MMP13_HUMAN
ID MMP13_HUMAN Reviewed; 471 AA.
AC P45452; A8K846; B2RCZ3; Q6NWN6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Collagenase 3;
DE EC=3.4.24.-;
DE AltName: Full=Matrix metalloproteinase-13;
DE Short=MMP-13;
DE Flags: Precursor;
GN Name=MMP13;
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], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Mammary carcinoma;
RX PubMed=8207000; DOI=10.1016/s0021-9258(19)89457-7;
RA Freije J.M.P., Diez-Itza I., Balbin M., Sanchez L.M., Blasco R.,
RA Tolivia J., Lopez-Otin C.;
RT "Molecular cloning and expression of collagenase-3, a novel human matrix
RT metalloproteinase produced by breast carcinomas.";
RL J. Biol. Chem. 269:16766-16773(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9562863; DOI=10.1016/s0171-2985(98)80046-6;
RA Willmroth F., Peter H.H., Conca W.;
RT "A matrix metalloproteinase gene expressed in human T lymphocytes is
RT identical with collagenase 3 from breast carcinomas.";
RL Immunobiology 198:375-384(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Esophagus, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-390.
RG NIEHS SNPs program;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP PROTEIN SEQUENCE OF 20-27 AND 104-118, PROPEPTIDE, AUTOCATALYTIC
RP PROCESSING, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-117,
RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND INTERACTION WITH TIMP1;
RP TIMP2 AND TIMP3.
RX PubMed=8576151; DOI=10.1074/jbc.271.3.1544;
RA Knaeuper V., Lopez-Otin C., Smith B., Knight G., Murphy G.;
RT "Biochemical characterization of human collagenase-3.";
RL J. Biol. Chem. 271:1544-1550(1996).
RN [7]
RP PARTIAL PROTEIN SEQUENCE, PROPEPTIDE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8663255; DOI=10.1074/jbc.271.29.17124;
RA Knaeuper V., Will H., Lopez-Otin C., Smith B., Atkinson S.J., Stanton H.,
RA Hembry R.M., Murphy G.;
RT "Cellular mechanisms for human procollagenase-3 (MMP-13) activation.
RT Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to
RT generate active enzyme.";
RL J. Biol. Chem. 271:17124-17131(1996).
RN [8]
RP FUNCTION.
RX PubMed=8603731; DOI=10.1016/0014-5793(95)01539-6;
RA Fosang A.J., Last K., Knaeuper V., Murphy G., Neame P.J.;
RT "Degradation of cartilage aggrecan by collagenase-3 (MMP-13).";
RL FEBS Lett. 380:17-20(1996).
RN [9]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=8798568; DOI=10.1074/jbc.271.38.23577;
RA Borden P., Solymar D., Sucharczuk A., Lindman B., Cannon P., Heller R.A.;
RT "Cytokine control of interstitial collagenase and collagenase-3 gene
RT expression in human chondrocytes.";
RL J. Biol. Chem. 271:23577-23581(1996).
RN [10]
RP TISSUE SPECIFICITY, AND INDUCTION BY TGFB1.
RX PubMed=9056642;
RX DOI=10.1002/(sici)1097-0177(199703)208:3<387::aid-aja9>3.0.co;2-e;
RA Johansson N., Saarialho-Kere U., Airola K., Herva R., Nissinen L.,
RA Westermarck J., Vuorio E., Heino J., Kaehaeri V.M.;
RT "Collagenase-3 (MMP-13) is expressed by hypertrophic chondrocytes,
RT periosteal cells, and osteoblasts during human fetal bone development.";
RL Dev. Dyn. 208:387-397(1997).
RN [11]
RP DOMAIN, CATALYTIC ACTIVITY, AUTOCATALYTIC PROCESSING, FUNCTION, INTERACTION
RP WITH TIMP1; TIMP2 AND TIMP3, AND ACTIVITY REGULATION.
