FURIN_MOUSE
ID FURIN_MOUSE Reviewed; 793 AA.
AC P23188; Q6GTN6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Furin;
DE EC=3.4.21.75 {ECO:0000269|PubMed:18713856};
DE AltName: Full=Dibasic-processing enzyme;
DE AltName: Full=Paired basic amino acid residue-cleaving enzyme;
DE Short=PACE;
DE AltName: Full=Prohormone convertase 3;
DE Flags: Precursor;
GN Name=Furin; Synonyms=Fur, Pcsk3;
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], AND TISSUE SPECIFICITY.
RX PubMed=2266110; DOI=10.1016/s0021-9258(18)45669-4;
RA Hatsuzawa K., Hosaka M., Nakagawa T., Nagase M., Shoda A., Murakami K.,
RA Nakayama K.;
RT "Structure and expression of mouse furin, a yeast Kex2-related protease.
RT Lack of processing of coexpressed prorenin in GH4C1 cells.";
RL J. Biol. Chem. 265:22075-22078(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Creemers J.W.M., Roebroek A.J.M., van den Ouweland A.M.W.,
RA van Duijnhoven H.L.P., van de Ven W.J.M.;
RT "Cloning and functional expression of a 4.3 kbp mouse fur cDNA: evidence
RT for differential expression.";
RL Life Sci. Adv. (Mol. Biol.) 11:127-138(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
RP INTERACTION WITH FLNA.
RX PubMed=9412467; DOI=10.1083/jcb.139.7.1719;
RA Liu G., Thomas L., Warren R.A., Enns C.A., Cunningham C.C., Hartwig J.H.,
RA Thomas G.;
RT "Cytoskeletal protein ABP-280 directs the intracellular trafficking of
RT furin and modulates proprotein processing in the endocytic pathway.";
RL J. Cell Biol. 139:1719-1733(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18713856; DOI=10.1073/pnas.0800340105;
RA Louagie E., Taylor N.A., Flamez D., Roebroek A.J., Bright N.A.,
RA Meulemans S., Quintens R., Herrera P.L., Schuit F., Van de Ven W.J.,
RA Creemers J.W.;
RT "Role of furin in granular acidification in the endocrine pancreas:
RT identification of the V-ATPase subunit Ac45 as a candidate substrate.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12319-12324(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 108-578 IN COMPLEX WITH CALCIUM
RP AND INHIBITOR, GLYCOSYLATION AT ASN-387 AND ASN-440, AND DISULFIDE BONDS.
RX PubMed=12794637; DOI=10.1038/nsb941;
RA Henrich S., Cameron A., Bourenkov G.P., Kiefersauer R., Huber R.,
RA Lindberg I., Bode W., Than M.E.;
RT "The crystal structure of the proprotein processing proteinase furin
RT explains its stringent specificity.";
RL Nat. Struct. Biol. 10:520-526(2003).
CC -!- FUNCTION: Ubiquitous endoprotease within constitutive secretory
CC pathways capable of cleavage at the RX(K/R)R consensus motif
CC (PubMed:18713856). Mediates processing of TGFB1, an essential step in
CC TGF-beta-1 activation (By similarity). Converts through proteolytic
CC cleavage the non-functional Brain natriuretic factor prohormone into
CC its active hormone BNP(1-45) (By similarity). By mediating processing
CC of accessory subunit ATP6AP1/Ac45 of the V-ATPase, regulates the
CC acidification of dense-core secretory granules in islets of Langerhans
CC cells (PubMed:18713856). {ECO:0000250|UniProtKB:P09958,
CC ECO:0000269|PubMed:18713856}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of mature proteins from their proproteins by cleavage
CC of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and
CC Yaa is Arg or Lys. Releases albumin, complement component C3 and von
CC Willebrand factor from their respective precursors.; EC=3.4.21.75;
CC Evidence={ECO:0000269|PubMed:18713856};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12794637};
CC Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958};
CC -!- ACTIVITY REGULATION: Inhibited by the not secondly cleaved propeptide.
CC Inhibited by m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-
CC benzamidine (m-guanidinomethyl-Phac-RVR-Amb) and 4-guanidinomethyl-
CC phenylacetyl-Arg-Tle-Arg-4-amidinobenzylamide (MI-1148). Inhibited by
CC Decanoyl-Arg-Val-Lys-Arg-chloromethylketone (decanoyl-RVKR-CMK).
CC Inhibited by heparin/heparan sulfate-binding.
CC {ECO:0000250|UniProtKB:P09958}.
CC -!- SUBUNIT: Interacts with FLNA (PubMed:9412467). Binds to PACS1 which
CC mediates TGN localization and connection to clathrin adapters (By
CC similarity). {ECO:0000250|UniProtKB:P09958,
CC ECO:0000269|PubMed:9412467}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P09958}; Single-
CC pass type I membrane protein {ECO:0000305}. Secreted
CC {ECO:0000250|UniProtKB:Q28193}. Endosome membrane
CC {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Shuttles between the trans-Golgi network and the
CC cell surface. Propeptide cleavage is a prerequisite for exit of furin
CC molecules out of the endoplasmic reticulum (ER). A second cleavage
CC within the propeptide occurs in the trans Golgi network (TGN), followed
CC by the release of the propeptide and the activation of furin.
