MMP1_HUMAN
ID MMP1_HUMAN Reviewed; 469 AA.
AC P03956; P08156;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 3.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Interstitial collagenase;
DE EC=3.4.24.7 {ECO:0000269|PubMed:1645757, ECO:0000269|PubMed:16807369, ECO:0000269|PubMed:2153297, ECO:0000269|PubMed:2557822};
DE AltName: Full=Fibroblast collagenase;
DE AltName: Full=Matrix metalloproteinase-1;
DE Short=MMP-1;
DE Contains:
DE RecName: Full=22 kDa interstitial collagenase;
DE Contains:
DE RecName: Full=27 kDa interstitial collagenase;
DE Flags: Precursor;
GN Name=MMP1; Synonyms=CLG;
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], AND SUBCELLULAR LOCATION.
RX PubMed=2167156;
RA Templeton N.S., Brown P.D., Levy A.T., Margulies I.M.K., Liotta L.A.,
RA Stetler-Stevenson W.G.;
RT "Cloning and characterization of human tumor cell interstitial
RT collagenase.";
RL Cancer Res. 50:5431-5437(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3030290; DOI=10.1042/bj2400913;
RA Whitham S.E., Murphy G., Angel P., Rahmsdorf H.J., Smith B., Lyons A.,
RA Harris T.J.R., Reynolds J.J., Herrlich P., Docherty A.J.P.;
RT "Comparison of human stromelysin and collagenase by cloning and sequence
RT analysis.";
RL Biochem. J. 240:913-916(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3009463; DOI=10.1016/s0021-9258(19)84605-7;
RA Goldberg G.I., Wilhelm S.M., Kronberger A., Bauer E.A., Grant G.A.,
RA Eisen A.Z.;
RT "Human fibroblast collagenase. Complete primary structure and homology to
RT an oncogene transformation-induced rat protein.";
RL J. Biol. Chem. 261:6600-6605(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lin D., Duncan M., Allen E., Araujo R., Aparicio A., Chai A., Chung E.,
RA Davis K., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O.,
RA Lashkari D., Lew H., Namath A., Oefner P., Roberts D., Heller R.,
RA Davis R.W.;
RT "Three matrix metalloproteinases on 81kb of P1 insert.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-191; GLN-405 AND
RP THR-406.
RG NIEHS SNPs program;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
RX PubMed=3037355; DOI=10.1128/mcb.7.6.2256-2266.1987;
RA Angel P., Baumann I., Stein B., Delius H., Rahmsdorf H.J., Herrlich P.;
RT "12-O-tetradecanoyl-phorbol-13-acetate induction of the human collagenase
RT gene is mediated by an inducible enhancer element located in the 5'-
RT flanking region.";
RL Mol. Cell. Biol. 7:2256-2266(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-70.
RC TISSUE=Synovial cell;
RX PubMed=3027129; DOI=10.1172/jci112845;
RA Brinckerhoff C.E., Ruby P.L., Austin S.D., Fini M.E., White H.D.;
RT "Molecular cloning of human synovial cell collagenase and selection of a
RT single gene from genomic DNA.";
RL J. Clin. Invest. 79:542-546(1987).
RN [10]
RP PROTEIN SEQUENCE OF 100-112 AND 270-287, AND CATALYTIC ACTIVITY.
RC TISSUE=Fibroblast;
RX PubMed=2557822; DOI=10.1042/bj2630201;
RA Clark I.M., Cawston T.E.;
RT "Fragments of human fibroblast collagenase. Purification and
RT characterization.";
RL Biochem. J. 263:201-206(1989).
RN [11]
RP SIMILARITY TO THERMOLYSIN TYPE PROTEASES.
RX PubMed=3032950; DOI=10.1016/s0021-9258(18)45517-2;
RA McKerrow J.H.;
RT "Human fibroblast collagenase contains an amino acid sequence homologous to
RT the zinc-binding site of Serratia protease.";
RL J. Biol. Chem. 262:5943-5943(1987).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=2153297; DOI=10.1073/pnas.87.1.364;
RA Springman E.B., Angleton E.L., Birkedal-Hansen H., Van Wart H.E.;
RT "Multiple modes of activation of latent human fibroblast collagenase:
RT evidence for the role of a Cys73 active-site zinc complex in latency and a
RT 'cysteine switch' mechanism for activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:364-368(1990).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1645757; DOI=10.1172/jci115262;
RA Desrochers P.E., Jeffrey J.J., Weiss S.J.;
RT "Interstitial collagenase (matrix metalloproteinase-1) expresses serpinase
RT activity.";
RL J. Clin. Invest. 87:2258-2265(1991).
