FACE1_DICDI
ID FACE1_DICDI Reviewed; 426 AA.
AC Q54FH7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=CAAX prenyl protease 1 homolog;
DE EC=3.4.24.84;
DE AltName: Full=Prenyl protein-specific endoprotease 1;
GN Name=zmpste24; ORFNames=DDB_G0290849;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated proteins. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000305}.
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DR EMBL; AAFI02000171; EAL62019.1; -; Genomic_DNA.
DR RefSeq; XP_635524.1; XM_630432.1.
DR AlphaFoldDB; Q54FH7; -.
DR SMR; Q54FH7; -.
DR STRING; 44689.DDB0237846; -.
DR MEROPS; M48.A08; -.
DR PaxDb; Q54FH7; -.
DR EnsemblProtists; EAL62019; EAL62019; DDB_G0290849.
DR GeneID; 8627861; -.
DR KEGG; ddi:DDB_G0290849; -.
DR dictyBase; DDB_G0290849; zmpste24.
DR eggNOG; KOG2719; Eukaryota.
DR HOGENOM; CLU_025947_3_3_1; -.
DR InParanoid; Q54FH7; -.
DR OMA; FYFLEVA; -.
DR PhylomeDB; Q54FH7; -.
DR PRO; PR:Q54FH7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:dictyBase.
DR GO; GO:0071586; P:CAAX-box protein processing; IBA:GO_Central.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..426
FT /note="CAAX prenyl protease 1 homolog"
FT /id="PRO_0000328899"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..106
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..178
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..333
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 283
FT /evidence="ECO:0000250"
FT ACT_SITE 366
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 426 AA; 49930 MW; A05A32D4C30623EE CRC64;
MVNYFIISIS FFLLEHFYSF YLNFRQSKLL KNLTKVPEYC KDRITQEDFK KSQEYSKAKL
DYKTLTSTIQ VLTTLLSFYY PVYPYFWNLS LELAEKIGYP NEIIRSCFFF AFTVGVSVIT
EIPFSYYYQF ILEEKFGYNR MTRTLFIKDK IISTLLMIGF GLPILSLAIF IINWSGPQLW
FYCWLLLVAI TLLSITIYPT FIQPLFNKFT PVDGELAESI FALAKRVGFP ASKDTIFVVD
NSKRDGHMNA YFYGLFGTKR IVLYDTLVNE LDKEELLAVM GHEFGHYKMS HTLKQMLLVQ
VHLVTLLYAF SLLINDDQLY QQFGFVSSKD SVLVGLTLFM FLYSPIDRIF SLLINIFSRK
YEFQADDFAV ELGFLNSNHL FKLHFKELGC LVYDPLYSAY HHSHPTLVER SNNIDKKVAL
YKLKNK
