CRERF_HUMAN
ID CRERF_HUMAN Reviewed; 639 AA.
AC Q8IUR6; B3DFH2; B3KW49; D3DQM2; F5GXN3; Q5HYG4; Q5HYK0; Q86YR3; Q8IZG1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=CREB3 regulatory factor;
DE AltName: Full=Luman recruitment factor;
DE Short=LRF;
GN Name=CREBRF; Synonyms=C5orf41;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP CREB3, SUBCELLULAR LOCATION, AND INDUCTION.
RC TISSUE=Cervix carcinoma, and Retina;
RX PubMed=18391022; DOI=10.1128/mcb.01439-07;
RA Audas T.E., Li Y., Liang G., Lu R.;
RT "A novel protein, Luman/CREB3 recruitment factor, inhibits Luman activation
RT of the unfolded protein response.";
RL Mol. Cell. Biol. 28:3952-3966(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-483.
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-602 (ISOFORM 3).
RC TISSUE=Adipose tissue, and Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
CC -!- FUNCTION: Acts as a negative regulator of the endoplasmic reticulum
CC stress response or unfolded protein response (UPR). Represses the
CC transcriptional activity of CREB3 during the UPR. Recruits CREB3 into
CC nuclear foci. {ECO:0000269|PubMed:18391022}.
CC -!- SUBUNIT: Interacts (via leucine-zipper domain) with CREB3 (via leucine-
CC zipper domain); the interaction promotes CREB3 degradation.
CC {ECO:0000269|PubMed:18391022}.
CC -!- INTERACTION:
CC Q8IUR6; O43889-2: CREB3; NbExp=4; IntAct=EBI-1042699, EBI-625022;
CC Q8IUR6; O60519: CREBL2; NbExp=5; IntAct=EBI-1042699, EBI-2872455;
CC Q8IUR6; Q14451-3: GRB7; NbExp=3; IntAct=EBI-1042699, EBI-11991632;
CC Q8IUR6; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-1042699, EBI-10172526;
CC Q8IUR6; P41227: NAA10; NbExp=3; IntAct=EBI-1042699, EBI-747693;
CC Q8IUR6; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-1042699, EBI-2585120;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18391022}.
CC Note=Colocalizes with CREB3 in nuclear foci.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IUR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IUR6-2; Sequence=VSP_027601, VSP_027602;
CC Name=3;
CC IsoId=Q8IUR6-3; Sequence=VSP_027603;
CC -!- INDUCTION: Up-regulated by endoplasmic reticulum stress.
CC {ECO:0000269|PubMed:18391022}.
CC -!- PTM: Probably degraded by the proteasome.
CC -!- SIMILARITY: Belongs to the bZIP family. CREBRF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AC008378; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY139008; AAN28956.1; -; mRNA.
DR EMBL; AY174896; AAO18732.1; -; mRNA.
DR EMBL; AY635785; AAV34175.1; -; mRNA.
DR EMBL; AK124117; BAG54011.1; -; mRNA.
DR EMBL; AC008378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61414.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61415.1; -; Genomic_DNA.
DR EMBL; BC041709; AAH41709.1; -; mRNA.
DR EMBL; BX647768; CAI46039.1; -; mRNA.
DR EMBL; BX647573; CAI46104.1; -; mRNA.
DR CCDS; CCDS34293.1; -. [Q8IUR6-1]
DR CCDS; CCDS54948.1; -. [Q8IUR6-2]
DR RefSeq; NP_001161865.1; NM_001168393.1. [Q8IUR6-2]
DR RefSeq; NP_001161866.1; NM_001168394.1. [Q8IUR6-2]
DR RefSeq; NP_705835.2; NM_153607.2. [Q8IUR6-1]
DR RefSeq; XP_006714885.1; XM_006714822.3. [Q8IUR6-1]
DR AlphaFoldDB; Q8IUR6; -.
DR SMR; Q8IUR6; -.
DR BioGRID; 127485; 10.
DR IntAct; Q8IUR6; 8.
DR STRING; 9606.ENSP00000296953; -.
DR GlyGen; Q8IUR6; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8IUR6; -.
DR PhosphoSitePlus; Q8IUR6; -.
DR BioMuta; CREBRF; -.
DR DMDM; 158563850; -.
DR MassIVE; Q8IUR6; -.
DR MaxQB; Q8IUR6; -.
DR PaxDb; Q8IUR6; -.
DR PeptideAtlas; Q8IUR6; -.
DR PRIDE; Q8IUR6; -.
DR ProteomicsDB; 70604; -. [Q8IUR6-1]
DR ProteomicsDB; 70605; -. [Q8IUR6-2]
DR ProteomicsDB; 70606; -. [Q8IUR6-3]
DR Antibodypedia; 28933; 28 antibodies from 12 providers.
DR DNASU; 153222; -.