RN [14]
RP GLYCOSYLATION AT ASN-120.
RX PubMed=10092871; DOI=10.1046/j.1432-1327.1999.00105.x;
RA Saarinen J., Welgus H.G., Flizar C.A., Kalkkinen N., Helin J.;
RT "N-glycan structures of matrix metalloproteinase-1 derived from human
RT fibroblasts and from HT-1080 fibrosarcoma cells.";
RL Eur. J. Biochem. 259:829-840(1999).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH HIV-1 TAT (MICROBIAL
RP INFECTION).
RX PubMed=16807369; DOI=10.1096/fj.05-5619fje;
RA Rumbaugh J., Turchan-Cholewo J., Galey D., St Hillaire C., Anderson C.,
RA Conant K., Nath A.;
RT "Interaction of HIV Tat and matrix metalloproteinase in HIV
RT neuropathogenesis: a new host defense mechanism.";
RL FASEB J. 20:1736-1738(2006).
RN [16]
RP PHOSPHORYLATION AT SER-57; THR-274 AND TYR-360, AND MUTAGENESIS OF TYR-360.
RX PubMed=25171405; DOI=10.1016/j.cell.2014.06.048;
RA Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr.,
RA Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M.,
RA Dixon J.E., Yeo C.Y., Whitman M.;
RT "A secreted tyrosine kinase acts in the extracellular environment.";
RL Cell 158:1033-1044(2014).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 101-269 IN COMPLEX WITH CALCIUM
RP AND ZINC.
RX PubMed=7656013; DOI=10.1038/nsb0294-106;
RA Borkakoti N., Winkler F.K., Williams D.H., D'Arcy A., Broadhurst M.J.,
RA Brown P.A., Johnson W.H., Murray E.J.;
RT "Structure of the catalytic domain of human fibroblast collagenase
RT complexed with an inhibitor.";
RL Nat. Struct. Biol. 1:106-110(1994).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 102-269 IN COMPLEX WITH CALCIUM
RP AND ZINC.
RX PubMed=8031754; DOI=10.1021/bi00193a006;
RA Lovejoy B., Hassell A.M., Luther M.A., Weigl D., Jordan S.R.;
RT "Crystal structures of recombinant 19-kDa human fibroblast collagenase
RT complexed to itself.";
RL Biochemistry 33:8207-8217(1994).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 101-269 IN COMPLEX WITH CALCIUM
RP AND ZINC.
RX PubMed=8278810; DOI=10.1126/science.8278810;
RA Lovejoy B., Cleasby A., Hassell A.M., Longley K., Luther M.A., Weigl D.,
RA McGeehan G., McElroy A.B., Drewry D., Lambert M.H., Jordan S.R.;
RT "Structure of the catalytic domain of fibroblast collagenase complexed with
RT an inhibitor.";
RL Science 263:375-377(1994).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 101-269 IN COMPLEX WITH CALCIUM
RP AND ZINC.
RX PubMed=8090713; DOI=10.1002/prot.340190203;
RA Spurlino J.C., Smallwood A.M., Carlton D.D., Banks T.M., Vavra K.J.,
RA Johnson J.S., Cook E.R., Falvo J., Wahl R.C., Pulvino T.A., Et A.L.;
RT "1.56-A structure of mature truncated human fibroblast collagenase.";
RL Proteins 19:98-109(1994).
RN [21]
RP STRUCTURE BY NMR OF 101-269 IN COMPLEX WITH CALCIUM AND ZINC.
RX PubMed=9484219; DOI=10.1021/bi972181w;
RA Moy F.J., Chanda P.K., Cosmi S., Pisano M.R., Urbano C., Wilhelm J.,
RA Powers R.;
RT "High-resolution solution structure of the inhibitor-free catalytic
RT fragment of human fibroblast collagenase determined by multidimensional
RT NMR.";
RL Biochemistry 37:1495-1504(1998).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-469 IN COMPLEX WITH CALCIUM
RP AND ZINC, AND DOMAIN.
