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 27-MAR-2024, entry version 242. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 23. 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 GlyCosmos; P03956; 2 sites, 48 glycans. 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; 9606-ENSP00000322788; -. DR PeptideAtlas; P03956; -. DR ProteomicsDB; 51623; -. DR Antibodypedia; 18022; 1252 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 AGR; HGNC:7155; -. 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; LHGYPKD; -. DR OrthoDB; 391167at2759; -. 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 1168 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 127 other cell types or tissues. DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. 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:0019538; P:protein metabolic process; TAS:Reactome. DR GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL. DR CDD; cd00094; HX; 1. DR CDD; cd04278; ZnMc_MMP; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR Gene3D; 2.110.10.10; Hemopexin-like domain; 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 PANTHER; PTHR10201:SF151; INTERSTITIAL COLLAGENASE; 1. DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1. 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; SSF50923; Hemopexin-like domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF47090; PGBD-like; 1. DR PROSITE; PS00546; CYSTEINE_SWITCH; 1. DR PROSITE; PS00024; HEMOPEXIN; 1. DR PROSITE; PS51642; HEMOPEXIN_2; 4. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR Genevisible; P03956; HS. 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 //