FACE1_MOUSE
ID FACE1_MOUSE Reviewed; 475 AA.
AC Q80W54; Q8BJK4; Q8K569;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=Zmpste24; Synonyms=Face1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11399759; DOI=10.1074/jbc.m102908200;
RA Leung G.K., Schmidt W.K., Bergo M.O., Gavino B., Wong D.H., Tam A.,
RA Ashby M.N., Michaelis S., Young S.G.;
RT "Biochemical studies of Zmpste24-deficient mice.";
RL J. Biol. Chem. 276:29051-29058(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION IN LAMIN A/C PROCESSING.
RC STRAIN=C57BL/6J;
RX PubMed=11923874; DOI=10.1038/ng871;
RA Pendas A.M., Zhou Z., Cadinanos J., Freije J.M.P., Wang J., Hultenby K.,
RA Astudillo A., Wernerson A., Rodriguez F., Triggvason K., Lopez-Otin C.;
RT "Defective prelamin A processing and muscular and adipocyte alterations in
RT Zmpste24 metalloproteinase deficient mice.";
RL Nat. Genet. 31:94-99(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated proteins. Acts on lamin A/C.
CC {ECO:0000269|PubMed:11923874}.
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}. Nucleus inner membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The metalloprotease domain is constituted by the two C-terminal
CC nuclear regions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M48A family. {ECO:0000305}.
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DR EMBL; AY029194; AAK38172.1; -; mRNA.
DR EMBL; AJ487544; CAD31792.1; -; mRNA.
DR EMBL; AK083566; BAC38953.1; -; mRNA.
DR CCDS; CCDS18600.1; -.
DR RefSeq; NP_766288.1; NM_172700.2.
DR AlphaFoldDB; Q80W54; -.
DR SMR; Q80W54; -.
DR STRING; 10090.ENSMUSP00000053900; -.
DR BindingDB; Q80W54; -.
DR ChEMBL; CHEMBL1075286; -.
DR DrugCentral; Q80W54; -.
DR MEROPS; M48.003; -.
DR iPTMnet; Q80W54; -.
DR PhosphoSitePlus; Q80W54; -.
DR SwissPalm; Q80W54; -.
DR EPD; Q80W54; -.
DR jPOST; Q80W54; -.
DR MaxQB; Q80W54; -.
DR PaxDb; Q80W54; -.
DR PRIDE; Q80W54; -.
DR ProteomicsDB; 271852; -.
DR Antibodypedia; 1711; 416 antibodies from 31 providers.
DR DNASU; 230709; -.
DR Ensembl; ENSMUST00000058754; ENSMUSP00000053900; ENSMUSG00000043207.
DR GeneID; 230709; -.
DR KEGG; mmu:230709; -.
DR UCSC; uc008uny.1; mouse.
DR CTD; 10269; -.
DR MGI; MGI:1890508; Zmpste24.
DR VEuPathDB; HostDB:ENSMUSG00000043207; -.
DR eggNOG; KOG2719; Eukaryota.
DR GeneTree; ENSGT00390000002053; -.
DR HOGENOM; CLU_025947_3_0_1; -.
DR InParanoid; Q80W54; -.
DR OMA; LPFKIYK; -.
DR OrthoDB; 878143at2759; -.
DR PhylomeDB; Q80W54; -.
DR TreeFam; TF105972; -.
DR BRENDA; 3.4.24.84; 3474.
DR BioGRID-ORCS; 230709; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Zmpste24; mouse.
DR PRO; PR:Q80W54; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80W54; protein.
DR Bgee; ENSMUSG00000043207; Expressed in cleaving embryo and 247 other tissues.
DR ExpressionAtlas; Q80W54; baseline and differential.
DR Genevisible; Q80W54; MM.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IGI:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0030282; P:bone mineralization; IGI:MGI.
DR GO; GO:0071586; P:CAAX-box protein processing; IBA:GO_Central.
DR GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; IMP:MGI.
DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; IMP:MGI.
