ID   A0A2Y9SI99_PHYMC        Unreviewed;       514 AA.
AC   A0A2Y9SI99;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   11-DEC-2019, entry version 10.
DE   SubName: Full=beta-secretase 2 {ECO:0000313|RefSeq:XP_023976050.1};
GN   Name=BACE2 {ECO:0000313|RefSeq:XP_023976050.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023976050.1};
RN   [1] {ECO:0000313|RefSeq:XP_023976050.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023976050.1};
RG   RefSeq;
RL   Submitted (APR-2019) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS01079896}.
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DR   RefSeq; XP_023976050.1; XM_024120282.1.
DR   KEGG; pcad:102989241; -.
DR   KO; K07747; -.
DR   Proteomes; UP000248484; Genome assembly.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd05473; beta_secretase_like; 1.
DR   Gene3D; 2.40.70.10; -; 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; PTHR13683; PTHR13683; 1.
DR   PANTHER; PTHR13683:SF262; PTHR13683:SF262; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR01817; BACE2.
DR   PRINTS; PR01815; BACEFAMILY.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 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|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..514
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015981666"
FT   TRANSMEM        463..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..425
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   514 AA;  55686 MW;  213023DDF1EA3757 CRC64;
     MGALARALLL PLLAQWLLRA APAPAPAPFT LPLRVASASS RGAAPSPGPG PPAEPRADGL
     ALALEPAAGA ANFLAMVDNL QGDSGRGYYL EMLIGTPPQK LQILVDTGSS NFAVAGAPHP
     YVDSYFDTER SSTYRPKGFD VTVKYTQGSW TGFVGEDVVT IPKGFNSSFL VNIATIFESE
     NFFLPGIKWN GILGLAYATL AKPSSSLETF FDSLVAQARI PDVFSMQMCG AGLPVAGSGT
     NGGSLVLGGI EPTLYKGDIW YTPIKEEWYY QIEILKLEIG GQNLNLDCRE YNADKAIVDS
     GTTLLRLPQK VFDAVVEAVA RTSLIPEFSD GFWTGSQLAC WTNSETPWSY FPKISIYLRD
     ENSSRSFRIT ILPQLYIQPM MGAGLNYECY RFGISPSTNA LVIGATVMEG FYVVFDRARK
     RVGFAASPCA EIAGAPVSEI SGPFSTEDIA SNCVPALPLN EPILWIVSYT LMSVCGIILL
     ILIILLLLPF RCRHLPPDPE VVNDESSLVR HRWK
//