RX PubMed=9065415; DOI=10.1074/jbc.272.12.7608;
RA Knaeuper V., Cowell S., Smith B., Lopez-Otin C., O'Shea M., Morris H.,
RA Zardi L., Murphy G.;
RT "The role of the C-terminal domain of human collagenase-3 (MMP-13) in the
RT activation of procollagenase-3, substrate specificity, and tissue inhibitor
RT of metalloproteinase interaction.";
RL J. Biol. Chem. 272:7608-7616(1997).
RN [12]
RP INVOLVEMENT IN MDST, AND VARIANT MDST GLY-207.
RX PubMed=24648384; DOI=10.1002/ajmg.a.36431;
RA Bonafe L., Liang J., Gorna M.W., Zhang Q., Ha-Vinh R., Campos-Xavier A.B.,
RA Unger S., Beckmann J.S., Le Bechec A., Stevenson B., Giedion A., Liu X.,
RA Superti-Furga G., Wang W., Spahr A., Superti-Furga A.;
RT "MMP13 mutations are the cause of recessive metaphyseal dysplasia, Spahr
RT type.";
RL Am. J. Med. Genet. A 164A:1175-1179(2014).
RN [13]
RP PHOSPHORYLATION AT TYR-366.
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 [14]
RP INVOLVEMENT IN MDST.
RX PubMed=24781753; DOI=10.1038/ejhg.2014.76;
RA Li D., Weber D.R., Deardorff M.A., Hakonarson H., Levine M.A.;
RT "Exome sequencing reveals a nonsense mutation in MMP13 as a new cause of
RT autosomal recessive metaphyseal anadysplasia.";
RL Eur. J. Hum. Genet. 23:264-266(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 265-471 IN COMPLEX WITH CALCIUM,
RP AND DISULFIDE BOND.
RX PubMed=8969305; DOI=10.1006/jmbi.1996.0661;
RA Gomis-Rueth F.-X., Gohlke U., Betz M., Knaeuper V., Murphy G.,
RA Lopez-Otin C., Bode W.;
RT "The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its
RT C-terminal haemopexin-like domain.";
RL J. Mol. Biol. 264:556-566(1996).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 104-271 IN COMPLEXES WITH
RP SYNTHETIC INHIBITORS; CALCIUM AND ZINC, PROPEPTIDE, AND AUTOCATALYTIC
RP PROCESSING.
RX PubMed=10074939; DOI=10.1038/6657;
RA Lovejoy B., Welch A.R., Carr S., Luong C., Broka C., Hendricks R.T.,
RA Campbell J.A., Walker K.A., Martin R., Van Wart H., Browner M.F.;
RT "Crystal structures of MMP-1 and -13 reveal the structural basis for
RT selectivity of collagenase inhibitors.";
RL Nat. Struct. Biol. 6:217-221(1999).
RN [17]
RP STRUCTURE BY NMR OF 104-274 IN COMPLEX WITH CALCIUM AND ZINC.
RX PubMed=10926524; DOI=10.1006/jmbi.2000.3988;
RA Zhang X., Gonnella N.C., Koehn J., Pathak N., Ganu V., Melton R.,
RA Parker D., Hu S.I., Nam K.Y.;
RT "Solution structure of the catalytic domain of human collagenase-3 (MMP-13)
RT complexed to a potent non-peptidic sulfonamide inhibitor: binding
RT comparison with stromelysin-1 and collagenase-1.";
RL J. Mol. Biol. 301:513-524(2000).
