FACE1_HUMAN
ID FACE1_HUMAN Reviewed; 475 AA.
AC O75844; B3KQI7; D3DPU7; Q8NDZ8; Q9UBQ2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 198.
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, STE24;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10076063; DOI=10.1016/s0304-4165(98)00170-6;
RA Kumagai H., Kawamura Y., Yanagisawa K., Komano H.;
RT "Identification of a human cDNA encoding a novel protein structurally
RT related to the yeast membrane-associated metalloprotease, Ste24p.";
RL Biochim. Biophys. Acta 1426:468-474(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=B-cell, and Fetal brain;
RX PubMed=9700155; DOI=10.1083/jcb.142.3.635;
RA Tam A., Nouvet F.J., Fujimura-Kamada K., Slunt H., Sisodia S.S.,
RA Michaelis S.;
RT "Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal
RT proteolysis and COOH-terminal CAAX processing.";
RL J. Cell Biol. 142:635-649(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=10373325; DOI=10.1006/geno.1999.5834;
RA Freije J.M.P., Blay P., Pendas A.M., Cadinanos J., Crespo P.,
RA Lopez-Otin C.;
RT "Identification and chromosomal location of two human genes encoding
RT enzymes potentially involved in proteolytic maturation of farnesylated
RT proteins.";
RL Genomics 58:270-280(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-137.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH TETRAPEPTIDE, ACTIVE
RP SITE, COFACTOR, METALLOPROTEASE DOMAIN, TOPOLOGY, ZINC-BINDING SITES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23539603; DOI=10.1126/science.1231513;
RA Quigley A., Dong Y.Y., Pike A.C., Dong L., Shrestha L., Berridge G.,
RA Stansfeld P.J., Sansom M.S., Edwards A.M., Bountra C., von Delft F.,
RA Bullock A.N., Burgess-Brown N.A., Carpenter E.P.;
RT "The structural basis of ZMPSTE24-dependent laminopathies.";
RL Science 339:1604-1607(2013).
RN [11]
RP VARIANT MADB ARG-340.
RX PubMed=12913070; DOI=10.1093/hmg/ddg213;
RA Agarwal A.K., Fryns J.-P., Auchus R.J., Garg A.;
RT "Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral
RT dysplasia.";
RL Hum. Mol. Genet. 12:1995-2001(2003).
RN [12]
RP INVOLVEMENT IN RSDM1.
RX PubMed=15317753; DOI=10.1093/hmg/ddh265;
RA Navarro C.L., De Sandre-Giovannoli A., Bernard R., Boccaccio I., Boyer A.,
RA Genevieve D., Hadj-Rabia S., Gaudy-Marqueste C., Smitt H.S., Vabres P.,
RA Faivre L., Verloes A., Van Essen T., Flori E., Hennekam R., Beemer F.A.,
RA Laurent N., Le Merrer M., Cau P., Levy N.;
RT "Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and
RT identify restrictive dermopathy as a lethal neonatal laminopathy.";
RL Hum. Mol. Genet. 13:2493-2503(2004).
RN [13]
RP VARIANT MADB SER-265.
RX PubMed=17152860; DOI=10.2310/6650.2006.05068;
RA Agarwal A.K., Zhou X.J., Hall R.K., Nicholls K., Bankier A., Van Esch H.,
RA Fryns J.P., Garg A.;
RT "Focal segmental glomerulosclerosis in patients with mandibuloacral
RT dysplasia owing to ZMPSTE24 deficiency.";
RL J. Invest. Med. 54:208-213(2006).
RN [14]
RP VARIANT MADB LEU-248, AND CHARACTERIZATION OF VARIANT MADB.
RX PubMed=18435794; DOI=10.1111/j.1399-0004.2008.00992.x;
RA Miyoshi Y., Akagi M., Agarwal A.K., Namba N., Kato-Nishimura K., Mohri I.,
RA Yamagata M., Nakajima S., Mushiake S., Shima M., Auchus R.J., Taniike M.,
RA Garg A., Ozono K.;
RT "Severe mandibuloacral dysplasia caused by novel compound heterozygous
RT ZMPSTE24 mutations in two Japanese siblings.";
RL Clin. Genet. 73:535-544(2008).
