ID G3VRN1_SARHA Unreviewed; 528 AA.
AC G3VRN1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Beta-secretase 2 {ECO:0000313|Ensembl:ENSSHAP00000005836.2};
GN Name=BACE2 {ECO:0000313|Ensembl:ENSSHAP00000005836.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000005836.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000005836.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000005836.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; G3VRN1; -.
DR STRING; 9305.ENSSHAP00000005836; -.
DR Ensembl; ENSSHAT00000005890.2; ENSSHAP00000005836.2; ENSSHAG00000005092.2.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000159548; -.
DR HOGENOM; CLU_039009_0_0_1; -.
DR InParanoid; G3VRN1; -.
DR TreeFam; TF329595; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0033162; C:melanosome membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0032438; P:melanosome organization; IEA:Ensembl.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
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:UP000007648};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..528
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029484426"
FT TRANSMEM 478..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..440
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 122
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 315
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT DISULFID 245..444
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT DISULFID 304..468
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT DISULFID 356..404
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
SQ SEQUENCE 528 AA; 58340 MW; 8190E71AF5B6FE9D CRC64;
MCTLGEKQVL VLLQLLFLWT TQALAQAPTP FILPLKVSPI KLNGNLPRPP PVTVSRAAPF
RNDSGGRLRH VDAEGLALAL DPARGLVNFL PMIDNLQGDA GLGYYLEMLI GTPPQKLQIL
VDTGSSNFAV AGVPDPHTTS YFDIEKSYTY QSKNLNINVK YTQGSWTGSV GEDVVTIPKG
FNSTFLVNVA VIFESEDFFL PKTKWNGILG LAYATLAKPS SSLETFFDSL VKQAKISNIF
SIQMCGAGLP RDGTGTNGGS LVMGGIEPSL YKGDIWYTTI KREWYYQIEI LKLEIGGQNL
NLDCREYNVD KAIVDSGTTL LHLPQKVFDA VVKAISQTSL ISEFSEEFWT GSQLACWKYE
TPWSYFPNIS IYFRDENSSK SFRITVLPQL YILPVLGIDS NYECYRFGIS SSANSLVIGA
TVMEGFYVVF DRAQKRIGFA LSSCAKVDGV PVSEISGPFS TDDIASSCIS FSTSNEPILW
IVSYALMTLC GIIFLVLIIL LFPFCSLNCS RDRNLVNDES CLVQHRWK
//