RN [18]
RP STRUCTURE BY NMR OF 104-268 IN COMPLEX WITH CALCIUM AND ZINC, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10986126; DOI=10.1006/jmbi.2000.4082;
RA Moy F.J., Chanda P.K., Chen J.M., Cosmi S., Edris W., Levin J.I.,
RA Powers R.;
RT "High-resolution solution structure of the catalytic fragment of human
RT collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor.";
RL J. Mol. Biol. 302:671-689(2000).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 104-271 IN COMPLEX WITH CALCIUM
RP AND ZINC, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=15780611; DOI=10.1016/j.bmcl.2005.02.038;
RA Blagg J.A., Noe M.C., Wolf-Gouveia L.A., Reiter L.A., Laird E.R.,
RA Chang S.P., Danley D.E., Downs J.T., Elliott N.C., Eskra J.D.,
RA Griffiths R.J., Hardink J.R., Haugeto A.I., Jones C.S., Liras J.L.,
RA Lopresti-Morrow L.L., Mitchell P.G., Pandit J., Robinson R.P.,
RA Subramanyam C., Vaughn-Bowser M.L., Yocum S.A.;
RT "Potent pyrimidinetrione-based inhibitors of MMP-13 with enhanced
RT selectivity over MMP-14.";
RL Bioorg. Med. Chem. Lett. 15:1807-1810(2005).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 104-274 IN COMPLEX WITH CALCIUM
RP AND ZINC, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=15734645; DOI=10.1016/j.chembiol.2004.11.014;
RA Engel C.K., Pirard B., Schimanski S., Kirsch R., Habermann J., Klingler O.,
RA Schlotte V., Weithmann K.U., Wendt K.U.;
RT "Structural basis for the highly selective inhibition of MMP-13.";
RL Chem. Biol. 12:181-189(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 104-270 IN COMPLEX WITH CALCIUM
RP AND ZINC, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION IN CARTILAGE
RP DEGRADATION.
RX PubMed=17623656; DOI=10.1074/jbc.m703286200;
RA Johnson A.R., Pavlovsky A.G., Ortwine D.F., Prior F., Man C.F.,
RA Bornemeier D.A., Banotai C.A., Mueller W.T., McConnell P., Yan C.,
RA Baragi V., Lesch C., Roark W.H., Wilson M., Datta K., Guzman R., Han H.K.,
RA Dyer R.D.;
RT "Discovery and characterization of a novel inhibitor of matrix
RT metalloprotease-13 that reduces cartilage damage in vivo without joint
RT fibroplasia side effects.";
RL J. Biol. Chem. 282:27781-27791(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 104-268 IN COMPLEX WITH TIMP2;
RP CALCIUM AND ZINC, AND INTERACTION WITH TIMP2.
RX PubMed=17196980; DOI=10.1016/j.jmb.2006.11.072;
RA Maskos K., Lang R., Tschesche H., Bode W.;
RT "Flexibility and variability of TIMP binding: X-ray structure of the
RT complex between collagenase-3/MMP-13 and TIMP-2.";
RL J. Mol. Biol. 366:1222-1231(2007).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 104-274 IN COMPLEX WITH CALCIUM
RP AND ZINC, CATALYTIC ACTIVITY, COFACTOR, AND FUNCTION.
RX PubMed=19422229; DOI=10.1021/jm801394m;
RA Monovich L.G., Tommasi R.A., Fujimoto R.A., Blancuzzi V., Clark K.,
RA Cornell W.D., Doti R., Doughty J., Fang J., Farley D., Fitt J., Ganu V.,
RA Goldberg R., Goldstein R., Lavoie S., Kulathila R., Macchia W.,
RA Parker D.T., Melton R., O'Byrne E., Pastor G., Pellas T., Quadros E.,
RA Reel N., Roland D.M., Sakane Y., Singh H., Skiles J., Somers J.,
RA Toscano K., Wigg A., Zhou S., Zhu L., Shieh W.C., Xue S., McQuire L.W.;
RT "Discovery of potent, selective, and orally active carboxylic acid based
RT inhibitors of matrix metalloproteinase-13.";
RL J. Med. Chem. 52:3523-3538(2009).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 104-270 IN COMPLEX WITH CALCIUM
RP AND ZINC, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=20005097; DOI=10.1016/j.bmcl.2009.11.081;
RA Schnute M.E., O'Brien P.M., Nahra J., Morris M., Howard Roark W.,
RA Hanau C.E., Ruminski P.G., Scholten J.A., Fletcher T.R., Hamper B.C.,
RA Carroll J.N., Patt W.C., Shieh H.S., Collins B., Pavlovsky A.G.,
RA Palmquist K.E., Aston K.W., Hitchcock J., Rogers M.D., McDonald J.,
RA Johnson A.R., Munie G.E., Wittwer A.J., Man C.F., Settle S.L.,
RA Nemirovskiy O., Vickery L.E., Agawal A., Dyer R.D., Sunyer T.;
RT "Discovery of (pyridin-4-yl)-2H-tetrazole as a novel scaffold to identify
RT highly selective matrix metalloproteinase-13 inhibitors for the treatment
RT of osteoarthritis.";
RL Bioorg. Med. Chem. Lett. 20:576-580(2010).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 104-267 IN COMPLEX WITH CALCIUM
RP AND ZINC, CATALYTIC ACTIVITY, COFACTOR, AND FUNCTION.
