ID PREB_RAT Reviewed; 417 AA.
AC Q9WTV0; Q6AYS1;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 24-JAN-2024, entry version 147.
DE RecName: Full=Prolactin regulatory element-binding protein;
DE AltName: Full=Mammalian guanine nucleotide exchange factor mSec12;
GN Name=Preb; Synonyms=Sec12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar Furth; TISSUE=Pituitary;
RX PubMed=10194769; DOI=10.1210/mend.13.4.0260;
RA Fliss M.S., Hinkle P.M., Bancroft C.;
RT "Expression cloning and characterization of PREB (prolactin regulatory
RT element binding), a novel WD motif DNA-binding protein with a capacity to
RT regulate prolactin promoter activity.";
RL Mol. Endocrinol. 13:644-657(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
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).
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:0000269|PubMed:10194769}.
CC -!- SUBUNIT: Interacts with SAR1B (GDP-bound form) (By similarity).
CC Interacts with MIA2; recruits PREB to endoplasmic reticulum exit sites
CC (By similarity). Interacts with CIDEB; facilitating loading of SCAP-
CC SREBP into COPII vesicles (By similarity).
CC {ECO:0000250|UniProtKB:Q9HCU5, ECO:0000250|UniProtKB:Q9WUQ2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11422940}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11422940}. Nucleus {ECO:0000269|PubMed:10194769}.
CC Note=Concentrates at endoplasmic reticulum exit sites (ERES), also
CC known as transitional endoplasmic reticulum (tER).
CC {ECO:0000250|UniProtKB:Q9HCU5}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF061817; AAD28300.1; -; mRNA.
DR EMBL; BC078936; AAH78936.1; -; mRNA.
DR RefSeq; NP_001164179.1; NM_001170708.1.
DR AlphaFoldDB; Q9WTV0; -.
DR SMR; Q9WTV0; -.
DR STRING; 10116.ENSRNOP00000009566; -.
DR iPTMnet; Q9WTV0; -.
DR PhosphoSitePlus; Q9WTV0; -.
DR jPOST; Q9WTV0; -.
DR PaxDb; 10116-ENSRNOP00000009566; -.
DR GeneID; 58842; -.
DR KEGG; rno:58842; -.
DR AGR; RGD:61929; -.
DR CTD; 10113; -.
DR RGD; 61929; Preb.
DR eggNOG; KOG0771; Eukaryota.
DR InParanoid; Q9WTV0; -.
DR OrthoDB; 2727235at2759; -.
DR PhylomeDB; Q9WTV0; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR PRO; PR:Q9WTV0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0048208; P:COPII vesicle coating; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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_rpt.
DR PANTHER; PTHR23284; PROLACTIN REGULATORY ELEMENT BINDING PROTEIN; 1.
DR PANTHER; PTHR23284:SF0; PROLACTIN REGULATORY ELEMENT-BINDING PROTEIN; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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_0000051156"
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 MOD_RES 10
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUQ2"
FT CONFLICT 52..54
FT /note="QIS -> LIN (in Ref. 1; AAD28300)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="I -> V (in Ref. 1; AAD28300)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="A -> P (in Ref. 1; AAD28300)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="E -> Q (in Ref. 1; AAD28300)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="T -> N (in Ref. 1; AAD28300)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="S -> T (in Ref. 1; AAD28300)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="Q -> R (in Ref. 1; AAD28300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 45357 MW; 8F059A196CC696FE CRC64;
MGRRRGVELY RAPFPLYALR IDPKTGLLIA AGGGGAAKTG IKNGVHFLQL EQISGCLSAS
LLHSHDTETR ATMNLALAGD ILAAGQDAQC QLLRFQIHQQ KGSKAEKSGS KEQGPRQRKG
AAPAEKKSGA EVHPEGVELK VKNLEAVQTD FSTEPLQKVV CFNHDNTLLA TGGSDGHVRV
WKVPSLEKVL EFKAHEGEIG DLALGPDGKL VTVGWDFKAS VWQKDQLVTQ LQWQENGPTS
SNTPYRYQAC RFGQVPDQPG GLRLFTVQIP HKRLRQPPPC YLTAWDSSTF LPLQTRSCGH
EVISCLTVSE SGTFLGLGTV TGSVAIYIAF SLQRLYYVKE AHGIVVTDVT FLPEKGCGPK
LLGPHETALF SVAVDSRCQL HLLPSRRSVP VWLLLLLCVG LIIVTILLLQ SAFPGFL
//
