APH1B_PONAB
ID APH1B_PONAB Reviewed; 257 AA.
AC Q5RDM3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Gamma-secretase subunit APH-1B;
DE Short=APH-1b;
DE AltName: Full=Aph-1beta;
GN Name=APH1B;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral proteins such as Notch receptors and APP (amyloid-beta
CC precursor protein). It probably represents a stabilizing cofactor for
CC the presenilin homodimer that promotes the formation of a stable
CC complex. Probably present in a minority of gamma-secretase complexes
CC compared to APH1A (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Probable component of the gamma-secretase complex, a complex
CC composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN),
CC APH1 (APH1A or APH1B) and PEN2. Such minimal complex is sufficient for
CC secretase activity, although other components may exist. Interacts with
CC PSEN1 and PSEN2 (By similarity). {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; CR857881; CAH90134.1; -; mRNA.
DR RefSeq; NP_001125030.1; NM_001131558.1.
DR AlphaFoldDB; Q5RDM3; -.
DR SMR; Q5RDM3; -.
DR STRING; 9601.ENSPPYP00000007417; -.
DR Ensembl; ENSPPYT00000007721; ENSPPYP00000007417; ENSPPYG00000006539.
DR GeneID; 100171910; -.
DR KEGG; pon:100171910; -.
DR CTD; 83464; -.
DR eggNOG; KOG3972; Eukaryota.
DR GeneTree; ENSGT00390000002049; -.
DR HOGENOM; CLU_086389_0_0_1; -.
DR InParanoid; Q5RDM3; -.
DR OMA; EKKKWYV; -.
DR OrthoDB; 1085102at2759; -.
DR TreeFam; TF314362; -.
DR Proteomes; UP000001595; Chromosome 15.
DR GO; GO:0070765; C:gamma-secretase complex; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030133; C:transport vesicle; IEA:Ensembl.
DR GO; GO:0061133; F:endopeptidase activator activity; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0034205; P:amyloid-beta formation; IEA:Ensembl.
DR GO; GO:0007220; P:Notch receptor processing; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR InterPro; IPR009294; Aph-1.
DR PANTHER; PTHR12889; PTHR12889; 1.
DR Pfam; PF06105; Aph-1; 1.
PE 2: Evidence at transcript level;
KW Membrane; Notch signaling pathway; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..257
FT /note="Gamma-secretase subunit APH-1B"
FT /id="PRO_0000221054"
FT TRANSMEM 5..25
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
SQ SEQUENCE 257 AA; 28519 MW; 911DEA19B41B494B CRC64;
MTAAVFFGCA FIAFGPALAL YVFTIATEPL RIIFLIAGAF FWLVSLLISS LVWFMARVII
DNKDGPTQKY LLIFGTFVSV YIQEMFRFAY YRLLKKASEG LKSINPGETA PSMRLLAYVS
GLGFGIMSGV FSFVNTLSDS LGPGTVGIHG DSPQFFLYSA FMTLVIILLH VFWGIVFFDG
CEKKKWGILL IVLLTHLLVS AQTFISSYYG INLASAFIIL VLMGTWAFLA AGGSCRSLKL
CLLCQDKDFL LYNQRSR