RX PubMed=20726512; DOI=10.1021/jm100669j;
RA Becker D.P., Barta T.E., Bedell L.J., Boehm T.L., Bond B.R., Carroll J.,
RA Carron C.P., Decrescenzo G.A., Easton A.M., Freskos J.N.,
RA Funckes-Shippy C.L., Heron M., Hockerman S., Howard C.P., Kiefer J.R.,
RA Li M.H., Mathis K.J., McDonald J.J., Mehta P.P., Munie G.E., Sunyer T.,
RA Swearingen C.A., Villamil C.I., Welsch D., Williams J.M., Yu Y., Yao J.;
RT "Orally active MMP-1 sparing alpha-tetrahydropyranyl and alpha-piperidinyl
RT sulfone matrix metalloproteinase (MMP) inhibitors with efficacy in cancer,
RT arthritis, and cardiovascular disease.";
RL J. Med. Chem. 53:6653-6680(2010).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 104-272 IN COMPLEX WITH CALCIUM
RP AND ZINC, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=22689580; DOI=10.1074/jbc.m112.380782;
RA Devel L., Beau F., Amoura M., Vera L., Cassar-Lajeunesse E., Garcia S.,
RA Czarny B., Stura E.A., Dive V.;
RT "Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of
RT matrix metalloproteases and other metzincins.";
RL J. Biol. Chem. 287:26647-26656(2012).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 103-274 IN COMPLEX WITH CALCIUM
RP AND ZINC, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=23810497; DOI=10.1016/j.bmcl.2013.05.089;
RA De Savi C., Waterson D., Pape A., Lamont S., Hadley E., Mills M.,
RA Page K.M., Bowyer J., Maciewicz R.A.;
RT "Hydantoin based inhibitors of MMP13--discovery of AZD6605.";
RL Bioorg. Med. Chem. Lett. 23:4705-4712(2013).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 104-471 OF MUTANT ALA-223 IN
RP COMPLEX WITH CALCIUM AND ZINC, COFACTOR, DISULFIDE BOND, MUTAGENESIS OF
RP GLU-223, ACTIVE SITE, AND SUBUNIT.
RX PubMed=23913860; DOI=10.1096/fj.13-233601;
RA Stura E.A., Visse R., Cuniasse P., Dive V., Nagase H.;
RT "Crystal structure of full-length human collagenase 3 (MMP-13) with
RT peptides in the active site defines exosites in the catalytic domain.";
RL FASEB J. 27:4395-4405(2013).
RN [29]
RP VARIANT SEMDM SER-75, CHARACTERIZATION OF VARIANT SEMDM SER-75, AND
RP FUNCTION IN BONE DEVELOPMENT.