RN [15]
RP VARIANT MADB LEU-248.
RX PubMed=20814950; DOI=10.1002/ajmg.a.33664;
RA Ahmad Z., Zackai E., Medne L., Garg A.;
RT "Early onset mandibuloacral dysplasia due to compound heterozygous
RT mutations in ZMPSTE24.";
RL Am. J. Med. Genet. A 152:2703-2710(2010).
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated proteins. Acts on lamin A/C.
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;
CC Evidence={ECO:0000269|PubMed:23539603};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23539603};
CC -!- INTERACTION:
CC O75844; P02545-1: LMNA; NbExp=2; IntAct=EBI-1056377, EBI-351949;
CC O75844; P06821: M; Xeno; NbExp=2; IntAct=EBI-1056377, EBI-2547404;
CC O75844; C5E519: M2; Xeno; NbExp=2; IntAct=EBI-1056377, EBI-12562139;
CC O75844; Q20MH8: M2; Xeno; NbExp=2; IntAct=EBI-1056377, EBI-12576433;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23539603}. Nucleus inner membrane
CC {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23539603}.
CC -!- TISSUE SPECIFICITY: Widely expressed. High levels in kidney, prostate,
CC testis and ovary.
CC -!- DOMAIN: The metalloprotease domain is constituted by the two C-terminal
CC nuclear regions.
CC -!- DISEASE: Mandibuloacral dysplasia with type B lipodystrophy (MADB)
CC [MIM:608612]: A form of mandibuloacral dysplasia, a rare progeroid
CC disorder with clinical and genetic heterogeneity, characterized by
CC growth retardation, craniofacial dysmorphic features due to distal bone
CC resorption, musculoskeletal and skin abnormalities associated with
CC lipodystrophy. MADB is a disease characterized by mandibular and
CC clavicular hypoplasia, acroosteolysis, delayed closure of the cranial
CC suture, joint contractures, and generalized lipodystrophy with loss of
CC subcutaneous fat from the extremities, face, neck and trunk.
CC {ECO:0000269|PubMed:12913070, ECO:0000269|PubMed:17152860,
CC ECO:0000269|PubMed:18435794, ECO:0000269|PubMed:20814950}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase M48A family. {ECO:0000305}.
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DR EMBL; AB016068; BAA33727.1; -; mRNA.
DR EMBL; AF064867; AAC68866.1; -; mRNA.
DR EMBL; Y13834; CAB46277.1; -; mRNA.
DR EMBL; AK075007; BAG52049.1; -; mRNA.
DR EMBL; AL050341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07233.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07234.1; -; Genomic_DNA.
DR EMBL; BC037283; AAH37283.1; -; mRNA.
DR CCDS; CCDS449.1; -.
DR RefSeq; NP_005848.2; NM_005857.4.
DR PDB; 2YPT; X-ray; 3.80 A; A/B/D/E=1-475.
DR PDB; 4AW6; X-ray; 3.40 A; A/B/D/E=1-475.
DR PDB; 5SYT; X-ray; 2.00 A; A=1-474.
DR PDB; 6BH8; X-ray; 3.85 A; A/B=1-475.
DR PDBsum; 2YPT; -.
DR PDBsum; 4AW6; -.
DR PDBsum; 5SYT; -.
DR PDBsum; 6BH8; -.
DR AlphaFoldDB; O75844; -.
DR SMR; O75844; -.
DR BioGRID; 115560; 166.
DR DIP; DIP-39641N; -.
DR IntAct; O75844; 34.
DR STRING; 9606.ENSP00000361845; -.
DR ChEMBL; CHEMBL3739253; -.
DR MEROPS; M48.003; -.
