QRIC1_BOVIN
ID QRIC1_BOVIN Reviewed; 779 AA.
AC Q0P5J0; A5D7N1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Transcriptional regulator QRICH1 {ECO:0000305};
DE AltName: Full=Glutamine-rich protein 1;
GN Name=QRICH1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex, and Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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. Controls the outcome
CC of the unfolded protein response (UPR), an ER-stress response pathway
CC that either promotes recovery of ER homeostasis and cell survival, or
CC triggers the terminal UPR which elicits programmed cell death when ER
CC stress is prolonged and unresolved. ER stress induces QRICH1
CC translation by a ribosome translation re-initiation mechanism in
CC response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced
CC QRICH1 regulates a transcriptional program associated with protein
CC translation, protein secretion-mediated proteotoxicity and cell death
CC during the terminal UPR. May cooperate with ATF4 transcription factor
CC signaling to regulate ER homeostasis which is critical for cell
CC viability. Up-regulates CASP3/caspase-3 activity in epithelial cells
CC under ER stress. Central regulator of proteotoxicity associated with ER
CC stress-mediated inflammatory diseases in the intestines and liver.
CC Involved in chondrocyte hypertrophy, a process required for normal
CC longitudinal bone growth. {ECO:0000250|UniProtKB:Q2TAL8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2TAL8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q2TAL8}. Cell membrane
CC {ECO:0000250|UniProtKB:Q2TAL8}.
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; BC119972; AAI19973.1; -; mRNA.
DR EMBL; BC140621; AAI40622.1; -; mRNA.
DR RefSeq; NP_001091484.1; NM_001098015.2.
DR RefSeq; XP_005222840.1; XM_005222783.3.
DR RefSeq; XP_015315045.1; XM_015459559.1.
DR AlphaFoldDB; Q0P5J0; -.
DR SMR; Q0P5J0; -.
DR STRING; 9913.ENSBTAP00000025183; -.
DR PaxDb; Q0P5J0; -.
DR PRIDE; Q0P5J0; -.
DR Ensembl; ENSBTAT00000025183; ENSBTAP00000025183; ENSBTAG00000018924.
DR GeneID; 511970; -.
DR KEGG; bta:511970; -.
DR CTD; 54870; -.
DR VEuPathDB; HostDB:ENSBTAG00000018924; -.
DR VGNC; VGNC:33602; QRICH1.
DR eggNOG; ENOG502QU8W; Eukaryota.
DR GeneTree; ENSGT00940000155241; -.
DR HOGENOM; CLU_025446_0_0_1; -.
DR InParanoid; Q0P5J0; -.
DR OMA; DKMVGTT; -.
DR OrthoDB; 587724at2759; -.
DR TreeFam; TF336988; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000018924; Expressed in mesenteric lymph node and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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: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; ISS:UniProtKB.
DR InterPro; IPR021893; DUF3504.
DR Pfam; PF12012; DUF3504; 1.
PE 2: Evidence at transcript 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..779
FT /note="Transcriptional regulator QRICH1"
FT /id="PRO_0000269852"
FT DOMAIN 6..48
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 141..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..443
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 467
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 779 AA; 86752 MW; 033E0C748A3ECF50 CRC64;
MNNSLENTIS FEEYIRVKAR SVPQHRMKEF LDSLASKGPE ALQEFQQTAT TTMVYQQGGN
CIYTDSTEVA GSLLELACPV TTSVQPQTQP EQQIQVQQPQ QVQVQVQVQQ SPQQVSAQQL
SPQLTVHQPA EQPIHVQVQI QGQAAQPAAP SIQTPSLQSP SPSQLQAAQI QVQHMQAAQQ
IQAPEIPEEH IPHQQIQAQL VAGQSLAGGQ QIQIQTVGAL SPPPSQQGSP REGERRVGTA
SVLQPVKKRK VDMPITVSYA ISGQPVATVL AIPQGQQQSY VSLRPDLLTV DSAHLYSATG
TITSPTGETW TIPVYSAQPR GDPQQQSITH IAIPQEAYNA VHVSGSPTAL AAVKLEDDKE
KMVGTTSVVK NSHEEVVQTL ANSLFPAQFM NGNIHIPVAV QAVAGTYQNT AQTVHIWDPQ
QQPQQQTPQE QTPPPPQQQQ QQQLQVTCSA QTVQVAEVEP QSQPQPSPEL LLPNSLKPEE
GLEVWKNWAQ TKNAELEKDA QNRLAPIGRR QLLRFQEDLI SSAVAELNYG LCLMTREARN
GEGEPYDPDV LYYIFLCIQK YLFENGRVDD IFSDLYYVRF TEWLHEVLKD VQPRVTPLGY
VLPSHVTEEM LWECKQLGAH SPSTLLTTLM FFNTKYFLLK TVDQHMKLAF SKVLRQTKKN
PSNPKDKSTS IRYLKALGIH QTGQKVTDDM YAEQTENPEN PLRCPIKLYD FYLFKCPQSV
KGRNDTFYLT PEPVVAPNSP IWYSVQPISR EQMGQMLTRI LVIREIQEAI AVASASTMH
