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Protein

Presenilin hop-1

Gene

hop-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1). Probably works redundantly of lin-12, which provides more presenilin function.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei182 – 1821By similarity
Active sitei278 – 2781By similarity

GO - Molecular functioni

GO - Biological processi

  • embryo development ending in birth or egg hatching Source: WormBase
  • gonad development Source: WormBase
  • nematode larval development Source: WormBase
  • Notch signaling pathway Source: UniProtKB-KW
  • oviposition Source: WormBase
  • positive regulation of cell proliferation Source: WormBase
  • positive regulation of Notch signaling pathway Source: WormBase
  • protein processing Source: InterPro
  • regulation of cell fate specification Source: WormBase
  • regulation of vulval development Source: WormBase
  • reproduction Source: WormBase
Complete GO annotation...

Keywords - Biological processi

Notch signaling pathway

Enzyme and pathway databases

ReactomeiR-CEL-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiO02100.

Protein family/group databases

MEROPSiA22.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Presenilin hop-1
Gene namesi
Name:hop-1
ORF Names:C18E3.8
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiC18E3.8; CE08317; WBGene00001985; hop-1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence analysisAdd
BLAST
Transmembranei13 – 3321HelicalSequence analysisAdd
BLAST
Topological domaini34 – 5724LumenalSequence analysisAdd
BLAST
Transmembranei58 – 7821HelicalSequence analysisAdd
BLAST
Topological domaini79 – 868CytoplasmicSequence analysis
Transmembranei87 – 10721HelicalSequence analysisAdd
BLAST
Topological domaini108 – 1158LumenalSequence analysis
Transmembranei116 – 13621HelicalSequence analysisAdd
BLAST
Topological domaini137 – 14812CytoplasmicSequence analysisAdd
BLAST
Transmembranei149 – 16921HelicalSequence analysisAdd
BLAST
Topological domaini170 – 1701LumenalSequence analysis
Transmembranei171 – 19121HelicalSequence analysisAdd
BLAST
Topological domaini192 – 27382CytoplasmicSequence analysisAdd
BLAST
Transmembranei274 – 29421HelicalSequence analysisAdd
BLAST
Topological domaini295 – 2973LumenalSequence analysis
Transmembranei298 – 31821HelicalSequence analysisAdd
BLAST
Topological domaini319 – 3213CytoplasmicSequence analysis
Intramembranei322 – 34221HelicalSequence analysisAdd
BLAST
Topological domaini343 – 35816CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Presenilin hop-1PRO_0000073902Add
BLAST

Proteomic databases

PaxDbiO02100.

Expressioni

Tissue specificityi

Weakly expressed.

Developmental stagei

Expressed both maternally and zygotically. Predominantly expressed in the adult. Weakly expressed in the embryo, L2 and L3 stages, and almost absent in L1 stage larvae.1 Publication

Inductioni

Down-regulated by spr-1, spr-3, spr-4 and spr-5.

Interactioni

Subunit structurei

Homodimer. Component of the gamma-secretase complex, a complex probably composed of the presenilin homodimer (sel-12, hop-1 or spe-4), nicastrin (aph-2), aph-1 and pen-2 (Probable).Curated

Protein-protein interaction databases

STRINGi6239.C18E3.8.

Structurei

3D structure databases

ProteinModelPortaliO02100.
SMRiO02100. Positions 64-358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi324 – 3263PAL

Domaini

The PAL motif is required for normal active site conformation.By similarity

Sequence similaritiesi

Belongs to the peptidase A22A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2736. Eukaryota.
ENOG410XPZD. LUCA.
GeneTreeiENSGT00390000016593.
InParanoidiO02100.
KOiK06060.
OMAiVALCMIF.
OrthoDBiEOG7HQND4.
PhylomeDBiO02100.