RX PubMed=15611040; DOI=10.1074/jbc.m411084200;
RA Jozic D., Bourenkov G., Lim N.H., Visse R., Nagase H., Bode W., Maskos K.;
RT "X-ray structure of human proMMP-1: new insights into procollagenase
RT activation and collagen binding.";
RL J. Biol. Chem. 280:9578-9585(2005).
CC -!- FUNCTION: Cleaves collagens of types I, II, and III at one site in the
CC helical domain. Also cleaves collagens of types VII and X
CC (PubMed:2557822, PubMed:2153297, PubMed:1645757). In case of HIV
CC infection, interacts and cleaves the secreted viral Tat protein,
CC leading to a decrease in neuronal Tat's mediated neurotoxicity
CC (PubMed:16807369). {ECO:0000269|PubMed:1645757,
CC ECO:0000269|PubMed:16807369, ECO:0000269|PubMed:2153297,
CC ECO:0000269|PubMed:2557822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of the triple helix of collagen at about three-
CC quarters of the length of the molecule from the N-terminus, at 775-
CC Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates
CC and alpha-macroglobulins at bonds where P1' is a hydrophobic
CC residue.; EC=3.4.24.7; Evidence={ECO:0000269|PubMed:1645757,
CC ECO:0000269|PubMed:16807369, ECO:0000269|PubMed:2153297,
CC ECO:0000269|PubMed:2557822};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
CC ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
CC ECO:0000269|PubMed:9484219};
CC Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000269|PubMed:7656013,
CC ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713,
CC ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
CC ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
CC ECO:0000269|PubMed:9484219};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:7656013,
CC ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713,
CC ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219};
CC -!- ACTIVITY REGULATION: Can be activated without removal of the activation
CC peptide.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
CC {ECO:0000269|PubMed:16807369}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305|PubMed:2167156}.
CC -!- DOMAIN: There are two distinct domains in this protein; the catalytic
CC N-terminal, and the C-terminal which is involved in substrate
CC specificity and in binding TIMP (tissue inhibitor of
CC metalloproteinases).
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme. {ECO:0000269|PubMed:15611040,
CC ECO:0000269|PubMed:2153297}.
CC -!- PTM: Undergoes autolytic cleavage to two major forms (22 kDa and 27
CC kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa
CC form. The 27 kDa form has no activity while the 22/25 kDa form can act
CC as activator for collagenase. {ECO:0000269|PubMed:10092871}.
CC -!- PTM: Tyrosine phosphorylated in platelets by PKDCC/VLK.
CC {ECO:0000269|PubMed:25171405}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mmp1/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Collagenase entry;
CC URL="https://en.wikipedia.org/wiki/Collagenase";
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DR EMBL; X54925; CAA38691.1; -; mRNA.
DR EMBL; X05231; CAA28858.1; -; mRNA.
DR EMBL; M13509; AAA35699.1; -; mRNA.
DR EMBL; U78045; AAB36941.1; -; Genomic_DNA.
DR EMBL; BT006874; AAP35520.1; -; mRNA.
DR EMBL; AY769434; AAV28732.1; -; Genomic_DNA.
DR EMBL; BC013875; AAH13875.1; -; mRNA.
DR EMBL; M16567; AAA52033.1; -; Genomic_DNA.
DR EMBL; M15996; AAA35700.1; -; mRNA.
DR CCDS; CCDS8322.1; -.
DR PIR; A37308; KCHUI.
DR RefSeq; NP_002412.1; NM_002421.3.
DR PDB; 1AYK; NMR; -; A=101-269.
DR PDB; 1CGE; X-ray; 1.90 A; A=102-269.
DR PDB; 1CGF; X-ray; 2.10 A; A/B=102-263.
DR PDB; 1CGL; X-ray; 2.40 A; A/B=101-269.
DR PDB; 1HFC; X-ray; 1.50 A; A=101-269.
DR PDB; 1SU3; X-ray; 2.20 A; A/B=20-469.
DR PDB; 2AYK; NMR; -; A=101-269.
DR PDB; 2CLT; X-ray; 2.67 A; A/B=100-466.