DR TCDB; 9.B.1.1.1; the integral membrane caax protease (caax protease) family.
DR iPTMnet; O75844; -.
DR MetOSite; O75844; -.
DR PhosphoSitePlus; O75844; -.
DR SwissPalm; O75844; -.
DR BioMuta; ZMPSTE24; -.
DR EPD; O75844; -.
DR jPOST; O75844; -.
DR MassIVE; O75844; -.
DR MaxQB; O75844; -.
DR PaxDb; O75844; -.
DR PeptideAtlas; O75844; -.
DR PRIDE; O75844; -.
DR ProteomicsDB; 50226; -.
DR Antibodypedia; 1711; 416 antibodies from 31 providers.
DR DNASU; 10269; -.
DR Ensembl; ENST00000372759.4; ENSP00000361845.3; ENSG00000084073.10.
DR GeneID; 10269; -.
DR KEGG; hsa:10269; -.
DR MANE-Select; ENST00000372759.4; ENSP00000361845.3; NM_005857.5; NP_005848.2.
DR UCSC; uc001cfg.5; human.
DR CTD; 10269; -.
DR DisGeNET; 10269; -.
DR GeneCards; ZMPSTE24; -.
DR HGNC; HGNC:12877; ZMPSTE24.
DR HPA; ENSG00000084073; Low tissue specificity.
DR MalaCards; ZMPSTE24; -.
DR MIM; 275210; phenotype.
DR MIM; 606480; gene.
DR MIM; 608612; phenotype.
DR neXtProt; NX_O75844; -.
DR OpenTargets; ENSG00000084073; -.
DR Orphanet; 740; Hutchinson-Gilford progeria syndrome.
DR Orphanet; 90154; Mandibuloacral dysplasia with type B lipodystrophy.
DR Orphanet; 1662; Restrictive dermopathy.
DR PharmGKB; PA37466; -.
DR VEuPathDB; HostDB:ENSG00000084073; -.
DR eggNOG; KOG2719; Eukaryota.
DR GeneTree; ENSGT00390000002053; -.
DR HOGENOM; CLU_025947_3_0_1; -.
DR InParanoid; O75844; -.
DR OMA; LPFKIYK; -.
DR OrthoDB; 878143at2759; -.
DR PhylomeDB; O75844; -.
DR TreeFam; TF105972; -.
DR BRENDA; 3.4.24.84; 2681.
DR PathwayCommons; O75844; -.
DR SignaLink; O75844; -.
DR BioGRID-ORCS; 10269; 24 hits in 1080 CRISPR screens.
DR ChiTaRS; ZMPSTE24; human.
DR GenomeRNAi; 10269; -.
DR Pharos; O75844; Tbio.
DR PRO; PR:O75844; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75844; protein.
DR Bgee; ENSG00000084073; Expressed in hair follicle and 210 other tissues.
DR ExpressionAtlas; O75844; baseline and differential.
DR Genevisible; O75844; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008235; F:metalloexopeptidase activity; TAS:ProtInc.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0071586; P:CAAX-box protein processing; IBA:GO_Central.
DR GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; IEA:Ensembl.
DR GO; GO:0061337; P:cardiac conduction; IEA:Ensembl.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0003231; P:cardiac ventricle development; IEA:Ensembl.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:Ensembl.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR GO; GO:0003417; P:growth plate cartilage development; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:1990164; P:histone H2A phosphorylation; IEA:Ensembl.
DR GO; GO:0043979; P:histone H2B-K5 acetylation; IEA:Ensembl.
DR GO; GO:0044029; P:hypomethylation of CpG island; IEA:Ensembl.
DR GO; GO:0006925; P:inflammatory cell apoptotic process; IEA:Ensembl.
DR GO; GO:0060993; P:kidney morphogenesis; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0043007; P:maintenance of rDNA; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:1903799; P:negative regulation of miRNA maturation; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0006998; P:nuclear envelope organization; IEA:Ensembl.
