QRIC1_MOUSE
ID QRIC1_MOUSE Reviewed; 777 AA.
AC Q3UA37;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Transcriptional regulator QRICH1 {ECO:0000305};
DE AltName: Full=Glutamine-rich protein 1;
GN Name=Qrich1 {ECO:0000312|MGI:MGI:1916482};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, Spleen, 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).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30281152; DOI=10.1111/cge.13457;
RA Lui J.C., Jee Y.H., Lee A., Yue S., Wagner J., Donnelly D.E., Vogt K.S.,
RA Baron J.;
RT "QRICH1 mutations cause a chondrodysplasia with developmental delay.";
RL Clin. Genet. 95:160-164(2019).
RN [4]
RP FUNCTION, INDUCTION BY ER STRESS, AND DOMAIN.
RX PubMed=33384352; DOI=10.1126/science.abb6896;
RA You K., Wang L., Chou C.H., Liu K., Nakata T., Jaiswal A., Yao J.,
RA Lefkovith A., Omar A., Perrigoue J.G., Towne J.E., Regev A., Graham D.B.,
RA Xavier R.J.;
RT "QRICH1 dictates the outcome of ER stress through transcriptional control
RT of proteostasis.";
RL Science 371:0-0(2021).
CC -!- FUNCTION: Transcriptional regulator that acts as a mediator of the
CC integrated stress response (ISR) through transcriptional control of
CC protein homeostasis under conditions of ER stress (PubMed:33384352).
CC Controls the outcome of the unfolded protein response (UPR), an ER-
CC stress response pathway that either promotes recovery of ER homeostasis
CC and cell survival, or triggers the terminal UPR which elicits
CC programmed cell death when ER stress is prolonged and unresolved
CC (PubMed:33384352). ER stress induces QRICH1 translation by a ribosome
CC translation re-initiation mechanism in response to EIF2S1/eIF-2-alpha
CC phosphorylation, and stress-induced QRICH1 regulates a transcriptional
CC program associated with protein translation, protein secretion-mediated
CC proteotoxicity and cell death during the terminal UPR (By similarity).
CC May cooperate with ATF4 transcription factor signaling to regulate ER
CC homeostasis which is critical for cell viability (By similarity). Up-
CC regulates CASP3/caspase-3 activity in epithelial cells under ER stress.
CC Central regulator of proteotoxicity associated with ER stress-mediated
CC inflammatory diseases in the intestines and liver (PubMed:33384352).
CC Involved in chondrocyte hypertrophy, a process required for normal
CC longitudinal bone growth (PubMed:30281152).
CC {ECO:0000250|UniProtKB:Q2TAL8, ECO:0000269|PubMed:30281152,
CC ECO:0000269|PubMed:33384352}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2TAL8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q2TAL8}. Cell membrane
CC {ECO:0000250|UniProtKB:Q2TAL8}.
CC -!- TISSUE SPECIFICITY: Expressed highly in prefrontal cortex, craniofacial
CC area and near the limbs of mouse embryos. Expressed in heart, skeletal
CC muscle, liver, kidney, lung, brain, spleen, intestine and growth plate
CC in mice. {ECO:0000269|PubMed:30281152}.
CC -!- DOMAIN: The CARD domain may be involved in the regulation of caspase
CC activity in the context of programmed cell death.
CC {ECO:0000250|UniProtKB:Q2TAL8}.
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DR EMBL; AK151491; BAE30444.1; -; mRNA.
DR EMBL; AK151530; BAE30478.1; -; mRNA.
DR CCDS; CCDS52927.1; -.
DR RefSeq; NP_001107591.1; NM_001114119.1.
DR RefSeq; NP_780352.2; NM_175143.5.
DR AlphaFoldDB; Q3UA37; -.
DR SMR; Q3UA37; -.
DR BioGRID; 213306; 3.
DR IntAct; Q3UA37; 2.
DR MINT; Q3UA37; -.
DR STRING; 10090.ENSMUSP00000006851; -.
DR iPTMnet; Q3UA37; -.
DR PhosphoSitePlus; Q3UA37; -.
DR EPD; Q3UA37; -.
DR MaxQB; Q3UA37; -.
DR PaxDb; Q3UA37; -.
DR PeptideAtlas; Q3UA37; -.
DR PRIDE; Q3UA37; -.
DR ProteomicsDB; 300368; -.
DR DNASU; 69232; -.
DR GeneID; 69232; -.
DR KEGG; mmu:69232; -.
DR CTD; 54870; -.
DR MGI; MGI:1916482; Qrich1.
DR eggNOG; ENOG502QU8W; Eukaryota.
DR InParanoid; Q3UA37; -.
DR OrthoDB; 587724at2759; -.
DR PhylomeDB; Q3UA37; -.
DR BioGRID-ORCS; 69232; 10 hits in 71 CRISPR screens.
DR ChiTaRS; Qrich1; mouse.
DR PRO; PR:Q3UA37; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UA37; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:0140467; P:integrated stress response signaling; ISS:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0036499; P:PERK-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR InterPro; IPR021893; DUF3504.
DR Pfam; PF12012; DUF3504; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Unfolded protein response.
FT CHAIN 1..777
FT /note="Transcriptional regulator QRICH1"
FT /id="PRO_0000269854"
FT DOMAIN 6..48
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 140..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q2TAL8"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TAL8"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TAL8"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q2TAL8"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q2TAL8"
SQ SEQUENCE 777 AA; 86556 MW; 18D47BDB95A2507A CRC64;
MNNSLENTIS FEEYIRVKAR SVPQHRMKEF LDSLASKGPE ALQEFQQTAT TTMVYQQGGN
CIYTDSTEVA GSLLELACPV TTSVQPQTQQ EQQIQVQQPQ QVQVQVQVQQ SPQQVSAQQL
SPQFTVHQPA EQPIQVQVQI QGQAPQSAAP SIQTPSLQSP SPSQLQAAQI QVQHVQAAQQ
IQAAEIPEEH IPHQQIQAQL VAGQSLAGGQ QIQIQTVGAL SPPPSQQGSP REGERRVGTA
SVLQPVKKRK VDMPITVSYA ISGQPVATVL AIPQGQQQSY VSLRPDLLTV DSAHLYSATG
TITSPTGETW TIPVYSAQPR GDPQQQSITH IAIPQEAYNA VHVSGSPKAL AAVKLEDDKE
KMVGTTSVVK NSHEEVVQTL ANSLFPAQFM NGNIHIPVAV QAVAGTYQNT AQTVHIWDPQ
QQPQQQTAQE QTPPPQQQQQ QLQVTCSAQT VQVAEVEPQS QPQPSPELLL PNSLKPEEGL
EVWKNWAQTK NAELEKDAQN RLAPIGRRQL LRFQEDLISS AVAELNYGLC LMTREARNGE
GEPYDPDVLY YIFLCIQKYL FENGRVDDIF SDLYYVRFTE WLHEVLKDVQ PRVTPLGYVL
PSHVTEEMLW ECKQLGAHSP STLLTTLMFF NTKYFLLKTV DQHMKLAFSK VLRQTKKSPS
NPKDKSTSIR YLKALGIHQT GQKVTDDMYA EQTENPENPL RCPIKLYDFY LFKCPQSVKG
RNDTFYLTPE PVVAPNSPIW YSVQPISREQ MGQMLTRILV IREIQEAIAV ANATTMH
