKYGP LENERSINLL TWTLQLLGLC FMYSSIQIPH
     IALAIVVIAL CTKNLDYPIH WLYITYRKMC KATEKTVPPR LLTEEEYRLQ GEVETRKALE
     QLREYCNSPD CSAWKTVSRI QSPKRFADFV EGSFHLTPNE VSVHEQEYGL GSIIAQDELS
     EETSSEEEDS DSRYPLVVQQ NSFLT
 
 
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