DR PDB; 2J0T; X-ray; 2.54 A; A/B/C=101-269.
DR PDB; 2TCL; X-ray; 2.20 A; A=101-269.
DR PDB; 3AYK; NMR; -; A=101-269.
DR PDB; 3SHI; X-ray; 2.20 A; A/G/M=106-261.
DR PDB; 4AUO; X-ray; 3.00 A; A/B=100-466.
DR PDB; 4AYK; NMR; -; A=101-269.
DR PDB; 966C; X-ray; 1.90 A; A=108-264.
DR PDBsum; 1AYK; -.
DR PDBsum; 1CGE; -.
DR PDBsum; 1CGF; -.
DR PDBsum; 1CGL; -.
DR PDBsum; 1HFC; -.
DR PDBsum; 1SU3; -.
DR PDBsum; 2AYK; -.
DR PDBsum; 2CLT; -.
DR PDBsum; 2J0T; -.
DR PDBsum; 2TCL; -.
DR PDBsum; 3AYK; -.
DR PDBsum; 3SHI; -.
DR PDBsum; 4AUO; -.
DR PDBsum; 4AYK; -.
DR PDBsum; 966C; -.
DR AlphaFoldDB; P03956; -.
DR BMRB; P03956; -.
DR SASBDB; P03956; -.
DR SMR; P03956; -.
DR BioGRID; 110456; 10.
DR DIP; DIP-529N; -.
DR IntAct; P03956; 3.
DR MINT; P03956; -.
DR STRING; 9606.ENSP00000322788; -.
DR BindingDB; P03956; -.
DR ChEMBL; CHEMBL332; -.
DR DrugBank; DB08482; [[1-[N-HYDROXY-ACETAMIDYL]-3-METHYL-BUTYL]-CARBONYL-LEUCINYL]-ALANINE ETHYL ESTER.
DR DrugBank; DB07556; CGS-27023.
DR DrugBank; DB00786; Marimastat.
DR DrugBank; DB08403; METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC ACID.
DR DrugBank; DB07926; N-[3-(N'-HYDROXYCARBOXAMIDO)-2-(2-METHYLPROPYL)-PROPANOYL]-O-TYROSINE-N-METHYLAMIDE.
DR DrugBank; DB08491; N-HYDROXY-2-[4-(4-PHENOXY-BENZENESULFONYL)-TETRAHYDRO-PYRAN-4-YL]-ACETAMIDE.
DR DrugCentral; P03956; -.
DR GuidetoPHARMACOLOGY; 1628; -.
DR MEROPS; M10.001; -.
DR GlyConnect; 301; 25 N-Linked glycans (2 sites).
DR GlyGen; P03956; 3 sites, 48 N-linked glycans (3 sites).
DR iPTMnet; P03956; -.
DR PhosphoSitePlus; P03956; -.
DR BioMuta; MMP1; -.
DR DMDM; 116852; -.
DR jPOST; P03956; -.
DR MassIVE; P03956; -.
DR PaxDb; P03956; -.
DR PeptideAtlas; P03956; -.
DR PRIDE; P03956; -.
DR ProteomicsDB; 51623; -.
DR Antibodypedia; 18022; 1129 antibodies from 46 providers.
DR DNASU; 4312; -.
DR Ensembl; ENST00000315274.7; ENSP00000322788.6; ENSG00000196611.6.
DR GeneID; 4312; -.
DR KEGG; hsa:4312; -.
DR MANE-Select; ENST00000315274.7; ENSP00000322788.6; NM_002421.4; NP_002412.1.
DR UCSC; uc001phi.3; human.
DR CTD; 4312; -.
DR DisGeNET; 4312; -.
DR GeneCards; MMP1; -.
DR HGNC; HGNC:7155; MMP1.
DR HPA; ENSG00000196611; Tissue enhanced (gallbladder, stomach, urinary bladder).
DR MalaCards; MMP1; -.
DR MIM; 120353; gene.
DR neXtProt; NX_P03956; -.
DR OpenTargets; ENSG00000196611; -.
DR Orphanet; 79408; Autosomal recessive generalized dystrophic epidermolysis bullosa, severe form.
DR PharmGKB; PA30867; -.
DR VEuPathDB; HostDB:ENSG00000196611; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000154907; -.