DR GO; GO:0061337; P:cardiac conduction; IMP:MGI.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0003231; P:cardiac ventricle development; IMP:MGI.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IMP:MGI.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0003417; P:growth plate cartilage development; IMP:MGI.
DR GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0043969; P:histone H2B acetylation; IMP:MGI.
DR GO; GO:0043979; P:histone H2B-K5 acetylation; IMP:MGI.
DR GO; GO:0044029; P:hypomethylation of CpG island; IMP:MGI.
DR GO; GO:0006925; P:inflammatory cell apoptotic process; IMP:MGI.
DR GO; GO:0060993; P:kidney morphogenesis; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0043007; P:maintenance of rDNA; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:1903799; P:negative regulation of miRNA maturation; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:MGI.
DR GO; GO:0006997; P:nucleus organization; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0030327; P:prenylated protein catabolic process; IDA:MGI.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0010506; P:regulation of autophagy; IMP:MGI.
DR GO; GO:1903522; P:regulation of blood circulation; IMP:MGI.
DR GO; GO:0030500; P:regulation of bone mineralization; IGI:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
DR GO; GO:2000772; P:regulation of cellular senescence; IMP:MGI.
DR GO; GO:0050688; P:regulation of defense response to virus; IMP:MGI.
DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IMP:MGI.
DR GO; GO:0044030; P:regulation of DNA methylation; IMP:MGI.
DR GO; GO:0048145; P:regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IMP:MGI.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR GO; GO:0090239; P:regulation of histone H4 acetylation; IMP:MGI.
DR GO; GO:2000618; P:regulation of histone H4-K16 acetylation; IMP:MGI.
DR GO; GO:0032350; P:regulation of hormone metabolic process; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:MGI.
DR GO; GO:1903463; P:regulation of mitotic cell cycle DNA replication; IMP:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IGI:MGI.
DR GO; GO:1903025; P:regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IMP:MGI.
DR GO; GO:0070302; P:regulation of stress-activated protein kinase signaling cascade; IMP:MGI.
DR GO; GO:2000730; P:regulation of termination of RNA polymerase I transcription; IMP:MGI.
DR GO; GO:0032006; P:regulation of TOR signaling; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:MGI.
DR GO; GO:0072423; P:response to DNA damage checkpoint signaling; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR GO; GO:0003229; P:ventricular cardiac muscle tissue development; IMP:MGI.
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 Nucleus; Protease; Reference proteome; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..475
FT /note="CAAX prenyl protease 1 homolog"
FT /id="PRO_0000138845"
FT TOPO_DOM 1..18
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..81
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..123
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..170
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..195
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..347
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..382
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..475
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT REGION 293..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 336
FT /evidence="ECO:0000250"
FT ACT_SITE 419
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 53
FT /note="A -> S (in Ref. 2; CAD31792)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="H -> Q (in Ref. 1; AAK38172)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="H -> Q (in Ref. 1; AAK38172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 54735 MW; 509B82D757FC7A4B CRC64;
MGMWASVDAM WDFPAEKRIF GAVLLFSWTV YLWETFLAQR QRRIYKTTTR VPAELEQIMD
SDTFEKSRLY QLDKSTFSFW SGLYSEVEGT FILLFGGIPY LWRLSGQFCS SAGFGPEYEI
IQSLVFLLLA TLFSALTGLP WSLYNTFVIE EKHGFNHQTL EFFMKDAIKK FIVTQCILLP
VSALLLYIIK IGGDYFFIYA WLFTLVVSLV LVTIYADYIA PLFDKFTPLP EGKLKQEIEV
MAKSIDFPLT KVYVVEGSKR SSHSNAYFYG FFKNKRIVLF DTLLEEYSVP NKDNQEESGM
EARNEGEGDS EEVKAKVKNK KQGCKNEEVL AVLGHELGHW KLGHTVKNII ISQMNSFLCF
FLFAVLIGRR ELFAAFGFYD SQPTLIGLLI IFQFIFSPYN EVLSFCLTVL SRRFEFQADA
FAKKLGKAKD LYSALIKLNK DNLGFPVSDW LFSTWHYSHP PLLERLQALK NAKQD
