ID   G3V6W2_RAT              Unreviewed;       417 AA.
AC   G3V6W2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Prolactin regulatory element-binding protein {ECO:0000256|RuleBase:RU369019};
DE   AltName: Full=Mammalian guanine nucleotide exchange factor mSec12 {ECO:0000256|RuleBase:RU369019};
GN   Name=Preb {ECO:0000313|Ensembl:ENSRNOP00000009566.5,
GN   ECO:0000313|RGD:61929};
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 {ECO:0000313|Ensembl:ENSRNOP00000009566.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000009566.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000009566.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000009566.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000009566.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|RuleBase:RU369019}.
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:0000256|RuleBase:RU369019}.
CC   -!- SUBUNIT: Interacts with SAR1B (GDP-bound form). Interacts with MIA2;
CC       recruits PREB to endoplasmic reticulum exit sites.
CC       {ECO:0000256|RuleBase:RU369019}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU369019}; Single-pass membrane protein
CC       {ECO:0000256|RuleBase:RU369019}. Nucleus
CC       {ECO:0000256|RuleBase:RU369019}. Note=Concentrates at endoplasmic
CC       reticulum exit sites (ERES), also known as transitional endoplasmic
CC       reticulum (tER). {ECO:0000256|RuleBase:RU369019}.
CC   -!- SIMILARITY: Belongs to the WD repeat SEC12 family.
CC       {ECO:0000256|RuleBase:RU369019}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU369019}.
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DR   AlphaFoldDB; G3V6W2; -.
DR   SMR; G3V6W2; -.
DR   Ensembl; ENSRNOT00000009565.7; ENSRNOP00000009566.5; ENSRNOG00000007141.7.
DR   RGD; 61929; Preb.
DR   GeneTree; ENSGT00390000018031; -.
DR   HOGENOM; CLU_054579_1_0_1; -.
DR   OMA; YYVQPRI; -.
DR   TreeFam; TF314383; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000007141; Expressed in skeletal muscle tissue and 20 other cell types or tissues.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0032527; P:protein exit from endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0003400; P:regulation of COPII vesicle coating; IEA:UniProtKB-UniRule.
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.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU369019};
KW   Membrane {ECO:0000256|RuleBase:RU369019};
KW   Protein transport {ECO:0000256|RuleBase:RU369019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|RuleBase:RU369019};
KW   Transmembrane {ECO:0000256|RuleBase:RU369019};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU369019};
KW   Transport {ECO:0000256|RuleBase:RU369019};
KW   WD repeat {ECO:0000256|RuleBase:RU369019}.
FT   TRANSMEM        312..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369019"
FT   TRANSMEM        391..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369019"
SQ   SEQUENCE   417 AA;  45371 MW;  8F059A182993C3A9 CRC64;
     MGRRRGVELY RAPFPLYALR IDPKTGLLIA AGGGGAAKTG IKNGVHFLQL EQISGCLSAS
     LLHSHDTETR ATMNLALAGD ILAAGQDAQC QLLRFQIHQQ KGSKAEKSGS KEQGPRQRKG
     AAPAEKKSGA EVHPEGVELK VKNLEAVQTD FSTEPLQKVV CFNHDNTLLA TGGTDGHVRV
     WKVPSLEKVL EFKAHEGEIG DLALGPDGKL VTVGWDFKAS VWQKDQLVTQ LQWQENGPTS
     SNTPYRYQAC RFGQVPDQPG GLRLFTVQIP HKRLRQPPPC YLTAWDSSTF LPLQTRSCGH
     EVISCLTVSE SGTFLGLGTV TGSVAIYIAF SLQRLYYVKE AHGIVVTDVT FLPEKGCGPK
     LLGPHETALF SVAVDSRCQL HLLPSRRSVP VWLLLLLCVG LIIVTILLLQ SAFPGFL
//