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Database: UniProt
Entry: A0A093QXX4_PHACA
LinkDB: A0A093QXX4_PHACA
Original site: A0A093QXX4_PHACA 
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}.
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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
//
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