FACE1_ORYSJ
ID FACE1_ORYSJ Reviewed; 425 AA.
AC Q6EPN8; A3AA46; B9F1T6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=CAAX prenyl protease 1 homolog;
DE EC=3.4.24.84;
DE AltName: Full=Farnesylated proteins-converting enzyme 1;
DE Short=FACE-1;
DE AltName: Full=Prenyl protein-specific endoprotease 1;
DE AltName: Full=Zinc metalloproteinase Ste24 homolog;
GN Name=FACE1; Synonyms=STE24; OrderedLocusNames=Os02g0680400, LOC_Os02g45650;
GN ORFNames=OsJ_007668, OsJ_07930 {ECO:0000312|EMBL:EEE57578.1}, P0663F07.25;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 M48A family. {ECO:0000305}.
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DR EMBL; AP005823; BAD29382.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09653.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80294.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE57578.1; -; Genomic_DNA.
DR EMBL; AK102210; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015622849.1; XM_015767363.1.
DR AlphaFoldDB; Q6EPN8; -.
DR SMR; Q6EPN8; -.
DR STRING; 4530.OS02T0680400-01; -.
DR PaxDb; Q6EPN8; -.
DR PRIDE; Q6EPN8; -.
DR EnsemblPlants; Os02t0680400-01; Os02t0680400-01; Os02g0680400.
DR GeneID; 4330318; -.
DR Gramene; Os02t0680400-01; Os02t0680400-01; Os02g0680400.
DR KEGG; osa:4330318; -.
DR eggNOG; KOG2719; Eukaryota.
DR HOGENOM; CLU_025947_3_3_1; -.
DR InParanoid; Q6EPN8; -.
DR OMA; LPFKIYK; -.
DR OrthoDB; 878143at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6EPN8; baseline and differential.
DR Genevisible; Q6EPN8; OS.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..425
FT /note="CAAX prenyl protease 1 homolog"
FT /id="PRO_0000356241"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 285
FT /evidence="ECO:0000250"
FT ACT_SITE 366
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 288
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"
FT CONFLICT 153
FT /note="I -> V (in Ref. 5; AK102210)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="T -> A (in Ref. 5; AK102210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 48438 MW; 0496C1F0D1144885 CRC64;
MALPYLEAVL CFMILMYIFE TYLDIRQHRA LKLPTLPKPL VGVISGEKFE RSRAYSLDKS
KFHFIHEAVT ILMDTTILYY RVLPWVWKKS GELATNAGLN AENEILHTLA FLAGVMIWSQ
ITDLPFSLYS TFVIEAKHGF NKQTIWLFIR DMIKGILLSI LLGPPIVAAI IIIVQNGGPY
LAIYLWGFMF ALSLVMMTIY PIVIAPLFNK FTPLPEGVLR EKIEKLAASL SFPLKKLFVV
DGSTRSSHSN AYMYGFFKNK RIVLYDTLIQ QCSSEDEIVS VIAHELGHWK LNHTVYSFVA
VQLLMFLQFG GYTLVRNSKD LFESFGFEDQ PVIIGLIIFQ HTIIPVQHLL SFCLNLVSRA
FEFQADAFAK NLGYAPQLRA ALVKLQEENL SAMNTDPWYS AYHYSHPPLV ERLSALEDAD
SKKEN
