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Database: UniProt
Entry: G1U1R2_RABIT
LinkDB: G1U1R2_RABIT
Original site: G1U1R2_RABIT 
ID   G1U1R2_RABIT            Unreviewed;       340 AA.
AC   G1U1R2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Beta-secretase 2 {ECO:0000313|Ensembl:ENSOCUP00000023300.3};
GN   Name=BACE2 {ECO:0000313|Ensembl:ENSOCUP00000023300.3};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000023300.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000023300.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000023300.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000023300.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   AlphaFoldDB; G1U1R2; -.
DR   SMR; G1U1R2; -.
DR   STRING; 9986.ENSOCUP00000023300; -.
DR   PaxDb; 9986-ENSOCUP00000023300; -.
DR   Ensembl; ENSOCUT00000020935.3; ENSOCUP00000023300.3; ENSOCUG00000028198.3.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000159548; -.
DR   HOGENOM; CLU_830402_0_0_1; -.
DR   InParanoid; G1U1R2; -.
DR   TreeFam; TF329595; -.
DR   Proteomes; UP000001811; Unplaced.
DR   Bgee; ENSOCUG00000028198; Expressed in upper lobe of left lung and 15 other cell types or tissues.
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:Ensembl.
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   Gene3D; 2.40.70.10; Acid Proteases; 3.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR009119; BACE.
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; PR01815; BACEFAMILY.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        290..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..251
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   340 AA;  36631 MW;  5C40CDA0E5BD8179 CRC64;
     SSTYRPKGFD VTVKYTQGSW TGVVGEDLVT IPKGFNASFL VNVATIFESE NFFLPGIKWN
     GILGLAYATL AKPSSSLETF FDSLVAQAKI PDVFSMQMCG AGLPVAGSGT NGGSLVLGGI
     EPSLYKGDIW YTPIKEEWYY QIEILKLEVG GQSLNLDCRE VSALGIGKVE LKGKGGRTHS
     PRSCWTSPGS RCPPVVLPPQ LYIQPMVGAG LNYECYRFGI SPSTNALVIG ATVMEGFYVV
     FDRARRRVGF AASSCAEIAG APVSEISGPF STDDLASSCV PAQSLQEPTL WIISYALMSV
     CGAILLTLIA LLLLPLRCRH GARDPELVND ESSLVRHRWK
//
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