ID A0A067G1L0_CITSI Unreviewed; 504 AA.
AC A0A067G1L0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CISIN_1g010195mg {ECO:0000313|EMBL:KDO72240.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO72240.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO72240.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KK784888; KDO72240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067G1L0; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR Gene3D; 1.10.225.10; Saposin-like; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF20; EUKARYOTIC ASPARTYL PROTEASE FAMILY PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF47862; Saposin; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 3: Inferred from homology;
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..504
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001637592"
FT DOMAIN 80..501
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 310..350
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 374..415
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 111..117
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 276..280
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 504 AA; 55862 MW; F5CE8EDEB853FD29 CRC64;
MGIKFLLAAI CMWVCPCILA SMPPPPPPSH GLLRIQLKKR QLGINTINAA RLITKNEVHN
RFNHPKADVV YLNNYLDAQY YGEIGIGSPP QSFSVVFDTG SSNLWVPSSK CLFSISCYLH
SRYRARLSRT YTKIGVPCKI HYGSGQISGF FSQDNVKIGD MIIKDQEFVE VTKEGLLPFL
ALQFDGILGL GFRDIAAGNA TPLWYNMVRQ GHISQKIFSL WLNQDPNSEV GGEIIFGGFD
WRHFRGSHIY VPITEKGYWQ IKVGDILIEN SSTGFCEDGC TAILDSGTSV LAGPTTVVAQ
INHAIGAEGI VSMQCKTVVF EYGNMIWEFL ISGVQPETVC SDIGLCVYNG SSYMSTGIET
VVQHKTSNGS SINESTLCAF CEMIVFWIQM QLKQQKTKEA IFKYADKLCE VLPNPMGKSF
INCDDIASMP YVSFTIGNRS FPLSPEQYIF KIEEGHSTIC ISGFIALDVP PPQGPLWVLG
DMFLRAYHTV FDFGNLQIGF AEAA
//
