ID B3RU95_TRIAD Unreviewed; 505 AA.
AC B3RU95;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=TRIADDRAFT_55204 {ECO:0000313|EMBL:EDV25772.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV25772.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV25772.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV25772.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; DS985244; EDV25772.1; -; Genomic_DNA.
DR RefSeq; XP_002111805.1; XM_002111769.1.
DR AlphaFoldDB; B3RU95; -.
DR EnsemblMetazoa; TriadT55204; TriadP55204; TriadG55204.
DR GeneID; 6753018; -.
DR KEGG; tad:TRIADDRAFT_55204; -.
DR CTD; 6753018; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_039009_0_0_1; -.
DR InParanoid; B3RU95; -.
DR OMA; FLWTIVG; -.
DR OrthoDB; 603414at2759; -.
DR PhylomeDB; B3RU95; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR009119; BACE.
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; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR01815; BACEFAMILY.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..505
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002798308"
FT TRANSMEM 430..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 468..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 56142 MW; 4814F94C57323120 CRC64;
MNIVWRFILN ILAFMMVAGD IPFDKIDKSV KIHKYSLYRV HKWKENNFQN APSELSTRID
RMRGFPDIGY AIHITVGTPG QQFNALVDTG SSNFAIAASP NAGVPSYYHS RRSSTFQNRS
QQVTVQYGKG TWTGDLMSDI VHLDVGFNRA IRQDFSGTPT KTFFDQLVDK TGIANIFSLT
LYGPVLSKGL SWTSKDSNYG GEMTFGGIDR TLFLGHVYYT PVIKKWYYEV KLLNISVDGK
PITMCCHGYE KYVTFVDSGT TEIVVPPAVF RTIVHSLQKF IQAPKLFWEG REVICPAGLG
IAWSSLPIIE FTLPLAGVDG VLAYESSRFN LAISPQQYIR LSETVRNLGF PCYTFSISPS
SNDAPVIILG DALMEGYTVV FDRINNQVGF AVSRFAAKNL TVSPGINRLE RVKNGSLNIQ
NISSSSEDSV AIVSVVLASI SLFMTCISIG VMTCIYFNHH RNKSSNDYPY RQVSSPHHPP
AYSNAEEQYG SRDNSLADNG PTESD
//