SPR3_CAEEL
ID SPR3_CAEEL Reviewed; 684 AA.
AC Q17768; Q7JP33;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Suppressor of presenilin protein 3;
GN Name=spr-3; ORFNames=C07A12.5;
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 A), FUNCTION, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Probable transcriptional regulator, which participates in the
CC transcriptional repression of the presenilin protein hop-1.
CC {ECO:0000269|PubMed:12668626}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12668626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q17768-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q17768-2; Sequence=VSP_012009;
CC -!- DEVELOPMENTAL STAGE: Expressed in eggs, L2 stage and in adult.
CC Expressed at lower level in L1, L3 and L4 stages.
CC {ECO:0000269|PubMed:12668626}.
CC -!- DISRUPTION PHENOTYPE: Loss of function results in a suppression of sel-
CC 12 mutant phenotypes, possibly by up-regulating hop-1 expression.
CC {ECO:0000269|PubMed:12668626}.
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DR EMBL; FO080373; CCD63278.1; -; Genomic_DNA.
DR EMBL; FO080373; CCD63279.1; -; Genomic_DNA.
DR RefSeq; NP_001024367.1; NM_001029196.3. [Q17768-1]
DR RefSeq; NP_001024368.1; NM_001029197.3.
DR AlphaFoldDB; Q17768; -.
DR BioGRID; 45657; 1.
DR STRING; 6239.C07A12.5a; -.
DR iPTMnet; Q17768; -.
DR EPD; Q17768; -.
DR PaxDb; Q17768; -.
DR PeptideAtlas; Q17768; -.
DR PRIDE; Q17768; -.
DR EnsemblMetazoa; C07A12.5a.1; C07A12.5a.1; WBGene00005008. [Q17768-1]
DR EnsemblMetazoa; C07A12.5b.1; C07A12.5b.1; WBGene00005008.
DR GeneID; 180722; -.
DR KEGG; cel:CELE_C07A12.5; -.
DR UCSC; C07A12.5b; c. elegans. [Q17768-1]
DR CTD; 180722; -.
DR WormBase; C07A12.5a; CE36266; WBGene00005008; spr-3. [Q17768-1]
DR WormBase; C07A12.5b; CE36267; WBGene00005008; spr-3. [Q17768-2]
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00970000196069; -.
DR InParanoid; Q17768; -.
DR OMA; LHRDRHY; -.
DR OrthoDB; 1513393at2759; -.
DR PhylomeDB; Q17768; -.
DR PRO; PR:Q17768; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00005008; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..684
FT /note="Suppressor of presenilin protein 3"
FT /id="PRO_0000046892"
FT ZN_FING 21..43
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 48..71
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 123..145
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 261..283
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 291..313
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 590..612
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 618..641
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 337..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 437..498
FT /note="SKSDTQIALSVKQSSSMKMVKVSPGKVYQLPKTSKFYRPESPDSLASNNSAH
FT GDEIESTSSD -> N (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_012009"
SQ SEQUENCE 684 AA; 79480 MW; B67B377852B88110 CRC64;
MPPRKRKLEE LKNEQGEQGS YKCHLCGQCF YRGCGLASHL RRHAPVTFDC EHCAYTCKHK
YAYDRHLLQS HPELVESGPL VRMFKNEDED APMPILEREA DVSDDAVKYE ALSSFSEPEP
ISYKCPLCIS TFGSHARAVY HILSHRVKLY QAPKSLKFFS RKTMQALGGF RLESQLMIKW
RLQYDNRSVD EKRTRLWRYM EENFGHEHLK QPKLESDNPS TSSSFESQTN LNDSSIIKKK
LVMKCGTVFG QRLIHDNTQY YLCRNCPYVS WNVSSLWRHF RHHIQKSKQS WTCIACSYSS
SSRVKIDLHV KMHKEMPEID LEFATWLRYE RRINKNDLNK PTNKKKKPDG GNGSNHSDMR
SLHAFLSLKN SKNNVVKHDI DAPTLHPLSP APKLVAMTQF DFGEIVTYKS VNPLHQINKN
NSNPTVLPNK RNSIKTSKSD TQIALSVKQS SSMKMVKVSP GKVYQLPKTS KFYRPESPDS
LASNNSAHGD EIESTSSDQF QQSVKVPKYE DFLNMKPVMP YFQKQRHPLE AIAMYEKAKR
EYEKNHCFPN LPIFEFNIEY KNLHPLAKAQ YGKNNMKEYF LNEMEVEKSR ECTDCPFKHN
DLQQFRLHRD KHFYGGSHTC PECNYSSNNH NQVVEHTFVD HYLSDVRLVE GLPSSDSEDD
NIPVPPDTPQ RKKKAPKRGK RRGW
