ID HOP1_CAEEL Reviewed; 358 AA.
AC O02100;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=Presenilin hop-1;
GN Name=hop-1; ORFNames=C18E3.8;
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].
RC STRAIN=Bristol N2;
RX PubMed=9342387; DOI=10.1073/pnas.94.22.12204;
RA Li X., Greenwald I.;
RT "HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally
RT redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1
RT signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12204-12209(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
RX PubMed=10051671; DOI=10.1073/pnas.96.5.2497;
RA Westlund B., Parry D., Clover R., Basson M., Johnson C.D.;
RT "Reverse genetic analysis of Caenorhabditis elegans presenilins reveals
RT redundant but unequal roles for sel-12 and hop-1 in Notch-pathway
RT signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2497-2502(1999).
RN [4]
RP DOWN-REGULATION BY SPR-5.
RX PubMed=12411496; DOI=10.1093/emboj/cdf561;
RA Eimer S., Lakowski B., Donhauser R., Baumeister R.;
RT "Loss of spr-5 bypasses the requirement for the C.elegans presenilin sel-12
RT by derepressing hop-1.";
RL EMBO J. 21:5787-5796(2002).
RN [5]
RP DOWN-REGULATION BY SPR-1.
RX PubMed=12381669; DOI=10.1101/gad.1022402;
RA Jarriault S., Greenwald I.;
RT "Suppressors of the egg-laying defective phenotype of sel-12 presenilin
RT mutants implicate the CoREST corepressor complex in LIN-12/Notch signaling
RT in C. elegans.";
RL Genes Dev. 16:2713-2728(2002).
RN [6]
RP DEVELOPMENTAL STAGE, AND DOWN-REGULATION BY SPR-3 AND SPR-4.
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).
CC -!- FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral membrane proteins such as Notch receptors (lin-12 or glp-1).
CC Probably works redundantly of lin-12, which provides more presenilin
CC function. {ECO:0000269|PubMed:10051671}.
CC -!- SUBUNIT: Homodimer. Component of the gamma-secretase complex, a complex
CC probably composed of the presenilin homodimer (sel-12, hop-1 or spe-4),
CC nicastrin (aph-2), aph-1 and pen-2 (Probable). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Weakly expressed.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Predominantly expressed in the adult. Weakly expressed in the embryo,
CC L2 and L3 stages, and almost absent in L1 stage larvae.
CC {ECO:0000269|PubMed:12668626}.
CC -!- INDUCTION: Down-regulated by spr-1, spr-3, spr-4 and spr-5.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
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DR EMBL; AF021905; AAB84394.1; -; Genomic_DNA.
DR EMBL; FO080611; CCD65145.1; -; Genomic_DNA.
DR PIR; T15184; T15184.
DR RefSeq; NP_491328.1; NM_058927.1.
DR AlphaFoldDB; O02100; -.
DR SMR; O02100; -.
DR STRING; 6239.C18E3.8.1; -.
DR MEROPS; A22.010; -.
DR EPD; O02100; -.
DR PaxDb; 6239-C18E3-8; -.
DR EnsemblMetazoa; C18E3.8.1; C18E3.8.1; WBGene00001985.
DR GeneID; 172017; -.
DR KEGG; cel:CELE_C18E3.8; -.
DR UCSC; C18E3.8; c. elegans.
DR AGR; WB:WBGene00001985; -.
DR WormBase; C18E3.8; CE08317; WBGene00001985; hop-1.
DR eggNOG; KOG2736; Eukaryota.
DR HOGENOM; CLU_022975_3_0_1; -.
DR InParanoid; O02100; -.
DR OMA; ALCMIFV; -.
DR OrthoDB; 2881575at2759; -.
DR PhylomeDB; O02100; -.
DR Reactome; R-CEL-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-CEL-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR SignaLink; O02100; -.
DR PRO; PR:O02100; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001985; Expressed in germ line (C elegans) and 3 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
DR GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IBA:GO_Central.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR GO; GO:0018991; P:egg-laying behavior; IGI:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0008406; P:gonad development; IGI:WormBase.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0007220; P:Notch receptor processing; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:WormBase.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IGI:WormBase.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR GO; GO:0042659; P:regulation of cell fate specification; IGI:WormBase.
DR GO; GO:0040028; P:regulation of vulval development; IGI:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR Gene3D; 1.10.472.100; Presenilin; 1.
DR InterPro; IPR001108; Peptidase_A22A.
DR InterPro; IPR006639; Preselin/SPP.
DR InterPro; IPR042524; Presenilin_C.
DR PANTHER; PTHR10202; PRESENILIN; 1.
DR PANTHER; PTHR10202:SF14; PRESENILIN HOP-1; 1.
DR Pfam; PF01080; Presenilin; 2.
DR PRINTS; PR01072; PRESENILIN.
DR SMART; SM00730; PSN; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Notch signaling pathway;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..358
FT /note="Presenilin hop-1"
FT /id="PRO_0000073902"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..57
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..115
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..297
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 324..326
FT /note="PAL"
FT ACT_SITE 182
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 39865 MW; E811624695DB8E1A CRC64;
MPRTKRVYSG KTITGVLYPV AICMLFVAIN VKLSQPEQQE QSKVVYGLFH SYDTADSGTI
TLYLIGFLIL TTSLGVFCYQ MKFYKAIKVY VLANSIGILL VYSVFHFQRI AEAQSIPVSV
PTFFFLILQF GGLGITCLHW KSHRRLHQFY LIMLAGLTAI FILNILPDWT VWMALTAISF
WDIVAVLTPC GPLKMLVETA NRRGDDKFPA ILYNSSSYVN EVDSPDTTRS NSTPLTEFNN
SSSSRLLESD SLLRPPVIPR QIREVREVEG TIRLGMGDFV FYSLMLGNTV QTCPLPTVVA
CFVSNLVGLT ITLPIVTLSQ TALPALPFPL AIAAIFYFSS HIALTPFTDL CTSQLILI
//