RX PubMed=16167086; DOI=10.1172/jci22900;
RA Kennedy A.M., Inada M., Krane S.M., Christie P.T., Harding B.,
RA Lopez-Otin C., Sanchez L.M., Pannett A.A.J., Dearlove A., Hartley C.,
RA Byrne M.H., Reed A.A.C., Nesbit M.A., Whyte M.P., Thakker R.V.;
RT "MMP13 mutation causes spondyloepimetaphyseal dysplasia, Missouri type
RT (SEMD(MO).";
RL J. Clin. Invest. 115:2832-2842(2005).
RN [30]
RP VARIANTS MANDP1 SER-74; THR-91 AND ASN-232, AND FUNCTION IN BONE
RP DEVELOPMENT.
RX PubMed=19615667; DOI=10.1016/j.ajhg.2009.06.014;
RA Lausch E., Keppler R., Hilbert K., Cormier-Daire V., Nikkel S.,
RA Nishimura G., Unger S., Spranger J., Superti-Furga A., Zabel B.;
RT "Mutations in MMP9 and MMP13 determine the mode of inheritance and the
RT clinical spectrum of metaphyseal anadysplasia.";
RL Am. J. Hum. Genet. 85:168-178(2009).
CC -!- FUNCTION: Plays a role in the degradation of extracellular matrix
CC proteins including fibrillar collagen, fibronectin, TNC and ACAN.
CC Cleaves triple helical collagens, including type I, type II and type
CC III collagen, but has the highest activity with soluble type II
CC collagen. Can also degrade collagen type IV, type XIV and type X. May
CC also function by activating or degrading key regulatory proteins, such
CC as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling,
CC cartilage degradation, bone development, bone mineralization and
CC ossification. Required for normal embryonic bone development and
CC ossification. Plays a role in the healing of bone fractures via
CC endochondral ossification. Plays a role in wound healing, probably by a
CC mechanism that involves proteolytic activation of TGFB1 and degradation
CC of CCN2. Plays a role in keratinocyte migration during wound healing.
CC May play a role in cell migration and in tumor cell invasion.
CC {ECO:0000269|PubMed:16167086, ECO:0000269|PubMed:17623656,
CC ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:19615667,
CC ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580,
CC ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:8207000,
CC ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:8603731,
CC ECO:0000269|PubMed:8663255, ECO:0000269|PubMed:9065415}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10074939, ECO:0000269|PubMed:10926524,
CC ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
CC ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
CC ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
CC ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
CC ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
CC ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305};
CC Note=Can bind about 5 Ca(2+) ions per subunit.
CC {ECO:0000269|PubMed:10074939, ECO:0000269|PubMed:10926524,
CC ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
CC ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
CC ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
CC ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
CC ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
CC ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10074939, ECO:0000269|PubMed:10926524,
CC ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
CC ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
CC ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
CC ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
CC ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
CC ECO:0000269|PubMed:23913860};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:10074939,
CC ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126,
CC ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611,
CC ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656,
CC ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097,
CC ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580,
CC ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860};
CC -!- ACTIVITY REGULATION: Inhibited by TIMP1, TIMP2 and TIMP3. Inhibited by
CC acetohydroxamic acid and other zinc chelators.
CC {ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:8576151,
CC ECO:0000269|PubMed:9065415}.
CC -!- SUBUNIT: Monomer. Interacts with TIMP1, TIMP2 and TIMP3. Binds (via the
CC C-terminal region) to collagen. {ECO:0000269|PubMed:10926524,
CC ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
CC ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
CC ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
CC ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
CC ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
CC ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8576151,
CC ECO:0000269|PubMed:8969305, ECO:0000269|PubMed:9065415}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305|PubMed:8576151}. Secreted
CC {ECO:0000269|PubMed:8576151}.
CC -!- TISSUE SPECIFICITY: Detected in fetal cartilage and calvaria, in
CC chondrocytes of hypertrophic cartilage in vertebrae and in the dorsal
CC end of ribs undergoing ossification, as well as in osteoblasts and
CC periosteal cells below the inner periosteal region of ossified ribs.
CC Detected in chondrocytes from in joint cartilage that have been treated
CC with TNF and IL1B, but not in untreated chondrocytes. Detected in T
CC lymphocytes. Detected in breast carcinoma tissue.
