ID Q7T0Y2_XENLA Unreviewed; 500 AA.
AC Q7T0Y2;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Bace2-prov protein {ECO:0000313|EMBL:AAH55989.1};
DE SubName: Full=Beta-secretase 2 L homeolog precursor {ECO:0000313|RefSeq:NP_001080615.1};
DE EC=3.4.23.45 {ECO:0000313|RefSeq:NP_001080615.1};
GN Name=bace2.L {ECO:0000313|RefSeq:NP_001080615.1,
GN ECO:0000313|Xenbase:XB-GENE-17346104};
GN Synonyms=aeplc {ECO:0000313|RefSeq:NP_001080615.1}, alp56
GN {ECO:0000313|RefSeq:NP_001080615.1}, asp1
GN {ECO:0000313|RefSeq:NP_001080615.1}, asp21
GN {ECO:0000313|RefSeq:NP_001080615.1}, bace2
GN {ECO:0000313|RefSeq:NP_001080615.1,
GN ECO:0000313|Xenbase:XB-GENE-17346104}, bae2
GN {ECO:0000313|RefSeq:NP_001080615.1}, cda13
GN {ECO:0000313|RefSeq:NP_001080615.1}, ceap1
GN {ECO:0000313|RefSeq:NP_001080615.1}, drap
GN {ECO:0000313|RefSeq:NP_001080615.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH55989.1};
RN [1] {ECO:0000313|RefSeq:NP_001080615.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH55989.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH55989.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001080615.1}
RP IDENTIFICATION.
RG RefSeq;
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 EMBL; BC055989; AAH55989.1; -; mRNA.
DR RefSeq; NP_001080615.1; NM_001087146.1.
DR MEROPS; A01.041; -.
DR DNASU; 380307; -.
DR GeneID; 380307; -.
DR KEGG; xla:380307; -.
DR AGR; Xenbase:XB-GENE-17346104; -.
DR CTD; 380307; -.
DR Xenbase; XB-GENE-17346104; bace2.L.
DR OrthoDB; 603414at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 380307; Expressed in stomach and 19 other cell types or tissues.
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; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
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:UP000186698};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001080615.1};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..500
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001080615.1"
FT /id="PRO_5033206568"
FT TRANSMEM 451..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..413
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 94
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT DISULFID 217..417
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT DISULFID 276..441
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT DISULFID 328..377
FT /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
SQ SEQUENCE 500 AA; 54723 MW; 10F16756CAFDCD0B CRC64;
MKVPLVRLLL LCAAACASNK FIVPLNVSPA EIKGTLPVAP ATPKDKPGLL LASDPGGTIN
FFSMVDNLAG DSGRGYYLEL LIGSPPQKVN ILVDTGSSNF AVAGSPNPDV NTFFDSKLST
SYQSLNTEVT VRYTQGSWTG LLGKDVVSIP KGVNGTFLIN IASIFQSESF FLPNINWQGI
LGLAYSTLAK PSSSVEPFFD SLVQQENIPD VFSMQMCGAG QSSPGNGINA GSLVLGGVEP
SLYKGNIWYT PITEEWYYQV EVLKFEVGGQ RLNLDCTVYN SDKAIVDSGT TLLRLPDKVF
NAMVDAIVQT SLIQNFNAEF WAGLQLACWD KTQQPWNYFP DISIYLRDTN TSRSFRLTLK
PQLYIQSVLT FQESLNCFRF GISQSASTLV IGATVMEGFY VIFDRAEKRV GFAVSSCAEV
SGITVSEIAG PFGTSDVSSN CIARNPLREP IMWIISYSLM SLCGMILLVL VILLLLSNRQ
RHDDMETIND ESSLVQHRWK
//