DR GO; GO:0030327; P:prenylated protein catabolic process; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:2000772; P:regulation of cellular senescence; IEA:Ensembl.
DR GO; GO:0050688; P:regulation of defense response to virus; IDA:MGI.
DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0048145; P:regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR GO; GO:2000618; P:regulation of histone H4-K16 acetylation; IEA:Ensembl.
DR GO; GO:0032350; P:regulation of hormone metabolic process; IEA:Ensembl.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR GO; GO:1903463; P:regulation of mitotic cell cycle DNA replication; IEA:Ensembl.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:1903025; P:regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0070302; P:regulation of stress-activated protein kinase signaling cascade; IEA:Ensembl.
DR GO; GO:2000730; P:regulation of termination of RNA polymerase I transcription; IEA:Ensembl.
DR GO; GO:0032006; P:regulation of TOR signaling; IEA:Ensembl.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR GO; GO:0072423; P:response to DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0003229; P:ventricular cardiac muscle tissue development; IEA:Ensembl.
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 3D-structure; Disease variant; Endoplasmic reticulum; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleus; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..475
FT /note="CAAX prenyl protease 1 homolog"
FT /id="PRO_0000138844"
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 ACT_SITE 336
FT /evidence="ECO:0000269|PubMed:23539603"
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:0000269|PubMed:23539603"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:23539603"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:23539603"
FT VARIANT 137
FT /note="T -> A (in dbSNP:rs17853725)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034711"
FT VARIANT 248
FT /note="P -> L (in MADB; does not affect enzyme activity;
FT dbSNP:rs121908095)"
FT /evidence="ECO:0000269|PubMed:18435794,
FT ECO:0000269|PubMed:20814950"
FT /id="VAR_064501"
FT VARIANT 265
FT /note="N -> S (in MADB; dbSNP:rs281875371)"
FT /evidence="ECO:0000269|PubMed:17152860"
FT /id="VAR_064502"
FT VARIANT 340
FT /note="W -> R (in MADB; dbSNP:rs121908093)"
FT /evidence="ECO:0000269|PubMed:12913070"
FT /id="VAR_019308"
FT CONFLICT 16
FT /note="E -> K (in Ref. 1; BAA33727)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:4AW6"
FT HELIX 15..47
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:5SYT"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 61..94
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 119..147
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 160..191
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 196..218
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:5SYT"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:5SYT"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5SYT"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:4AW6"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:5SYT"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:5SYT"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5SYT"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 326..341
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 344..366
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:5SYT"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:5SYT"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 397..424
FT /evidence="ECO:0007829|PDB:5SYT"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:4AW6"
FT HELIX 428..441
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:5SYT"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:5SYT"
SQ SEQUENCE 475 AA; 54813 MW; 6C49179DEB0C8F7F CRC64;
MGMWASLDAL WEMPAEKRIF GAVLLFSWTV YLWETFLAQR QRRIYKTTTH VPPELGQIMD
SETFEKSRLY QLDKSTFSFW SGLYSETEGT LILLFGGIPY LWRLSGRFCG YAGFGPEYEI
TQSLVFLLLA TLFSALTGLP WSLYNTFVIE EKHGFNQQTL GFFMKDAIKK FVVTQCILLP
VSSLLLYIIK IGGDYFFIYA WLFTLVVSLV LVTIYADYIA PLFDKFTPLP EGKLKEEIEV
MAKSIDFPLT KVYVVEGSKR SSHSNAYFYG FFKNKRIVLF DTLLEEYSVL NKDIQEDSGM
EPRNEEEGNS EEIKAKVKNK KQGCKNEEVL AVLGHELGHW KLGHTVKNII ISQMNSFLCF
FLFAVLIGRK ELFAAFGFYD SQPTLIGLLI IFQFIFSPYN EVLSFCLTVL SRRFEFQADA
FAKKLGKAKD LYSALIKLNK DNLGFPVSDW LFSMWHYSHP PLLERLQALK TMKQH