CC {ECO:0000269|PubMed:8207000, ECO:0000269|PubMed:8798568,
CC ECO:0000269|PubMed:9056642, ECO:0000269|PubMed:9562863}.
CC -!- INDUCTION: Up-regulated by TNF and IL1B. {ECO:0000269|PubMed:8798568,
CC ECO:0000269|PubMed:9056642}.
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 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The C-terminal region binds to collagen.
CC {ECO:0000269|PubMed:9065415}.
CC -!- PTM: The proenzyme is activated by removal of the propeptide; this
CC cleavage can be effected by other matrix metalloproteinases, such as
CC MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage
CC can also be autocatalytic, after partial maturation by another protease
CC or after treatment with 4-aminophenylmercuric acetate (APMA) (in
CC vitro).
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8576151}.
CC -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC {ECO:0000269|PubMed:25171405}.
CC -!- DISEASE: Spondyloepimetaphyseal dysplasia, Missouri type (SEMDM)
CC [MIM:602111]: A bone disease characterized by moderate to severe
CC metaphyseal changes, mild epiphyseal involvement, rhizomelic shortening
CC of the lower limbs with bowing of the femora and/or tibiae, coxa vara,
CC genu varum and pear-shaped vertebrae in childhood. Epimetaphyseal
CC changes improve with age. {ECO:0000269|PubMed:16167086}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Metaphyseal anadysplasia 1 (MANDP1) [MIM:602111]: A bone
CC development disorder characterized by skeletal anomalies that resolve
CC spontaneously with age. Clinical characteristics are evident from the
CC first months of life and include slight shortness of stature and a mild
CC varus deformity of the legs. Patients attain a normal stature in
CC adolescence and show improvement or complete resolution of varus
CC deformity of the legs and rhizomelic micromelia.
CC {ECO:0000269|PubMed:19615667}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Metaphyseal dysplasia, Spahr type (MDST) [MIM:250400]: An
CC autosomal recessive, rare disease characterized by moderate short
CC stature, mild genua vara, and radiographic signs of metaphyseal
CC dysplasia, but no biochemical signs of rickets.
CC {ECO:0000269|PubMed:24648384, ECO:0000269|PubMed:24781753}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mmp13/";
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DR EMBL; X75308; CAA53056.1; -; mRNA.
DR EMBL; X81334; CAA57108.1; -; mRNA.
DR EMBL; AK292211; BAF84900.1; -; mRNA.
DR EMBL; AK315341; BAG37740.1; -; mRNA.
DR EMBL; AY741163; AAU13907.1; -; Genomic_DNA.
DR EMBL; BC067522; AAH67522.1; -; mRNA.
DR EMBL; BC067523; AAH67523.1; -; mRNA.
DR EMBL; BC074807; AAH74807.1; -; mRNA.
DR EMBL; BC074808; AAH74808.1; -; mRNA.
DR CCDS; CCDS8324.1; -.
DR PIR; A53711; A53711.
DR RefSeq; NP_002418.1; NM_002427.3.
DR PDB; 1EUB; NMR; -; A=104-274.
DR PDB; 1FLS; NMR; -; A=104-268.
DR PDB; 1FM1; NMR; -; A=104-268.
DR PDB; 1PEX; X-ray; 2.70 A; A=265-471.
DR PDB; 1XUC; X-ray; 1.70 A; A/B=104-274.
DR PDB; 1XUD; X-ray; 1.80 A; A/B=104-274.
DR PDB; 1XUR; X-ray; 1.85 A; A/B=104-274.
DR PDB; 1YOU; X-ray; 2.30 A; A/B=104-271.
DR PDB; 1ZTQ; X-ray; 2.00 A; A/B/C/D=104-268.
DR PDB; 2D1N; X-ray; 2.37 A; A/B=104-269.
DR PDB; 2E2D; X-ray; 2.00 A; A=104-268.
