ID A0A093QXX4_PHACA Unreviewed; 384 AA.
AC A0A093QXX4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Beta-secretase 2 {ECO:0000313|EMBL:KFW93728.1};
DE Flags: Fragment;
GN ORFNames=N336_01631 {ECO:0000313|EMBL:KFW93728.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW93728.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW93728.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW93728.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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; KL439181; KFW93728.1; -; Genomic_DNA.
DR RefSeq; XP_009508004.1; XM_009509709.1.
DR AlphaFoldDB; A0A093QXX4; -.
DR GeneID; 104049091; -.
DR KEGG; pcao:104049091; -.
DR CTD; 25825; -.
DR OrthoDB; 603414at2759; -.
DR Proteomes; UP000053238; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR009119; BACE.
DR InterPro; IPR009120; BACE1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR PANTHER; PTHR47965:SF40; BETA-SECRETASE 2; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR01816; BACE1.
DR PRINTS; PR01815; BACEFAMILY.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000053238};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 333..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..295
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW93728.1"
FT NON_TER 384
FT /evidence="ECO:0000313|EMBL:KFW93728.1"
SQ SEQUENCE 384 AA; 42288 MW; 33CE17EDBE30078D CRC64;
SSTYKSQGID VTVKYSQGSW AGVLGTDVIT IPKGIYGSYT VNIATILESE NFFLPGVKWH
GILGLAYDAL AKPSSSVETF FDSLVRQAKI PNIFSLQMCG AGLPVSGSGT NGGSLVLGGI
EPSLYKGDIW YTPIKEEWYY QVEILKLEVG GQNLELDCRE YNADKAIVDS GTTLLRLPQK
VFSAVVQAIA RTSLIQEFSS GFWTGSQLAC WDKTERPWSL FPKLSIYLRD ENSSRSFRIS
ILPQLYIQPI LGIGENLQCY RFGISSSMNA LVIGATVMEG FYVIFDRAQR RVGFAVSPCA
EVDGSPVSEI EGPFTTADVA SNCVSSVSFH EPVLWIASYA LMSLCGIILL VLIILLLIPP
RCQHRYTDND VVNDESSLVR HRWK
//