Family and domain databases

InterProiIPR033152. Hop-1.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERiPTHR10202. PTHR10202. 1 hit.
PTHR10202:SF14. PTHR10202:SF14. 1 hit.
PfamiPF01080. Presenilin. 2 hits.
[Graphical view]
PRINTSiPR01072. PRESENILIN.
SMARTiSM00730. PSN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O02100-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRTKRVYSG KTITGVLYPV AICMLFVAIN VKLSQPEQQE QSKVVYGLFH
60 70 80 90 100
SYDTADSGTI TLYLIGFLIL TTSLGVFCYQ MKFYKAIKVY VLANSIGILL
110 120 130 140 150
VYSVFHFQRI AEAQSIPVSV PTFFFLILQF GGLGITCLHW KSHRRLHQFY
160 170 180 190 200
LIMLAGLTAI FILNILPDWT VWMALTAISF WDIVAVLTPC GPLKMLVETA
210 220 230 240 250
NRRGDDKFPA ILYNSSSYVN EVDSPDTTRS NSTPLTEFNN SSSSRLLESD
260 270 280 290 300
SLLRPPVIPR QIREVREVEG TIRLGMGDFV FYSLMLGNTV QTCPLPTVVA
310 320 330 340 350
CFVSNLVGLT ITLPIVTLSQ TALPALPFPL AIAAIFYFSS HIALTPFTDL

CTSQLILI
Length:358
Mass (Da):39,865
Last modified:July 1, 1997 - v1
Checksum:iE811624695DB8E1A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021905 Genomic DNA. Translation: AAB84394.1.
FO080611 Genomic DNA. Translation: CCD65145.1.
PIRiT15184.
RefSeqiNP_491328.1. NM_058927.1.
UniGeneiCel.18540.

Genome annotation databases

EnsemblMetazoaiC18E3.8; C18E3.8; WBGene00001985.
GeneIDi172017.
KEGGicel:CELE_C18E3.8.
UCSCiC18E3.8. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021905 Genomic DNA. Translation: AAB84394.1.
FO080611 Genomic DNA. Translation: CCD65145.1.
PIRiT15184.
RefSeqiNP_491328.1. NM_058927.1.
UniGeneiCel.18540.

3D structure databases

ProteinModelPortaliO02100.
SMRiO02100. Positions 64-358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.C18E3.8.

Protein family/group databases

MEROPSiA22.010.

Proteomic databases

PaxDbiO02100.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC18E3.8; C18E3.8; WBGene00001985.
GeneIDi172017.
KEGGicel:CELE_C18E3.8.
UCSCiC18E3.8. c. elegans.

Organism-specific databases

CTDi172017.
WormBaseiC18E3.8; CE08317; WBGene00001985; hop-1.

Phylogenomic databases

eggNOGiKOG2736. Eukaryota.
ENOG410XPZD. LUCA.
GeneTreeiENSGT00390000016593.
InParanoidiO02100.
KOiK06060.
OMAiVALCMIF.
OrthoDBiEOG7HQND4.
PhylomeDBiO02100.

Enzyme and pathway databases

ReactomeiR-CEL-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiO02100.

Miscellaneous databases

NextBioi873677.
PROiO02100.

Family and domain databases

InterProiIPR033152. Hop-1.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERiPTHR10202. PTHR10202. 1 hit.
PTHR10202:SF14. PTHR10202:SF14. 1 hit.
PfamiPF01080. Presenilin. 2 hits.
[Graphical view]
PRINTSiPR01072. PRESENILIN.
SMARTiSM00730. PSN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signaling."
    Li X., Greenwald I.
    Proc. Natl. Acad. Sci. U.S.A. 94:12204-12209(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Bristol N2.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  3. "Reverse genetic analysis of Caenorhabditis elegans presenilins reveals redundant but unequal roles for sel-12 and hop-1 in Notch-pathway signaling."
    Westlund B., Parry D., Clover R., Basson M., Johnson C.D.
    Proc. Natl. Acad. Sci. U.S.A. 96:2497-2502(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Loss of spr-5 bypasses the requirement for the C.elegans presenilin sel-12 by derepressing hop-1."
    Eimer S., Lakowski B., Donhauser R., Baumeister R.
    EMBO J. 21:5787-5796(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION BY SPR-5.
  5. "Suppressors of the egg-laying defective phenotype of sel-12 presenilin mutants implicate the CoREST corepressor complex in LIN-12/Notch signaling in C. elegans."
    Jarriault S., Greenwald I.
    Genes Dev. 16:2713-2728(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION BY SPR-1.
  6. "Two suppressors of sel-12 encode C2H2 zinc-finger proteins that regulate presenilin transcription in Caenorhabditis elegans."
    Lakowski B., Eimer S., Goebel C., Boettcher A., Wagler B., Baumeister R.
    Development 130:2117-2128(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, DOWN-REGULATION BY SPR-3 AND SPR-4.

Entry informationi

Entry nameiHOP1_CAEEL
AccessioniPrimary (citable) accession number: O02100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 1, 1997
Last modified: May 11, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.