CC {ECO:0000250|UniProtKB:P09958}.
CC -!- TISSUE SPECIFICITY: Seems to be expressed ubiquitously
CC (PubMed:2266110). Expressed in islets of Langerhans (PubMed:18713856).
CC {ECO:0000269|PubMed:18713856, ECO:0000269|PubMed:2266110}.
CC -!- DOMAIN: Contains a cytoplasmic domain responsible for its TGN
CC localization and recycling from the cell surface.
CC {ECO:0000250|UniProtKB:P09958}.
CC -!- PTM: The inhibition peptide, which plays the role of an intramolecular
CC chaperone, is autocatalytically removed in the endoplasmic reticulum
CC (ER) and remains non-covalently bound to furin as a potent
CC autoinhibitor. Following transport to the trans Golgi, a second
CC cleavage within the inhibition propeptide results in propeptide
CC dissociation and furin activation. {ECO:0000250|UniProtKB:P09958}.
CC -!- PTM: Phosphorylation is required for TGN localization of the
CC endoprotease. In vivo, exists as di-, mono- and non-phosphorylated
CC forms. {ECO:0000250|UniProtKB:P09958}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in pancreas causes mild
CC glucose intolerance (PubMed:18713856). Insulin secretion by islets of
CC Langerhans cells is reduced (PubMed:18713856). In islets of Langerhans
CC cells, processing of pro-proteins including Pcsk2, Ins2/proinsulin II
CC and Gcg/proglucagon and acidification of dense-core secretory granules
CC are reduced (PubMed:18713856). Islets of Langerhans are normal
CC (PubMed:18713856). {ECO:0000269|PubMed:18713856}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
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DR EMBL; X54056; CAA37988.1; -; mRNA.
DR EMBL; L26489; AAA37643.1; -; mRNA.
DR EMBL; CH466543; EDL06988.1; -; Genomic_DNA.
DR EMBL; BC048234; AAH48234.1; -; mRNA.
DR CCDS; CCDS21397.1; -.
DR PIR; A23679; KXMSF.
DR RefSeq; NP_001074923.1; NM_001081454.2.
DR RefSeq; NP_035176.1; NM_011046.3.
DR PDB; 1P8J; X-ray; 2.60 A; A/B/C/D/E/F/G/H=108-578.
DR PDBsum; 1P8J; -.
DR AlphaFoldDB; P23188; -.
DR SMR; P23188; -.
DR BioGRID; 202059; 4.
DR ELM; P23188; -.
DR STRING; 10090.ENSMUSP00000113370; -.
DR MEROPS; S08.071; -.
DR GlyGen; P23188; 2 sites.
DR iPTMnet; P23188; -.
DR PhosphoSitePlus; P23188; -.
DR SwissPalm; P23188; -.
DR EPD; P23188; -.
DR MaxQB; P23188; -.
DR PaxDb; P23188; -.
DR PeptideAtlas; P23188; -.
DR PRIDE; P23188; -.
DR ProteomicsDB; 271646; -.
DR Antibodypedia; 4013; 453 antibodies from 39 providers.
DR DNASU; 18550; -.
DR Ensembl; ENSMUST00000107362; ENSMUSP00000102985; ENSMUSG00000030530.
DR Ensembl; ENSMUST00000120753; ENSMUSP00000113793; ENSMUSG00000030530.
DR Ensembl; ENSMUST00000122232; ENSMUSP00000113370; ENSMUSG00000030530.
DR GeneID; 18550; -.
DR KEGG; mmu:18550; -.
DR UCSC; uc009iau.1; mouse.
DR CTD; 5045; -.
DR MGI; MGI:97513; Furin.
DR VEuPathDB; HostDB:ENSMUSG00000030530; -.
DR eggNOG; KOG3525; Eukaryota.
DR GeneTree; ENSGT00940000157220; -.
DR HOGENOM; CLU_002976_4_0_1; -.
DR InParanoid; P23188; -.
DR OMA; CLGEPTH; -.
DR OrthoDB; 473018at2759; -.
DR PhylomeDB; P23188; -.
DR TreeFam; TF314277; -.
DR BRENDA; 3.4.21.75; 3474.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR Reactome; R-MMU-167060; NGF processing.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-1912420; Pre-NOTCH Processing in Golgi.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
DR BioGRID-ORCS; 18550; 10 hits in 78 CRISPR screens.
DR ChiTaRS; Furin; mouse.
DR EvolutionaryTrace; P23188; -.
DR PRO; PR:P23188; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P23188; protein.