DR PDB; 2OW9; X-ray; 1.74 A; A/B=104-270.
DR PDB; 2OZR; X-ray; 2.30 A; A/B/C/D/E/F/G/H=104-270.
DR PDB; 2PJT; X-ray; 2.80 A; A/B/C/D=104-268.
DR PDB; 2YIG; X-ray; 1.70 A; A/B=104-274.
DR PDB; 3ELM; X-ray; 1.90 A; A/B=104-274.
DR PDB; 3I7G; X-ray; 1.95 A; A/B=104-274.
DR PDB; 3I7I; X-ray; 2.21 A; A/B=104-274.
DR PDB; 3KEC; X-ray; 2.05 A; A/B=105-267.
DR PDB; 3KEJ; X-ray; 2.30 A; A/B=104-270.
DR PDB; 3KEK; X-ray; 1.97 A; A/B=104-270.
DR PDB; 3KRY; X-ray; 1.90 A; A/B/C/D=104-267.
DR PDB; 3LJZ; X-ray; 2.00 A; A/B/C/D=104-267.
DR PDB; 3O2X; X-ray; 1.90 A; A/B/C/D=105-267.
DR PDB; 3TVC; X-ray; 2.43 A; A=104-272.
DR PDB; 3WV1; X-ray; 1.98 A; A/B=104-274.
DR PDB; 3WV2; X-ray; 2.30 A; A/B=104-274.
DR PDB; 3WV3; X-ray; 1.60 A; A/B=104-274.
DR PDB; 3ZXH; X-ray; 1.30 A; A/B=104-274.
DR PDB; 456C; X-ray; 2.40 A; A/B=104-271.
DR PDB; 4A7B; X-ray; 2.20 A; A/B=104-272.
DR PDB; 4FU4; X-ray; 2.85 A; A/B=104-471, C/D=25-50.
DR PDB; 4FVL; X-ray; 2.44 A; A/B=104-471, C/D=31-50.
DR PDB; 4G0D; X-ray; 2.54 A; A/B/C/D=104-471, W/X/Y/Z=25-50.
DR PDB; 4JP4; X-ray; 1.43 A; A/B=103-274.
DR PDB; 4JPA; X-ray; 2.00 A; A/B=103-274.
DR PDB; 4L19; X-ray; 1.66 A; A/B=104-274.
DR PDB; 5B5O; X-ray; 1.20 A; A/B=103-274.
DR PDB; 5B5P; X-ray; 1.60 A; A/B=103-274.
DR PDB; 5BOT; X-ray; 1.85 A; A/B=104-274.
DR PDB; 5BOY; X-ray; 2.03 A; A/B=104-274.
DR PDB; 5BPA; X-ray; 1.79 A; A/B=104-274.
DR PDB; 5UWK; X-ray; 1.60 A; A/B=104-274.
DR PDB; 5UWL; X-ray; 2.55 A; A/B=104-274.
DR PDB; 5UWM; X-ray; 1.62 A; A/B=104-274.
DR PDB; 5UWN; X-ray; 3.20 A; A/B/C/D/E=104-274.
DR PDB; 7JU8; X-ray; 2.00 A; A/B=104-274.
DR PDB; 830C; X-ray; 1.60 A; A/B=104-271.
DR PDBsum; 1EUB; -.
DR PDBsum; 1FLS; -.
DR PDBsum; 1FM1; -.
DR PDBsum; 1PEX; -.
DR PDBsum; 1XUC; -.
DR PDBsum; 1XUD; -.
DR PDBsum; 1XUR; -.
DR PDBsum; 1YOU; -.
DR PDBsum; 1ZTQ; -.
DR PDBsum; 2D1N; -.
DR PDBsum; 2E2D; -.
DR PDBsum; 2OW9; -.
DR PDBsum; 2OZR; -.
DR PDBsum; 2PJT; -.
DR PDBsum; 2YIG; -.