DR HOGENOM; CLU_015489_6_0_1; -.
DR InParanoid; P03956; -.
DR OMA; FRNYNLY; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P03956; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.7; 2681.
DR PathwayCommons; P03956; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; P03956; -.
DR SIGNOR; P03956; -.
DR BioGRID-ORCS; 4312; 9 hits in 1084 CRISPR screens.
DR ChiTaRS; MMP1; human.
DR EvolutionaryTrace; P03956; -.
DR GeneWiki; MMP1; -.
DR GenomeRNAi; 4312; -.
DR Pharos; P03956; Tchem.
DR PRO; PR:P03956; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P03956; protein.
DR Bgee; ENSG00000196611; Expressed in epithelial cell of pancreas and 126 other tissues.
DR Genevisible; P03956; HS.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0004175; F:endopeptidase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0071492; P:cellular response to UV-A; IDA:UniProtKB.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR021158; Pept_M10A_Zn_BS.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Calcium; Collagen degradation;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Host-virus interaction; Hydrolase; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT PROPEP 20..99
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2557822"
FT /id="PRO_0000028703"
FT CHAIN 100..469
FT /note="Interstitial collagenase"
FT /id="PRO_0000028704"
FT CHAIN 100..269
FT /note="22 kDa interstitial collagenase"
FT /id="PRO_0000028705"
FT CHAIN 270..469
FT /note="27 kDa interstitial collagenase"
FT /id="PRO_0000028706"
FT REPEAT 275..324
FT /note="Hemopexin 1"
FT REPEAT 325..371
FT /note="Hemopexin 2"
FT REPEAT 374..422
FT /note="Hemopexin 3"
FT REPEAT 423..466
FT /note="Hemopexin 4"
FT REGION 98..276
FT /note="Metalloprotease"
FT MOTIF 90..97
FT /note="Cysteine switch"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:2153297"
FT ACT_SITE 219
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0007744|PDB:1SU3"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:8031754,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:2J0T, ECO:0007744|PDB:3SHI,
FT ECO:0007744|PDB:966C"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:2J0T, ECO:0007744|PDB:2TCL,
FT ECO:0007744|PDB:4AUO, ECO:0007744|PDB:966C"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3AYK,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:4AYK, ECO:0007744|PDB:966C"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1CGE,
FT ECO:0007744|PDB:1CGF, ECO:0007744|PDB:1CGL,
FT ECO:0007744|PDB:1HFC, ECO:0007744|PDB:1SU3,
FT ECO:0007744|PDB:2AYK, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:2J0T, ECO:0007744|PDB:2TCL,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:966C"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:2J0T, ECO:0007744|PDB:2TCL,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:966C"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3SHI,
FT ECO:0007744|PDB:4AUO, ECO:0007744|PDB:4AYK,
FT ECO:0007744|PDB:966C"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3SHI,
FT ECO:0007744|PDB:4AUO, ECO:0007744|PDB:966C"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3SHI,
FT ECO:0007744|PDB:4AUO, ECO:0007744|PDB:966C"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3AYK,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:4AYK, ECO:0007744|PDB:966C"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:2J0T, ECO:0007744|PDB:2TCL,
FT ECO:0007744|PDB:4AUO, ECO:0007744|PDB:966C"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:7656013,
FT ECO:0000269|PubMed:8031754, ECO:0007744|PDB:1CGE,
FT ECO:0007744|PDB:1CGF, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:2J0T, ECO:0007744|PDB:2TCL,
FT ECO:0007744|PDB:4AUO, ECO:0007744|PDB:966C"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:2J0T, ECO:0007744|PDB:2TCL,
FT ECO:0007744|PDB:4AUO, ECO:0007744|PDB:966C"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3AYK,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:4AYK, ECO:0007744|PDB:966C"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:2J0T, ECO:0007744|PDB:2TCL,
FT ECO:0007744|PDB:3AYK, ECO:0007744|PDB:3SHI,
FT ECO:0007744|PDB:4AUO, ECO:0007744|PDB:4AYK,
FT ECO:0007744|PDB:966C"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:8031754, ECO:0007744|PDB:1CGE,
FT ECO:0007744|PDB:1CGF, ECO:0007744|PDB:1SU3,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:966C"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3AYK,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:966C"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3AYK,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:4AYK, ECO:0007744|PDB:966C"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3AYK,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:4AYK, ECO:0007744|PDB:966C"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754,
