FACE_TAESO
ID FACE_TAESO Reviewed; 472 AA.
AC Q3Y6B8;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=CAAX prenyl protease 1 homolog {ECO:0000305};
DE EC=3.4.24.84 {ECO:0000250|UniProtKB:Q9XVE5};
DE AltName: Full=Zinc metalloproteinase Ste24 homolog {ECO:0000305|PubMed:16750535};
GN Name=TsSte24p {ECO:0000303|PubMed:16750535};
OS Taenia solium (Pork tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=6204 {ECO:0000312|EMBL:AAZ80484.1};
RN [1] {ECO:0000312|EMBL:AAZ80484.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=16750535; DOI=10.1016/j.ijpara.2006.03.009;
RA Cai G.B., Bae Y.A., Kim S.H., Na B.K., Kim T.S., Jiang M.S., Kong Y.;
RT "A membrane-associated metalloprotease of Taenia solium metacestode
RT structurally related to the FACE-1/Ste24p protease family.";
RL Int. J. Parasitol. 36:925-935(2006).
CC -!- FUNCTION: Zinc-dependent metalloproteinase (PubMed:16750535).
CC Proteolytically removes the C-terminal three residues of farnesylated
CC proteins (By similarity). {ECO:0000250|UniProtKB:Q9XVE5,
CC ECO:0000269|PubMed:16750535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The peptide bond hydrolyzed can be designated -C-|-A-A-X in
CC which C is an S-isoprenylated cysteine residue, A is usually
CC aliphatic and X is the C-terminal residue of the substrate protein,
CC and may be any of several amino acids.; EC=3.4.24.84;
CC Evidence={ECO:0000250|UniProtKB:Q9XVE5};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16750535};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844};
CC -!- ACTIVITY REGULATION: Inhibited by ethylenediaminetetraacetic acid
CC (EDTA) but not by serine, aspartic or cysteine protease inhibitors.
CC Inhibited by high concentration of Zn(2+) (> 0.1 mM).
CC {ECO:0000269|PubMed:16750535}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:16750535};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. Loss of catalytic activity
CC at temperatures above 50 degrees Celsius.
CC {ECO:0000269|PubMed:16750535};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:16750535}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P47154}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in scolex and bladder wall of
CC metacestode larval stage. Expressed in adults.
CC {ECO:0000269|PubMed:16750535}.
CC -!- SIMILARITY: Belongs to the peptidase M48A family. {ECO:0000305}.
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DR EMBL; DQ154010; AAZ80484.1; -; mRNA.
DR AlphaFoldDB; Q3Y6B8; -.
DR SMR; Q3Y6B8; -.
DR MEROPS; M48.003; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0071586; P:CAAX-box protein processing; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd07343; M48A_Zmpste24p_like; 1.
DR InterPro; IPR027057; CAXX_Prtase_1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR032456; Peptidase_M48_N.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..472
FT /note="CAAX prenyl protease 1 homolog"
FT /id="PRO_0000444118"
FT TOPO_DOM 1..8
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..124
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..207
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..382
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 330
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT ACT_SITE 414
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75844"
SQ SEQUENCE 472 AA; 54546 MW; D671C1DD0C29644E CRC64;
MDVGGALDLY GCSVNVYNAI LIFIWVLFLW ETYINLRQLK VAKRVTESPE EIKCLMNDVD
FDKSRRYAID KMNFDIVSGF YNILSLSAVL YFQLIAWAWH KSQEHMLFVC SYAPRSFGTT
EGSEILFSLL FTVYVALFQF FESLPWSYYR HFVIEERYGF NKQTIGFFIK DRLKSLAVGL
VIGLPIISML VWIIKAGGHY FYIYAYGFTF VVSFIIMFIY PEFIAPIFDR YEHFPDCELR
KKIEELAASI EFPLKKLYVV EGSKRSSHSN AYFYGFGKNK RIVLFDTLIK GFKMPGVEAD
SSANADESSD ETQNRGCGDD EEILATLAHE LGHWKLKHMT FNLIIAQINI FFMFFAFGQL
INVDQLFVDF GFPPSTAPIL IRLIVVFQFI FMPYSSVLEF LMTMLSRKFE FQADAFAVSL
KSGEKLKSAL LVLTKDNLSF PVYDWLYSMC NHSHPPIIER LAAIDAKMGK EK
