ID A0A315VZP0_GAMAF Unreviewed; 739 AA.
AC A0A315VZP0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 02-APR-2025, entry version 24.
DE RecName: Full=Gamma-secretase subunit APH-1 {ECO:0000256|RuleBase:RU369072};
DE Short=APH-1 {ECO:0000256|RuleBase:RU369072};
GN ORFNames=CCH79_00006314 {ECO:0000313|EMBL:PWA29092.1};
OS Gambusia affinis (Western mosquitofish) (Heterandria affinis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Gambusia.
OX NCBI_TaxID=33528 {ECO:0000313|EMBL:PWA29092.1, ECO:0000313|Proteomes:UP000250572};
RN [1] {ECO:0000313|EMBL:PWA29092.1, ECO:0000313|Proteomes:UP000250572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE01/NJP1002.9 {ECO:0000313|EMBL:PWA29092.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PWA29092.1};
RX PubMed=29703783;
RA Hoffberg S.L., Troendle N.J., Glenn T.C., Mahmud O., Louha S., Chalopin D.,
RA Bennetzen J.L., Mauricio R.;
RT "A High-Quality Reference Genome for the Invasive Mosquitofish Gambusia
RT affinis Using a Chicago Library.";
RL G3 (Bethesda) 8:1855-1861(2018).
CC -!- FUNCTION: Potential subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral proteins such as Notch receptors.
CC {ECO:0000256|RuleBase:RU369072}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Component of the gamma-secretase complex.
CC {ECO:0000256|RuleBase:RU369072}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU369072}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU369072}.
CC -!- SIMILARITY: Belongs to the APH-1 family.
CC {ECO:0000256|ARBA:ARBA00005577, ECO:0000256|RuleBase:RU369072}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU369072}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWA29092.1}.
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DR EMBL; NHOQ01000682; PWA29092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A315VZP0; -.
DR STRING; 33528.ENSGAFP00000021510; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000250572; Unassembled WGS sequence.
DR GO; GO:0070765; C:gamma-secretase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.5.350; -; 1.
DR Gene3D; 6.10.250.180; -; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR009294; Aph-1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR022252; SOCS4/SOCS5_dom.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR038077; Troponin_sf.
DR PANTHER; PTHR12889; GAMMA-SECRETASE SUBUNIT APH-1; 1.
DR Pfam; PF06105; Aph-1; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF12610; SOCS; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR Pfam; PF00992; Troponin; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF158235; SOCS box-like; 1.
DR SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369072};
KW Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976,
KW ECO:0000256|RuleBase:RU369072};
KW Reference proteome {ECO:0000313|Proteomes:UP000250572};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU369072};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU369072};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369072"
FT TRANSMEM 32..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369072"
FT TRANSMEM 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369072"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369072"
FT DOMAIN 581..676
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 671..720
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 309..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..217
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 309..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..384
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 83473 MW; 3062DEC2751DD22D CRC64;
MTAAVFFGCT FIAFGPAVSL FLFTIAREPL RVIFLIAGAF FWLVSLLLAS LVWFISVQIS
NKESASQQKG LLIFGVVLSV LLQETFRFAY YKLLKKANEG LLALSQEETM PISIRQLAYV
SGLGFGFMSG AFSVVNILAD SVGPGTVGIH GDSQHYFLSS EASGLYLGRV CRIKRVLGEG
SDQEQPKDRS LLLQIGKEML EEEARQAEEE KMAYIRENCP TLSFPQCTLE LQELCRQLHK
QIDLVDEERY DMEIKIDDLK MKVQDLNGRF KKPTLRRVRM SADAMLAALL GSKHKVSLDL
RANLKQVKKE LKDEEKQTGD WRKNIEDKAG MDGREQTAGM SEKKPRGADT RPKSGIRSWS
ADSYIWRGKK RSRSSRNGSS PGGSEADCSE ELSMRSTSCS RRRRERKCSC SALGDSLMAG
DVDGVCRKAL HRRSLRQKFQ DAVGQCLPLR HHHHHHYHHP PGSSRPFSIL FWSKRKIHVS
ELMQDKCPFS PKSELAKCWH LIKKQVADPG SLKDMETPLK PRVSSSTSPP QTPLSWEDIC
CSPAPLEDWD PSCLHGRPDG ACGNTDYILV PDLLQINNNP CYWGVLNRFE AEELLEGQPE
GTFLLRDSAQ DEFLFSVSFR RYSRSLHARI EQNGKRFSFD VRDPCMYRDA SVTGLLRHYS
DPATCLFFEP LLSRPLPRTF PFPLQHLCRA VICSCITYQG VEELPLPSQL REYLRQYHIK
CDGACAVSMP TAANTQDLH
//