ID I3MHS5_ICTTR Unreviewed; 488 AA.
AC I3MHS5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Beta-secretase 2 {ECO:0000313|Ensembl:ENSSTOP00000010470.3};
GN Name=BACE2 {ECO:0000313|Ensembl:ENSSTOP00000010470.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000010470.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000010470.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {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; AGTP01030049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01030050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01030051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MHS5; -.
DR STRING; 43179.ENSSTOP00000010470; -.
DR Ensembl; ENSSTOT00000011667.3; ENSSTOP00000010470.3; ENSSTOG00000011669.3.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000159548; -.
DR HOGENOM; CLU_039009_0_0_1; -.
DR InParanoid; I3MHS5; -.
DR TreeFam; TF329595; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
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; 1.
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:UP000005215};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 437..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 273
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT DISULFID 203..403
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT DISULFID 262..427
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT DISULFID 314..363
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
SQ SEQUENCE 488 AA; 53101 MW; 23CC2B13990E9BB7 CRC64;
APFTLPLQVA SATRHPASPA PEPVTSALAR ANGLALALEP AGVNANFLAM VDNLQGDSGR
GYYLEMLIGT PPQKLQILVD TGSSNFAVAG APHSYVDTYF DAERSSTYRF KGFEVTVKYT
QGSWTGFVGE DVVTIPKGFN SSFLVNIATI FKSENFFLPG IKWNGILGLA YATLAKPSSS
LKTFFDSLVT QAKIPNVFSM QMCGAGLPIA GSGTNGGSLV LGGIEPSLYT GDIWYTPIKE
EWYYQIEILK LEIGGQSLNL DCKEYNADKA IVDSGTTLLR LPQKVFDAVV EAVARTSMIP
EFSDGFWSGA QLACWANSET PWSYFPKISI YLREENSSRS FRITILPQLY IQPMMGAGLN
YECYRFGISS STNALVIGAT VMEGFYVVFD RAHKRVGFAA SPCAEMAGAP VSEIAGPFST
EDIASNCVPA QALNDPILWI VSYTLMSVCG VILLILILLL LIPFQCRHTP RDPEVVNDES
SLVRHRWK
//
