SPR4_CAEEL
ID SPR4_CAEEL Reviewed; 1311 AA.
AC O17582;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Suppressor of presenilin protein 4;
GN Name=spr-4; ORFNames=C09H6.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), AND FUNCTION.
RX PubMed=12668626; DOI=10.1242/dev.00429;
RA Lakowski B., Eimer S., Goebel C., Boettcher A., Wagler B., Baumeister R.;
RT "Two suppressors of sel-12 encode C2H2 zinc-finger proteins that regulate
RT presenilin transcription in Caenorhabditis elegans.";
RL Development 130:2117-2128(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY OXIDATIVE STRESS, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 683-TRP--VAL-1311.
RX PubMed=24670762; DOI=10.1038/nature13163;
RA Lu T., Aron L., Zullo J., Pan Y., Kim H., Chen Y., Yang T.H., Kim H.M.,
RA Drake D., Liu X.S., Bennett D.A., Colaiacovo M.P., Yankner B.A.;
RT "REST and stress resistance in ageing and Alzheimer's disease.";
RL Nature 507:448-454(2014).
CC -!- FUNCTION: Probable transcriptional regulator, which participates in the
CC transcriptional repression of the presenilin protein hop-1
CC (PubMed:12668626, PubMed:24670762). Might play a role in the oxidative
CC stress response (PubMed:24670762). {ECO:0000269|PubMed:12668626,
CC ECO:0000269|PubMed:24670762}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O17582-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O17582-2; Sequence=VSP_008060;
CC -!- TISSUE SPECIFICITY: Expressed in neurons.
CC {ECO:0000269|PubMed:24670762}.
CC -!- INDUCTION: Up-regulated by oxidative stress.
CC {ECO:0000269|PubMed:24670762}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC survival upon paraquat treatment to induce oxidative stress.
CC {ECO:0000269|PubMed:24670762}.
CC -!- MISCELLANEOUS: Loss of function results in a suppression of sel-12
CC phenotypes, possibly by up-regulating hop-1 expression.
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DR EMBL; Z81466; CAB03868.2; -; Genomic_DNA.
DR EMBL; Z81466; CAE45043.1; -; Genomic_DNA.
DR PIR; T19170; T19170.
DR RefSeq; NP_001020993.1; NM_001025822.2. [O17582-1]
DR RefSeq; NP_001020994.1; NM_001025823.3. [O17582-2]
DR AlphaFoldDB; O17582; -.
DR BioGRID; 38030; 1.
DR STRING; 6239.C09H6.1a; -.
DR EPD; O17582; -.
DR PaxDb; O17582; -.
DR PeptideAtlas; O17582; -.
DR PRIDE; O17582; -.
DR EnsemblMetazoa; C09H6.1a.1; C09H6.1a.1; WBGene00005009. [O17582-1]
DR EnsemblMetazoa; C09H6.1b.1; C09H6.1b.1; WBGene00005009. [O17582-2]
DR GeneID; 172596; -.
DR KEGG; cel:CELE_C09H6.1; -.
DR UCSC; C09H6.1b; c. elegans. [O17582-1]
DR CTD; 172596; -.
DR WormBase; C09H6.1a; CE30487; WBGene00005009; spr-4. [O17582-1]
DR WormBase; C09H6.1b; CE15609; WBGene00005009; spr-4. [O17582-2]
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156658; -.
DR InParanoid; O17582; -.
DR OMA; HIRLHFT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O17582; -.
DR SignaLink; O17582; -.
DR PRO; PR:O17582; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00005009; Expressed in embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 18.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1311
FT /note="Suppressor of presenilin protein 4"
FT /id="PRO_0000046893"
FT ZN_FING 112..134
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 141..163
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..349
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..379
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 451..476
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..510
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 585..607
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 613..635
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 709..731
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 737..759
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 794..816
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 823..845
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1022..1044
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1053..1075
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1104..1126
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1162..1184
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1190..1212
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1261..1284
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..910
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1241..1242
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_008060"
FT MUTAGEN 683..1311
FT /note="Missing: In by105; increased expression of
FT presenilin hop-1. Increased ROS levels and reduced survival
FT upon paraquat treatment to induce oxidative stress."
FT /evidence="ECO:0000269|PubMed:24670762"
SQ SEQUENCE 1311 AA; 150189 MW; A1C50E209FD98854 CRC64;
MSSEPTSSIE SDNLRRSKRK KFKLDFVAAA HGNNQKKSRK DPHGQGDDDD DTFDDDLNHF
EPLSVLTEQD VSMEMFEDDE EDTVSRRRTR RSTAHFQDYQ EPDRWIENSG PHACHKCPSR
YESKSSLANH TKMHLGEKRK FACELCDFSA STLKSLTHHN NIHQNFGVLS QQTSPVIPVA
SSADSTLNSS INSTGCQINA PPAPKLDEEA PIAVESVVVH HEDVAEFDTT PPPILEREDD
GPPVLIREAP VRKSNRPMKP TQKAQKMTKQ RERKSKTVES PKGSLPSSSA SSVTPPPVRK
DVEKPKIFVK TTKKNLKKTM KITKVRQRCP HCPFTTSTVT RLNRHSGGHK LKEGYICPSE
NCNFMCRKAG FLQKHYILHK GTLPWPPEYV KKGGAKMKRT FPESEEKKIE VTEKVQKMKK
MHKRRANTVQ VVAKAQLKSY IKVEVDDVIF KKCNIGECEF LTQTLTQLIV HKVKTHDTKT
AFPQHRFLCL TCGHRAKSYA ALRTHKLIEH TSTHKRFHRT YYLKECVGDK FFVKYNLSKV
QEEVKEEPKE ADGDESGDES FDSMCPASDV HPETLAAIEM KDVFFCCNMC PYKAPTMNRC
QRHYDKHFKN DEFKCQYCSW SSRSKEVIVN HEKLHPTVVV ANTNEAPVVK NEIEAKVEVL
SKTVSSPVEC TEESSLSKSI QLWCQREKLR HPELDEQFTR KMIDGVKGFQ CTDCPYTSKY
RGDMRSHKKR HDIEQLYRCV QCTYTTNRPV SLKDHLKQHA IVNMSIADIK SRRVVVNQGV
KIGMRRGVGK DKIYCCDKCP YVTLALGCLW RHHRNHRDTA KINICSNCSY SSIDQRKMEE
HTIIHLGLGL NEAVPFVKRV DQKGRPVSSL TDLNSEKMNE RKSTKRKMLD KVEKMEVGED
EEDDEESVDK GTDDGDYKQR PEKKRKQSSE EPASDPELFG SSSQPTRQLS ERATRNRINY
SLLSKNGSGK PTPSTSSANL EKLAGSSGGA SSESPEPDES VEVSHWKIRT FLRSEYGVKE
SLKCPDCPYK SSEPDVLEKH RYYHMTKTTP RPYACSDCTF NTYTPTALLQ HLKLHSEGVY
FDPMVKKHMK HRKGDSIPPG VKGYYCKNCS FKTSIHRNFI EHSAYHRQQL INRINITLKR
QPPRIEYQRP KLKHQFVAKN AKYCKKCTFK CVSQSNFIEH LDRHGWNQLY KCYSCDYSDN
TKSVVDFHQL NHHIVKDQTL HSICQSAKFR LENGVIQIPE FQTEKSKPTP DEFVSKTRGL
LKCPSCEYFC HVSSELAFHM SVHHLTEPNA RETISYLHMG LVPPKATVTT V