DR Ensembl; ENST00000296953.6; ENSP00000296953.2; ENSG00000164463.12. [Q8IUR6-1]
DR Ensembl; ENST00000520420.5; ENSP00000428290.1; ENSG00000164463.12. [Q8IUR6-2]
DR Ensembl; ENST00000522692.5; ENSP00000431107.1; ENSG00000164463.12. [Q8IUR6-2]
DR GeneID; 153222; -.
DR KEGG; hsa:153222; -.
DR MANE-Select; ENST00000296953.6; ENSP00000296953.2; NM_153607.3; NP_705835.2.
DR UCSC; uc003mcf.3; human. [Q8IUR6-1]
DR CTD; 153222; -.
DR DisGeNET; 153222; -.
DR GeneCards; CREBRF; -.
DR HGNC; HGNC:24050; CREBRF.
DR HPA; ENSG00000164463; Tissue enhanced (bone).
DR neXtProt; NX_Q8IUR6; -.
DR OpenTargets; ENSG00000164463; -.
DR PharmGKB; PA162380187; -.
DR VEuPathDB; HostDB:ENSG00000164463; -.
DR eggNOG; ENOG502QTAK; Eukaryota.
DR GeneTree; ENSGT00390000007125; -.
DR HOGENOM; CLU_791197_0_0_1; -.
DR InParanoid; Q8IUR6; -.
DR OMA; ECETVHS; -.
DR OrthoDB; 252839at2759; -.
DR PhylomeDB; Q8IUR6; -.
DR TreeFam; TF330810; -.
DR PathwayCommons; Q8IUR6; -.
DR Reactome; R-HSA-8874211; CREB3 factors activate genes.
DR SignaLink; Q8IUR6; -.
DR SIGNOR; Q8IUR6; -.
DR BioGRID-ORCS; 153222; 9 hits in 1076 CRISPR screens.
DR ChiTaRS; CREBRF; human.
DR GenomeRNAi; 153222; -.
DR Pharos; Q8IUR6; Tbio.
DR PRO; PR:Q8IUR6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8IUR6; protein.
DR Bgee; ENSG00000164463; Expressed in calcaneal tendon and 190 other tissues.
DR ExpressionAtlas; Q8IUR6; baseline and differential.
DR Genevisible; Q8IUR6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032388; P:positive regulation of intracellular transport; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0051222; P:positive regulation of protein transport; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR039165; CREBRF.
DR PANTHER; PTHR21552; PTHR21552; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Repressor;
KW Stress response; Transcription; Transcription regulation; Transport;
KW Unfolded protein response.
FT CHAIN 1..639
FT /note="CREB3 regulatory factor"
FT /id="PRO_0000299306"
FT DOMAIN 521..584
FT /note="bZIP"
FT REGION 302..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..532
FT /note="Basic motif"
FT /evidence="ECO:0000250"
FT REGION 533..540
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250"
FT COMPBIAS 311..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 409..417
FT /note="YENDSVEDL -> IIMLASLPD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18391022"
FT /id="VSP_027601"
FT VAR_SEQ 418..639
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18391022"
FT /id="VSP_027602"
FT VAR_SEQ 472
FT /note="H -> HGK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_027603"
FT VARIANT 483
FT /note="T -> A (in dbSNP:rs17854147)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034795"
FT CONFLICT 232
FT /note="K -> R (in Ref. 6; CAI46104)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="D -> G (in Ref. 1; AAN28956)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="N -> D (in Ref. 6; CAI46104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 72149 MW; 878B8F6FFB9A67CA CRC64;
MPQPSVSGMD PPFGDAFRSH TFSEQTLMST DLLANSSDPD FMYELDREMN YQQNPRDNFL
SLEDCKDIEN LESFTDVLDN EGALTSNWEQ WDTYCEDLTK YTKLTSCDIW GTKEVDYLGL
DDFSSPYQDE EVISKTPTLA QLNSEDSQSV SDSLYYPDSL FSVKQNPLPS SFPGKKITSR
AAAPVCSSKT LQAEVPLSDC VQKASKPTSS TQIMVKTNMY HNEKVNFHVE CKDYVKKAKV
KINPVQQSRP LLSQIHTDAA KENTCYCGAV AKRQEKKGME PLQGHATPAL PFKETQELLL
SPLPQEGPGS LAAGESSSLS ASTSVSDSSQ KKEEHNYSLF VSDNLGEQPT KCSPEEDEED
EEDVDDEDHD EGFGSEHELS ENEEEEEEEE DYEDDKDDDI SDTFSEPGYE NDSVEDLKEV
TSISSRKRGK RRYFWEYSEQ LTPSQQERML RPSEWNRDTL PSNMYQKNGL HHGKYAVKKS
RRTDVEDLTP NPKKLLQIGN ELRKLNKVIS DLTPVSELPL TARPRSRKEK NKLASRACRL
KKKAQYEANK VKLWGLNTEY DNLLFVINSI KQEIVNRVQN PRDERGPNMG QKLEILIKDT
LGLPVAGQTS EFVNQVLEKT AEGNPTGGLV GLRIPTSKV
