ID C3YUT2_BRAFL Unreviewed; 388 AA.
AC C3YUT2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Lysosomal aspartic protease-like {ECO:0000313|RefSeq:XP_035663526.1, ECO:0000313|RefSeq:XP_035663527.1};
GN Name=LOC118407207 {ECO:0000313|RefSeq:XP_035663526.1,
GN ECO:0000313|RefSeq:XP_035663527.1, ECO:0000313|RefSeq:XP_035663528.1,
GN ECO:0000313|RefSeq:XP_035663529.1, ECO:0000313|RefSeq:XP_035663530.1};
GN ORFNames=BRAFLDRAFT_74093 {ECO:0000313|EMBL:EEN55983.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN55983.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN55983.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN55983.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
RN [2] {ECO:0000313|RefSeq:XP_035663526.1, ECO:0000313|RefSeq:XP_035663527.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035663526.1,
RC ECO:0000313|RefSeq:XP_035663527.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035663526.1,
RC ECO:0000313|RefSeq:XP_035663527.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GG666554; EEN55983.1; -; Genomic_DNA.
DR RefSeq; XP_002599971.1; XM_002599925.1.
DR RefSeq; XP_035663526.1; XM_035807633.1.
DR RefSeq; XP_035663527.1; XM_035807634.1.
DR RefSeq; XP_035663528.1; XM_035807635.1.
DR RefSeq; XP_035663529.1; XM_035807636.1.
DR RefSeq; XP_035663530.1; XM_035807637.1.
DR STRING; 7739.C3YUT2; -.
DR MEROPS; A01.009; -.
DR KEGG; bfo:118407207; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; C3YUT2; -.
DR OMA; HDEMCRV; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000001554; Chromosome 19.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; 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:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454,
KW ECO:0000313|RefSeq:XP_035663526.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..388
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041156895"
FT DOMAIN 69..385
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 273
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 100..107
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 307..344
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 388 AA; 41953 MW; 2EA759138D10FE4E CRC64;
MKFLLVLLAI VATANALHRI PLTKMKTVRR HLAEVGVPYD KIIKDYSGKY YNMTGPQPEP
LSNYLDAQYF GPISIGTPPQ SFQVVFDTGS SNLWVPSKKC HYSNIACLLH NKYDASKSST
YKKNGEKFAI QYGSGSLSGF LSQDTVSVAG IEVKDQTFAE ALSEPGMAFV AAKFDGILGM
GYSNIAVDGV VPPFYNMVSQ GAVPEPVFSF YLNRDPSATA GGELILGGAD PNYYTGDFTF
LDVTRKGYWQ FKMDGINVGG STFCQEGCQA IADTGTSLIA GPIEEVNKLH KQIGATPLAG
GEYKVDCSKV TSLPTISFIL GGKEFELTGK EYILQVKQFG MTICLSGFMG MDIPPPAGPL
WILGDVFIGS YYTQFDLGKN LVGFATAK
//
