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Database: UniProt
Entry: L7N2R0_XENTR
LinkDB: L7N2R0_XENTR
Original site: L7N2R0_XENTR 
ID   L7N2R0_XENTR            Unreviewed;       421 AA.
AC   L7N2R0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 4.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Cathepsin D {ECO:0000256|ARBA:ARBA00015582};
DE            EC=3.4.23.5 {ECO:0000256|ARBA:ARBA00011930};
GN   Name=ctsd {ECO:0000313|Ensembl:ENSXETP00000010029};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000010029};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000010029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000010029};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000010029}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2013) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specificity similar to, but narrower than, that of pepsin A.
CC         Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.;
CC         EC=3.4.23.5; Evidence={ECO:0000256|ARBA:ARBA00000585};
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   AlphaFoldDB; L7N2R0; -.
DR   STRING; 8364.ENSXETP00000010029; -.
DR   Ensembl; ENSXETT00000010029; ENSXETP00000010029; ENSXETG00000024956.
DR   Xenbase; XB-GENE-5906945; ctsd.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_3_1; -.
DR   Bgee; ENSXETG00000024956; Expressed in early embryo and 16 other cell types or tissues.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05490; Cathepsin_D2; 1.
DR   Gene3D; 2.60.40.1960; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR033144; Cathepsin_D.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF42; CATHEPSIN D; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
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|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          101..418
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        132..139
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        297..301
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        340..377
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   421 AA;  45595 MW;  3C31B8A27A70EFEE CRC64;
     MLGHCKQTYI YIQSGESHSR TVMASLLVWV VLLASSLLQP GSALIRIPLK KFPSIRHTFT
     EAGKDVKELL ANEVPLKYSP GFPPSGEPTP EALKNYLDAQ YYGEIGLGSP PQNFTVVFDT
     GSSNLWVPSV HCSMLDIACW MHHKYDSSKS STYVKNGTAF AIQYGTGSLS GYLSKDTVTI
     GNLAVKGQIF GEAVKQPGVT FVAAKFDGIL GMAYPVISVD GAPPVFDNIM AQKLVESNIF
     SFYLNRNPDT QPGGELLLGG TDPKYYTGDF HYLSVTRKAY WQIHMDQLGV GDQLTLCKGG
     CEVIVDTGTS LITGPLEEVT ALQKAIGAVP LIQGQYMVQC DKVPTLPVIS LTLGGQVYTL
     TGEQYIMKVS QLGSTICLSG FMGLNIPPPA GPLWILGDVF IGQYYSVFDR ANNRVGFAKA
     K
//
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