ID A0A151MCG3_ALLMI Unreviewed; 405 AA.
AC A0A151MCG3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Cathepsin D {ECO:0000256|ARBA:ARBA00015582};
DE EC=3.4.23.5 {ECO:0000256|ARBA:ARBA00011930};
GN Name=CTSD {ECO:0000313|EMBL:KYO22169.1};
GN ORFNames=Y1Q_0000762 {ECO:0000313|EMBL:KYO22169.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO22169.1};
RN [1] {ECO:0000313|EMBL:KYO22169.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO22169.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO22169.1}.
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DR EMBL; AKHW03006283; KYO22169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151MCG3; -.
DR STRING; 8496.A0A151MCG3; -.
DR GlyCosmos; A0A151MCG3; 2 sites, No reported glycans.
DR eggNOG; KOG1339; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
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; 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; 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|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..405
FT /note="Cathepsin D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007584983"
FT DOMAIN 85..402
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 290
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT DISULFID 116..123
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 281..285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 324..361
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 405 AA; 44348 MW; 80DCCB9518D75BA3 CRC64;
MAQPGFSVLS IYSPLALWVL ISSENQALAI IPLTKFPSMR RVLNEVGSEI PDLNTVNEFL
KYKLDVPGIG EPTPEILKNY MDAQYYGEIG IGTPPQKFTV VFDTGSSNLW VPSIHCHLLD
IACLLHHKYD ASKSTTYVKN GTDFAIHYGT GSLSGYLSQD FVTLGGLKVK DQVFGEAVKQ
PGITFIAAKF DGILGMAFPK ISVKKVTPFF DNVMRQQLIE KNIFSFYLNR DPTAQPGGEL
LLGGTDPKYY SGDFNWVNVT RSAYWQIRMD QLNVANGPTL CKEGCEAIVD TGTSLITGPT
EEVKELQKAI GAKPLIKGQY VIPCEKVPTL PSVSLVLGGK PYQLTGEQYI FKVTVQGQTI
CLSGFSGLDV PPPGGPLWIL GDVFIGPYYT VFDRDNEAVG FAKCN
//
