FACE1_CAEEL
ID FACE1_CAEEL Reviewed; 442 AA.
AC Q9XVE5;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=CAAX prenyl protease 1 homolog {ECO:0000305};
DE EC=3.4.24.84 {ECO:0000269|PubMed:12487630};
DE AltName: Full=Farnesylated proteins-converting enzyme 1 {ECO:0000303|PubMed:12487630};
DE Short=FACE-1 {ECO:0000303|PubMed:12487630};
GN Name=fce-1 {ECO:0000312|WormBase:C04F12.10};
GN ORFNames=C04F12.10 {ECO:0000312|WormBase:C04F12.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12487630; DOI=10.1042/bj20021514;
RA Cadinanos J., Schmidt W.K., Fueyo A., Varela I., Lopez-Otin C.,
RA Freije J.M.P.;
RT "Identification, functional expression and enzymic analysis of two distinct
RT CaaX proteases from Caenorhabditis elegans.";
RL Biochem. J. 370:1047-1054(2003).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated proteins. {ECO:0000269|PubMed:12487630}.
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:0000269|PubMed:12487630};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O75844};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P47154}; Multi-pass membrane protein
CC {ECO:0000255}. Membrane {ECO:0000269|PubMed:12487630}.
CC -!- SIMILARITY: Belongs to the peptidase M48A family. {ECO:0000305}.
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DR EMBL; Z81461; CAB03839.1; -; Genomic_DNA.
DR PIR; T18917; T18917.
DR RefSeq; NP_492582.1; NM_060181.4.
DR AlphaFoldDB; Q9XVE5; -.
DR SMR; Q9XVE5; -.
DR STRING; 6239.C04F12.10.1; -.
DR EPD; Q9XVE5; -.
DR PaxDb; Q9XVE5; -.
DR PeptideAtlas; Q9XVE5; -.
DR EnsemblMetazoa; C04F12.10.1; C04F12.10.1; WBGene00001405.
DR GeneID; 172820; -.
DR KEGG; cel:CELE_C04F12.10; -.
DR UCSC; C04F12.10; c. elegans.
DR CTD; 172820; -.
DR WormBase; C04F12.10; CE19683; WBGene00001405; fce-1.
DR eggNOG; KOG2719; Eukaryota.
DR GeneTree; ENSGT00390000002053; -.
DR HOGENOM; CLU_025947_3_3_1; -.
DR InParanoid; Q9XVE5; -.
DR OMA; LPFKIYK; -.
DR OrthoDB; 878143at2759; -.
DR PhylomeDB; Q9XVE5; -.
DR PRO; PR:Q9XVE5; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001405; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:WormBase.
DR GO; GO:0071586; P:CAAX-box protein processing; IDA:WormBase.
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 Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..442
FT /note="CAAX prenyl protease 1 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431785"
FT TOPO_DOM 1..62
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..146
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..311
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..442
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 302
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT ACT_SITE 384
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75844"
SQ SEQUENCE 442 AA; 50699 MW; 63918265AFECC717 CRC64;
MDASCLFKAL LATNWALFLW DQYITFRQYK AHKNAVKRPN EVKELIGEED YKKARDYKID
NHLFGFFHSW FNQLLLTAQL IGGYYPFLWY ATASYPLHVA VFLSINSIIE TIIDLPWDLY
STFIIEDAHG FNKQTIGFYF VDKIKKMLVG FALTMPIVYG IEWIIVNGGP YFFVYIWLFV
SVVVLLLMTI YPTFIAPLFD KYFPLPDGDL KTKIEQLAAS LSYPLTELYV VNGSKRSAHS
NAYMYGFWKN KRIVLYDTLL SGAEKEKVHE LYVAAGEKIE ETENDKKRGM NNDEVVAVLG
HELGHWALWH TLINLVITEV NLFFSFAVFG YFYKWEALYQ GFGYHDTPPV IGMMLIFQFV
LALYNQLASI GMVIHSRSAE FGADEFAANL GHGENLIGAL TKLGVDNLSM PINDSLYSWC
THTHPPVVER VAAVRAFQAK NK
