SPE4_CAEEL
ID SPE4_CAEEL Reviewed; 465 AA.
AC Q01608;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Presenilin spe-4;
GN Name=spe-4 {ECO:0000312|WormBase:ZK524.1};
GN ORFNames=ZK524.1 {ECO:0000312|WormBase:ZK524.1};
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 / MRNA].
RC STRAIN=Bristol N2;
RX PubMed=1527173; DOI=10.1083/jcb.119.1.55;
RA L'Hernault S.W., Arduengo P.M.;
RT "Mutation of a putative sperm membrane protein in Caenorhabditis elegans
RT prevents sperm differentiation but not its associated meiotic divisions.";
RL J. Cell Biol. 119:55-68(1992).
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP SER-177 AND PRO-440.
RX PubMed=9819355; DOI=10.1242/jcs.111.24.3645;
RA Arduengo P.M., Appleberry O.K., Chuang P., L'Hernault S.W.;
RT "The presenilin protein family member SPE-4 localizes to an ER/Golgi
RT derived organelle and is required for proper cytoplasmic partitioning
RT during Caenorhabditis elegans spermatogenesis.";
RL J. Cell Sci. 111:3645-3654(1998).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF HIS-165.
RX PubMed=29879108; DOI=10.1371/journal.pbio.2005069;
RA Zhao Y., Tan C.H., Krauchunas A., Scharf A., Dietrich N., Warnhoff K.,
RA Yuan Z., Druzhinina M., Gu S.G., Miao L., Singson A., Ellis R.E.,
RA Kornfeld K.;
RT "The zinc transporter ZIPT-7.1 regulates sperm activation in nematodes.";
RL PLoS Biol. 16:E2005069-E2005069(2018).
CC -!- FUNCTION: Potential catalytic subunit of the gamma-secretase complex
CC during spermatogenesis, an endoprotease complex that catalyzes the
CC intramembrane cleavage of integral membrane proteins such as Notch
CC receptors (lin-12 or glp-1) (Probable). Involved in spermatid formation
CC during meiosis II (PubMed:9819355, PubMed:29879108). May be required
CC for proper localization of macromolecules that are subject to
CC asymmetric partitioning during spermatogenesis (PubMed:9819355).
CC {ECO:0000269|PubMed:29879108, ECO:0000269|PubMed:9819355, ECO:0000305}.
CC -!- SUBUNIT: Homodimer. Potential component of the gamma-secretase complex,
CC a complex probably composed of the presenilin homodimer (sel-12, hop-1
CC or spe-4), nicastrin (aph-2), aph-1 and pen-2 (Probable).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9819355}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9819355}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000269|PubMed:9819355}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9819355}. Note=Predominantly located in the
CC endoplasmic reticulum and in the cis-Golgi.
CC -!- DEVELOPMENTAL STAGE: Expressed during L4 stage, during spermatogenesis,
CC when hermaphrodites produces sperm.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z14066; CAA78449.1; -; mRNA.
DR EMBL; Z14067; CAA78450.1; -; Genomic_DNA.
DR EMBL; BX284601; CAA98145.1; -; Genomic_DNA.
DR PIR; T27885; T27885.
DR RefSeq; NP_492095.1; NM_059694.5.
DR AlphaFoldDB; Q01608; -.
DR BioGRID; 37940; 8.
DR STRING; 6239.ZK524.1; -.
DR MEROPS; A22.012; -.
DR PaxDb; Q01608; -.
DR PeptideAtlas; Q01608; -.
DR EnsemblMetazoa; ZK524.1.1; ZK524.1.1; WBGene00004958.
DR GeneID; 172498; -.
DR KEGG; cel:CELE_ZK524.1; -.
DR UCSC; ZK524.1; c. elegans.
DR CTD; 172498; -.
DR WormBase; ZK524.1; CE06618; WBGene00004958; spe-4.
DR eggNOG; KOG2736; Eukaryota.
DR HOGENOM; CLU_022975_0_0_1; -.
DR InParanoid; Q01608; -.
DR OMA; CGTFCYF; -.
DR OrthoDB; 797738at2759; -.
DR PhylomeDB; Q01608; -.
DR Reactome; R-CEL-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q01608; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004958; Expressed in larva and 1 other tissue.
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:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:WormBase.
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:0004190; F:aspartic-type endopeptidase activity; 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:0061024; P:membrane organization; IMP: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:0007220; P:Notch receptor processing; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006996; P:organelle organization; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR GO; GO:0007286; P:spermatid development; IMP:WormBase.
DR GO; GO:0048515; P:spermatid differentiation; IMP:UniProtKB.
DR Gene3D; 1.10.472.100; -; 1.
DR InterPro; IPR001108; Peptidase_A22A.
DR InterPro; IPR006639; Preselin/SPP.
DR InterPro; IPR042524; Presenilin_C.
DR InterPro; IPR033153; SPE-4.
DR PANTHER; PTHR10202; PTHR10202; 1.
DR PANTHER; PTHR10202:SF25; PTHR10202:SF25; 1.
DR Pfam; PF01080; Presenilin; 1.
DR SMART; SM00730; PSN; 1.
PE 1: Evidence at protein level;
KW Differentiation; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Notch signaling pathway; Reference proteome; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..465
FT /note="Presenilin spe-4"
FT /id="PRO_0000073904"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..71
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..136
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..190
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 287..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 440..442
FT /note="PAL"
FT COMPBIAS 305..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /evidence="ECO:0000250"
FT ACT_SITE 394
FT /evidence="ECO:0000250"
FT MUTAGEN 165
FT /note="H->Y: In hc196; failed spermatocyte division in a
FT zipt-7.1 mutant (ok971) background."
FT /evidence="ECO:0000269|PubMed:29879108"
FT MUTAGEN 177
FT /note="S->F: In HC78; induces an aberrant localization of
FT tubulin in spermatids."
FT /evidence="ECO:0000269|PubMed:9819355"
FT MUTAGEN 440
FT /note="P->L: In HC78; induces an aberrant localization of
FT tubulin in spermatids."
FT /evidence="ECO:0000269|PubMed:9819355"
SQ SEQUENCE 465 AA; 51830 MW; 65BE2A4DFDF3C844 CRC64;
MDTLRSISSE LVRSSQLRWT LFSVIANMSL TLSIWIGVYN MEVNSELSKT YFLDPSFEQT
TGNLLLDGFI NGVGTILVLG CVSFIMLAFV LFDFRRIVKA WLTLSCLLIL FGVSAQTLHD
MFSQVFDQDD NNQYYMTIVL IVVPTVVYGF GGIYAFFSNS SLILHQIFVV TNCSLISVFY
LRVFPSKTTW FVLWIVLFWD LFAVLAPMGP LKKVQEKASD YSKCVLNLIM FSANEKRLTA
GSNQEETNEG EESTIRRTVK QTIEYYTKRE AQDDEFYQKI RQRRAAINPD SVPTEHSPLV
EAEPSPIELK EKNSTEELSD DESDTSETSS GSSNLSSSDS STTVSTSDIS TAEECDQKEW
DDLVSNSLPN NDKRPATAAD ALNDGEVLRL GFGDFVFYSL LIGQAAASGC PFAVISAALG
ILFGLVVTLT VFSTEESTTP ALPLPVICGT FCYFSSMFFW EQLYG