FT ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810,
FT ECO:0000269|PubMed:9484219, ECO:0007744|PDB:1AYK,
FT ECO:0007744|PDB:1CGE, ECO:0007744|PDB:1CGF,
FT ECO:0007744|PDB:1CGL, ECO:0007744|PDB:1HFC,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2AYK,
FT ECO:0007744|PDB:2CLT, ECO:0007744|PDB:2J0T,
FT ECO:0007744|PDB:2TCL, ECO:0007744|PDB:3AYK,
FT ECO:0007744|PDB:3SHI, ECO:0007744|PDB:4AUO,
FT ECO:0007744|PDB:4AYK, ECO:0007744|PDB:966C"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:4AUO"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:4AUO"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:4AUO"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15611040,
FT ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT,
FT ECO:0007744|PDB:4AUO"
FT SITE 143
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:10092871"
FT SITE 269..270
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:2557822"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25171405"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25171405"
FT MOD_RES 360
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000269|PubMed:25171405"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10092871"
FT /id="CAR_000105"
FT DISULFID 278..466
FT /evidence="ECO:0000250"
FT VARIANT 29
FT /note="Q -> P (in dbSNP:rs554499)"
FT /id="VAR_011969"
FT VARIANT 191
FT /note="I -> V (in dbSNP:rs17879973)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_021024"
FT VARIANT 252
FT /note="D -> G (in dbSNP:rs513964)"
FT /id="VAR_011970"
FT VARIANT 262
FT /note="R -> S (in dbSNP:rs12282811)"
FT /id="VAR_054005"
FT VARIANT 405
FT /note="R -> Q (in dbSNP:rs17879165)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_021025"
FT VARIANT 406
FT /note="S -> T (in dbSNP:rs17884120)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_021026"
FT MUTAGEN 360
FT /note="Y->F: Partial reduction of tyrosine phosphorylation
FT in the presence of PKDCC/VLK."
FT /evidence="ECO:0000269|PubMed:25171405"
FT CONFLICT 43
FT /note="N -> K (in Ref. 9; AAA35700)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="Missing (in Ref. 9; AAA35700)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="T -> R (in Ref. 3; AAA35699)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="D -> H (in Ref. 2; CAA28858)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="R -> T (in Ref. 2; CAA28858)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="I -> T (in Ref. 2; CAA28858)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="G -> S (in Ref. 3; AAA35699)"
FT /evidence="ECO:0000305"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:1SU3"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:1SU3"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1AYK"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:3SHI"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2J0T"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1HFC"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1HFC"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:966C"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:1HFC"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1SU3"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:1SU3"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:1SU3"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:1SU3"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:1SU3"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:1SU3"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:1SU3"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:1SU3"
FT STRAND 453..459
FT /evidence="ECO:0007829|PDB:1SU3"
FT TURN 460..463
FT /evidence="ECO:0007829|PDB:1SU3"
SQ SEQUENCE 469 AA; 54007 MW; 4B1361DCF4C54B20 CRC64;
MHSFPPLLLL LFWGVVSHSF PATLETQEQD VDLVQKYLEK YYNLKNDGRQ VEKRRNSGPV
VEKLKQMQEF FGLKVTGKPD AETLKVMKQP RCGVPDVAQF VLTEGNPRWE QTHLTYRIEN
YTPDLPRADV DHAIEKAFQL WSNVTPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN
LAHAFQPGPG IGGDAHFDED ERWTNNFREY NLHRVAAHEL GHSLGLSHST DIGALMYPSY
TFSGDVQLAQ DDIDGIQAIY GRSQNPVQPI GPQTPKACDS KLTFDAITTI RGEVMFFKDR
FYMRTNPFYP EVELNFISVF WPQLPNGLEA AYEFADRDEV RFFKGNKYWA VQGQNVLHGY
PKDIYSSFGF PRTVKHIDAA LSEENTGKTY FFVANKYWRY DEYKRSMDPG YPKMIAHDFP
GIGHKVDAVF MKDGFFYFFH GTRQYKFDPK TKRILTLQKA NSWFNCRKN
