ID Q4U1U4_PIG Unreviewed; 410 AA.
AC Q4U1U4;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Cathepsin D {ECO:0000256|ARBA:ARBA00015582};
DE EC=3.4.23.5 {ECO:0000256|ARBA:ARBA00011930};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:AAY42144.1};
RN [1] {ECO:0000313|EMBL:AAY42144.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18607787; DOI=10.1080/10495390802072088;
RA Mei Y., Chen Y., Li J., Gao P., Wang C., Zhang H., Ling F., Li Y., Xie S.,
RA Li S., Zhang G.;
RT "Sequence identification, tissue distribution and polymorphism of the
RT porcine cathepsin D (CTSD) gene.";
RL Anim. Biotechnol. 19:144-158(2008).
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 EMBL; DQ018727; AAY42144.1; -; mRNA.
DR RefSeq; NP_001032810.1; NM_001037721.1.
DR AlphaFoldDB; Q4U1U4; -.
DR MEROPS; A01.009; -.
DR GeneID; 494568; -.
DR KEGG; ssc:494568; -.
DR CTD; 1509; -.
DR OrthoDB; 1120702at2759; -.
DR Genevisible; Q4U1U4; SS.
DR GO; GO:0005764; C:lysosome; 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; 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 2: Evidence at transcript level;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..410
FT /note="Cathepsin D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004244818"
FT DOMAIN 79..405
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT DISULFID 91..160
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-2"
FT DISULFID 110..117
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 284..288
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 327..364
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 410 AA; 44226 MW; A7803F1FF40631B8 CRC64;
MQPPSLLLLA LGLLAAPAAA LIRIPLHKFT SIRRTMSEVG GPVENLIAKG PILKYSQGVP
AVTQGPIPEV LKNYMDAQNY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH
HKYNSGKSST YVKNGTTFAI HYGSGSLSGY WSQDTVSVPC NSALLGVGGI KVERQTFGEA
TKQPGLTFIA AKFDGILGMA YPRISVNNVV PVFDNLMQQK LVDKNIFSFY LNRDPGAQPG
GELMLGGIDS KYYKGSLDYH NVTRKAYWQI HMDQVAVGSS LTLCKGGCEA IVDTGTSLIV
GPVEEVRELQ KAIGAVPLIQ GEYMIPCEKV PSLPDVTVTL GGKKYKLSSE NYTLKVSQAG
QTICLSGFMG MDIPPPGGPL WILGDVFIGR YYTVFDRDLN RVGLAEAATL
//
