ID A0A093ET83_TYTAL Unreviewed; 415 AA.
AC A0A093ET83;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Beta-secretase 2 {ECO:0000313|EMBL:KFV43818.1};
DE Flags: Fragment;
GN ORFNames=N341_11597 {ECO:0000313|EMBL:KFV43818.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV43818.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV43818.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV43818.1};
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; KK371621; KFV43818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093ET83; -.
DR MEROPS; A01.041; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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 CDD; cd05473; beta_secretase_like; 1.
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; IPR009121; BACE2.
DR InterPro; IPR033874; Memapsin-like.
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; PR01817; BACE2.
DR PRINTS; PR01815; BACEFAMILY.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR609121-2};
KW Glycoprotein {ECO:0000256|PIRSR:PIRSR609121-3};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 364..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..326
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 7
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-1"
FT ACT_SITE 200
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-1"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT DISULFID 130..330
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT DISULFID 189..354
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT DISULFID 241..290
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV43818.1"
FT NON_TER 415
FT /evidence="ECO:0000313|EMBL:KFV43818.1"
SQ SEQUENCE 415 AA; 45476 MW; ED3DB2162FA048F0 CRC64;
QLNILVDTGS SNFAVAGVPD PDVTSYFNTA LSSTYKSEGI DVTVKYSQGS WTGVLGTDVI
TIPKGIYGSY TINIATILES ENFFLPGVKW HGILGLAYDA LAKPSSSVET FFDSLVRQAK
IPNIFSLQMC GAGLPVSGSG TNGGSLVLGG IEPSLYRGDI WYTPIKEEWY YQVEILKLEV
GGHSLELDCR EYNADKAIVD SGTTLLRLPQ KVFSAVVEAI ARTSLIQEFS SGFWTGSQLA
CWDKTERPWS LFPKISIYLR DENSSRSFRI SVLPQLYIQP ILGIGENLQC YRFGISSSTN
ALVIGATVME GFYVIFDRAQ RRVGFAVSPC AEVDGSPVSE IEGPFTTADV ASNCVSSVSF
HEPVLWIASY ALMSLCGIIL LVLIILLLIP PRCQHRYSDN DVVNDESSLV HHRWK
//
