APH1_DICDI
ID APH1_DICDI Reviewed; 328 AA.
AC Q55FS3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Gamma-secretase subunit Aph-1;
GN Name=aph1; ORFNames=DDB_G0267976;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Essential subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral proteins such as Notch receptors precursor protein. It
CC probably represents a stabilizing cofactor for the presenilin homodimer
CC that promotes the formation of a stable complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the gamma-secretase complex, a complex composed
CC of a presenilin homodimer, nicastrin, aph1 and pen2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the APH-1 family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73441.1; -; Genomic_DNA.
DR RefSeq; XP_647460.1; XM_642368.1.
DR AlphaFoldDB; Q55FS3; -.
DR SMR; Q55FS3; -.
DR STRING; 44689.DDB0266683; -.
DR PaxDb; Q55FS3; -.
DR EnsemblProtists; EAL73441; EAL73441; DDB_G0267976.
DR GeneID; 8616267; -.
DR KEGG; ddi:DDB_G0267976; -.
DR dictyBase; DDB_G0267976; aph1.
DR eggNOG; KOG3972; Eukaryota.
DR HOGENOM; CLU_848440_0_0_1; -.
DR InParanoid; Q55FS3; -.
DR OMA; FFNAFDT; -.
DR PhylomeDB; Q55FS3; -.
DR PRO; PR:Q55FS3; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:dictyBase.
DR GO; GO:0070765; C:gamma-secretase complex; IMP:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:dictyBase.
DR GO; GO:0044351; P:macropinocytosis; IMP:dictyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:InterPro.
DR GO; GO:0016485; P:protein processing; IMP:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR InterPro; IPR009294; Aph-1.
DR PANTHER; PTHR12889; PTHR12889; 1.
DR Pfam; PF06105; Aph-1; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Notch signaling pathway; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..328
FT /note="Gamma-secretase subunit Aph-1"
FT /id="PRO_0000331266"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 106..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 328 AA; 37605 MW; 322C29649EED87E5 CRC64;
MTQVLFYGCL FITFSPILAF FFMVIAKNSQ LVILTIGGSF FWLVSILIAA IWWYIIPPMR
EHWWFIISFS VLFQEIFRYI FFRLYSYGFN DRPSLNQIKE TQHQMALDSM RKRKQAQQQK
QQPPTNEIES INNEIIDTTN NNTNNNNNNN NNINDDDNKE ITEEEKEKRK IEKQKQREIE
INARLETLSA RPNHTLSSAA IGVGSGVAYG FIMFGSILWE STGPGTLFSP ACPSVNLFML
SSIITLFMTL LHVVYNVLAF QGYRSKKYHL VAFVIITHFV TTYLTLLNLP TKTTSCVGSI
LPIGIITVFS VGFCIFSLLK SDSITKIH