DR Bgee; ENSMUSG00000030530; Expressed in epithelium of stomach and 227 other tissues.
DR ExpressionAtlas; P23188; baseline and differential.
DR Genevisible; P23188; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005769; C:early endosome; TAS:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0031985; C:Golgi cisterna; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:MGI.
DR GO; GO:0012510; C:trans-Golgi network transport vesicle membrane; TAS:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:1904399; F:heparan sulfate binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048406; F:nerve growth factor binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0001825; P:blastocyst formation; IGI:CACAO.
DR GO; GO:0090472; P:dibasic protein processing; ISO:MGI.
DR GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; ISO:MGI.
DR GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; ISO:MGI.
DR GO; GO:0032902; P:nerve growth factor production; ISO:MGI.
DR GO; GO:0043043; P:peptide biosynthetic process; ISO:MGI.
DR GO; GO:0016486; P:peptide hormone processing; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:1901394; P:positive regulation of transforming growth factor beta1 activation; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:MGI.
DR GO; GO:0032374; P:regulation of cholesterol transport; IMP:MGI.
DR GO; GO:0052548; P:regulation of endopeptidase activity; ISO:MGI.
DR GO; GO:0042176; P:regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; IDA:MGI.
DR GO; GO:0032940; P:secretion by cell; ISO:MGI.
DR GO; GO:0006465; P:signal peptide processing; ISO:MGI.
DR GO; GO:0019058; P:viral life cycle; IEA:Ensembl.
DR GO; GO:0031638; P:zymogen activation; ISO:MGI.
DR GO; GO:0097341; P:zymogen inhibition; ISO:MGI.
DR CDD; cd00064; FU; 2.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00261; FU; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Calcium; Cell membrane;
KW Cleavage on pair of basic residues; Disulfide bond; Endosome; Glycoprotein;
KW Golgi apparatus; Heparin-binding; Hydrolase; Membrane; Metal-binding;
KW Phosphoprotein; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal; Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..107
FT /note="Inhibition peptide"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT /id="PRO_0000027030"
FT CHAIN 108..793
FT /note="Furin"
FT /id="PRO_0000027031"
FT TOPO_DOM 108..714
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 121..435
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 444..576
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REPEAT 577..620
FT /note="FU 1"
FT /evidence="ECO:0000255"
FT REPEAT 638..681
FT /note="FU 2"
FT /evidence="ECO:0000255"
FT REGION 160..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..761
FT /note="Cell surface signal"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT REGION 766..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 498..500
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00293"
FT MOTIF 772..778
FT /note="Trans Golgi network signal"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT COMPBIAS 673..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 368
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 191..192
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 253..258
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 292..295
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT SITE 75..76
FT /note="Cleavage, second; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT SITE 107..108
FT /note="Cleavage, first; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12794637,
FT ECO:0007744|PDB:1P8J"
FT DISULFID 211..360
FT /evidence="ECO:0000269|PubMed:12794637"
FT DISULFID 303..333
FT /evidence="ECO:0000269|PubMed:12794637"
FT DISULFID 450..474
FT /evidence="ECO:0000269|PubMed:12794637"
FT CONFLICT 746
FT /note="V -> M (in Ref. 1; CAA37988)"
FT /evidence="ECO:0000305"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1P8J"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1P8J"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1P8J"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1P8J"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:1P8J"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1P8J"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:1P8J"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 367..384
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1P8J"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 431..438
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 448..455
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 482..496
FT /evidence="ECO:0007829|PDB:1P8J"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 528..535
FT /evidence="ECO:0007829|PDB:1P8J"
FT TURN 537..540
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 545..553
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:1P8J"
FT STRAND 561..573
FT /evidence="ECO:0007829|PDB:1P8J"
SQ SEQUENCE 793 AA; 86772 MW; 0F120C2DE2E1A431 CRC64;
MELRSWLLWV VAAAGAVVLL AADAQGQKIF TNTWAVHIPG GPAVADRVAQ KHGFHNLGQI
FGDYYHFWHR AVTKRSLSPH RPRHSRLQRE PQVKWLEQQV AKRRAKRDVY QEPTDPKFPQ
QWYLSGVTQR DLNVKEAWAQ GFTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP
DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL
GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH
DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC
TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNADD WATNGVGRKV
SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IVEILVEPKD IGKRLEVRKA VTACLGEPNH
ITRLEHVQAR LTLSYNRRGD LAIHLISPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD
EDPAGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLST PPESSGCKTL TSSQACVVCE
EGYSLHQKSC VQHCPPGFIP QVLDTHYSTE NDVEIIRASV CTPCHASCAT CQGPAPTDCL
SCPSHASLDP VEQTCSRQSQ SSRESRPQQQ PPALRPEVEM EPRLQAGLAS HLPEVLAGLS
CLIIVLIFGI VFLFLHRCSG FSFRGVKVYT MDRGLISYKG LPPEAWQEEC PSDSEEDEGR
GERTAFIKDQ SAL
