REEP4_XENLA
ID REEP4_XENLA Reviewed; 261 AA.
AC Q6AZM3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Receptor expression-enhancing protein 4;
GN Name=reep4;
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 [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19123125; DOI=10.1387/ijdb.072542ja;
RA Argasinska J., Rana A.A., Gilchrist M.J., Lachani K., Young A., Smith J.C.;
RT "Loss of REEP4 causes paralysis of the Xenopus embryo.";
RL Int. J. Dev. Biol. 53:37-43(2009).
RN [3]
RP INTERACTION WITH MICROTUBULES, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23911198; DOI=10.1016/j.devcel.2013.06.016;
RA Schlaitz A.L., Thompson J., Wong C.C., Yates J.R. III, Heald R.;
RT "REEP3/4 ensure endoplasmic reticulum clearance from metaphase chromatin
RT and proper nuclear envelope architecture.";
RL Dev. Cell 26:315-323(2013).
CC -!- FUNCTION: Microtubule-binding protein required to ensure proper cell
CC division and nuclear envelope reassembly by sequestering the
CC endoplasmic reticulum away from chromosomes during mitosis. Probably
CC acts by clearing the endoplasmic reticulum membrane from metaphase
CC chromosomes (By similarity). May play a role in the maintenance of both
CC the nervous system and the musculature. {ECO:0000250,
CC ECO:0000269|PubMed:19123125}.
CC -!- SUBUNIT: Interacts with microtubules. {ECO:0000269|PubMed:23911198}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: During gastrulation, expressed on the dorsal side
CC of the embryo and then in the neural plate and neural tube. At tailbud
CC stages, expressed in the somites, neural tube and otic vesicle.
CC {ECO:0000269|PubMed:19123125}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically. Maternal
CC expression declines during cleavage stages and gastrulation. Expression
CC then increases during neurula and tailbud stages.
CC {ECO:0000269|PubMed:19123125}.
CC -!- MISCELLANEOUS: Inactivation in embryos by antisense morpholino causes
CC paralysis and shortening of the body axis.
CC {ECO:0000305|PubMed:19123125}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
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DR EMBL; BC077625; AAH77625.1; -; mRNA.
DR RefSeq; NP_001086898.1; NM_001093429.1.
DR AlphaFoldDB; Q6AZM3; -.
DR DNASU; 446733; -.
DR GeneID; 446733; -.
DR KEGG; xla:446733; -.
DR CTD; 446733; -.
DR Xenbase; XB-GENE-982265; reep4.S.
DR OMA; WTSHGVP; -.
DR OrthoDB; 1473891at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 446733; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR PANTHER; PTHR12300; PTHR12300; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Endoplasmic reticulum; Membrane; Microtubule;
KW Mitosis; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..261
FT /note="Receptor expression-enhancing protein 4"
FT /id="PRO_0000424023"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 167..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 261 AA; 29821 MW; F489C831C0D5B71C CRC64;
MVSWIISRAV VLVFGLLYPA YASYKAVKTK NVRDYVRWMM YWIVFALFMT VETFTDIFIA
WFPFYYEIKM AFVVWLLSPY TRGASLLYRK CIHPTLSLKE KEIDSYIIQA KERSYESFVN
IGRKGLNIAA SAAVQAATKG QGALVGRLRS FSMQDLRALP DDTPIHYTDA LYPDEPQLHR
RPMGFPTTSQ ADSDSMDERW SDSEIAETRT AARTRGGMPS KSLQRSQSLR VSKKKGLSRE
VSTKTTKPRA KKKPAQSEPE N