PREB_MOUSE
ID PREB_MOUSE Reviewed; 417 AA.
AC Q9WUQ2; Q9QZ99;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Prolactin regulatory element-binding protein;
DE AltName: Full=Mammalian guanine nucleotide exchange factor mSec12;
GN Name=Preb; Synonyms=Sec12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Edgar A.J., Polak J.M.;
RT "The human and mouse homologues of rat prolactin regulatory element binding
RT protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10704286; DOI=10.1006/geno.1999.6089;
RA Taylor Clelland C.L., Craciun L., Bancroft C., Lufkin T.;
RT "Mapping and developmental expression analysis of the WD-repeat gene
RT Preb.";
RL Genomics 63:391-399(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH SAR1B.
RX PubMed=11422940; DOI=10.1034/j.1600-0854.2001.20704.x;
RA Weissman J.T., Plutner H., Balch W.E.;
RT "The mammalian guanine nucleotide exchange factor mSec12 is essential for
RT activation of the Sar1 GTPase directing endoplasmic reticulum export.";
RL Traffic 2:465-475(2001).
RN [5]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-10, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Guanine nucleotide exchange factor that specifically
CC activates the small GTPase SAR1B. Mediates the recruitment of SAR1B and
CC other COPII coat components to endoplasmic reticulum membranes and is
CC therefore required for the formation of COPII transport vesicles from
CC the ER. {ECO:0000269|PubMed:11422940}.
CC -!- FUNCTION: Was first identified based on its probable role in the
CC regulation of pituitary gene transcription. Binds to the prolactin gene
CC (PRL) promoter and seems to activate transcription.
CC {ECO:0000250|UniProtKB:Q9WTV0}.
CC -!- SUBUNIT: Interacts with SAR1B (GDP-bound form) (PubMed:11422940).
CC Interacts with MIA2; recruits PREB to endoplasmic reticulum exit sites
CC (By similarity). {ECO:0000250|UniProtKB:Q9HCU5,
CC ECO:0000269|PubMed:11422940}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9WTV0}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9WTV0}. Nucleus {ECO:0000250|UniProtKB:Q9WTV0}.
CC Note=Concentrates at endoplasmic reticulum exit sites (ERES), also
CC known as transitional endoplasmic reticulum (tER).
CC {ECO:0000250|UniProtKB:Q9HCU5}.
CC -!- DEVELOPMENTAL STAGE: Detected starting at 10.5 dpc in the ectoderm and
CC superficial mesoderm surrounding the caudal part of the tail region. At
CC 12.5 dpc detected in dorsal root ganglia, surface ectoderm surrounding
CC the caudal part of the tail, the inferior wall of the genital tubercle,
CC developing liver, in Rathke pouch and in condensing mesenchyme forming
CC the roof of the skull. At 14.5 dpc detected in the perichondrial region
CC of the craniofacial, axial, and appendicular skeleton. By 16.5 dpc
CC expression is much lower throughout the embryo, and is not detectable
CC by 18.5 dpc. {ECO:0000269|PubMed:10704286}.
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DR EMBL; AF150808; AAD31722.1; -; mRNA.
DR EMBL; AF193017; AAF07954.1; -; mRNA.
DR EMBL; BC017527; AAH17527.1; -; mRNA.
DR CCDS; CCDS39051.1; -.
DR RefSeq; NP_057912.2; NM_016703.3.
DR AlphaFoldDB; Q9WUQ2; -.
DR SMR; Q9WUQ2; -.
DR BioGRID; 206147; 6.
DR IntAct; Q9WUQ2; 3.
DR STRING; 10090.ENSMUSP00000074387; -.
DR iPTMnet; Q9WUQ2; -.
DR PhosphoSitePlus; Q9WUQ2; -.
DR SwissPalm; Q9WUQ2; -.
DR EPD; Q9WUQ2; -.
DR jPOST; Q9WUQ2; -.
DR MaxQB; Q9WUQ2; -.
DR PaxDb; Q9WUQ2; -.
DR PRIDE; Q9WUQ2; -.
DR ProteomicsDB; 289401; -.
DR Antibodypedia; 3012; 116 antibodies from 27 providers.
DR DNASU; 50907; -.
DR Ensembl; ENSMUST00000074840; ENSMUSP00000074387; ENSMUSG00000045302.
DR GeneID; 50907; -.
DR KEGG; mmu:50907; -.
DR UCSC; uc012dui.2; mouse.
DR CTD; 10113; -.
DR MGI; MGI:1355326; Preb.
DR VEuPathDB; HostDB:ENSMUSG00000045302; -.
DR eggNOG; KOG0771; Eukaryota.
DR GeneTree; ENSGT00390000018031; -.
DR HOGENOM; CLU_054579_1_0_1; -.
DR InParanoid; Q9WUQ2; -.
DR OMA; AHCQMYY; -.
DR OrthoDB; 828247at2759; -.
DR PhylomeDB; Q9WUQ2; -.
DR TreeFam; TF314383; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR BioGRID-ORCS; 50907; 23 hits in 77 CRISPR screens.
DR ChiTaRS; Preb; mouse.
DR PRO; PR:Q9WUQ2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9WUQ2; protein.
DR Bgee; ENSMUSG00000045302; Expressed in bone fossa and 269 other tissues.
DR ExpressionAtlas; Q9WUQ2; baseline and differential.
DR Genevisible; Q9WUQ2; MM.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0048208; P:COPII vesicle coating; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR045260; Sec12-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR PANTHER; PTHR23284; PTHR23284; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Nitration; Nucleus; Protein transport; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Transport; WD repeat.
FT CHAIN 1..417
FT /note="Prolactin regulatory element-binding protein"
FT /id="PRO_0000051155"
FT TOPO_DOM 1..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..417
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 152..191
FT /note="WD 1"
FT REPEAT 194..232
FT /note="WD 2"
FT REPEAT 298..337
FT /note="WD 3"
FT REGION 101..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT CONFLICT 136
FT /note="Missing (in Ref. 2; AAF07954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 45437 MW; 89F8B24F9A7684FA CRC64;
MGRRRGVELY RAPFPLYALR IDPKTGLLIA AGGGGAAKTG IKNGVHFLQL ELINGCLSAS
LLHSHDTETR ATMNLALAGD ILAAGQDAQC QLLRFQVHQQ KGSKAEKSGS KEQGPRQRKG
APPAEKKSGA QVHPEGVELK VKNLEAVQTD FSNEPLQKVV CFNHDNTLLA TGGTDGHVRV
WKVPSLEKVL EFKAHEGEIG DLTLGPDGKL VTVGWDFKAS VWQKDQLVTQ LQWQENGPAS
SNTPYRYQAC RFGQVPDQLG GLRLFTVQIP HKRLRQPPPC YLTAWDSSTF LPLRTRSCGH
EVISCLSVSD SGTFLGLGTV TGSVAIYIAF SLQRLYYVKE AHGIVVTDVT FLPEKGCGPK
LLGPHETALF SVAVDSRCQL HLLPSRRSVP VWLLLLLCVG LIIVTILLLQ TAFPGFL