DR PDBsum; 3ELM; -.
DR PDBsum; 3I7G; -.
DR PDBsum; 3I7I; -.
DR PDBsum; 3KEC; -.
DR PDBsum; 3KEJ; -.
DR PDBsum; 3KEK; -.
DR PDBsum; 3KRY; -.
DR PDBsum; 3LJZ; -.
DR PDBsum; 3O2X; -.
DR PDBsum; 3TVC; -.
DR PDBsum; 3WV1; -.
DR PDBsum; 3WV2; -.
DR PDBsum; 3WV3; -.
DR PDBsum; 3ZXH; -.
DR PDBsum; 456C; -.
DR PDBsum; 4A7B; -.
DR PDBsum; 4FU4; -.
DR PDBsum; 4FVL; -.
DR PDBsum; 4G0D; -.
DR PDBsum; 4JP4; -.
DR PDBsum; 4JPA; -.
DR PDBsum; 4L19; -.
DR PDBsum; 5B5O; -.
DR PDBsum; 5B5P; -.
DR PDBsum; 5BOT; -.
DR PDBsum; 5BOY; -.
DR PDBsum; 5BPA; -.
DR PDBsum; 5UWK; -.
DR PDBsum; 5UWL; -.
DR PDBsum; 5UWM; -.
DR PDBsum; 5UWN; -.
DR PDBsum; 7JU8; -.
DR PDBsum; 830C; -.
DR AlphaFoldDB; P45452; -.
DR BMRB; P45452; -.
DR SMR; P45452; -.
DR BioGRID; 110465; 27.
DR STRING; 9606.ENSP00000260302; -.
DR BindingDB; P45452; -.
DR ChEMBL; CHEMBL280; -.
DR DrugBank; DB02049; 2-{4-[4-(4-Chloro-Phenoxy)-Benzenesulfonyl]-Tetrahydro-Pyran-4-Yl}-N-Hydroxy-Acetamide.
DR DrugBank; DB01996; 3-Methylpyridine.
DR DrugBank; DB03033; 4-methoxybenzenesulfinate.
DR DrugBank; DB07827; 4-{[1-METHYL-2,4-DIOXO-6-(3-PHENYLPROP-1-YN-1-YL)-1,4-DIHYDROQUINAZOLIN-3(2H)-YL]METHYL}BENZOIC ACID.
DR DrugBank; DB08388; 5-(2-ETHOXYETHYL)-5-[4-(4-FLUOROPHENOXY)PHENOXY]PYRIMIDINE-2,4,6(1H,3H,5H)-TRIONE.
DR DrugBank; DB08561; BENZYL 6-BENZYL-5,7-DIOXO-6,7-DIHYDRO-5H-[1,3]THIAZOLO[3,2-C]PYRIMIDINE-2-CARBOXYLATE.
DR DrugBank; DB08490; CTS-1027.
DR DrugBank; DB06423; Endostatin.
DR DrugBank; DB02697; Hydroxyaminovaline.
DR DrugBank; DB00786; Marimastat.
DR DrugBank; DB04759; PYRIMIDINE-4,6-DICARBOXYLIC ACID BIS-(3-METHYL-BENZYLAMIDE).
DR DrugBank; DB04760; PYRIMIDINE-4,6-DICARBOXYLIC ACID BIS-(4-FLUORO-3-METHYL-BENZYLAMIDE).
DR DrugBank; DB04761; PYRIMIDINE-4,6-DICARBOXYLIC ACID BIS-[(PYRIDIN-3-YLMETHYL)-AMIDE].
DR DrugBank; DB07013; TERT-BUTYL 4-({[4-(BUT-2-YN-1-YLAMINO)PHENYL]SULFONYL}METHYL)-4-[(HYDROXYAMINO)CARBONYL]PIPERIDINE-1-CARBOXYLATE.
DR DrugBank; DB02071; WAY-151693.
DR DrugCentral; P45452; -.
DR GuidetoPHARMACOLOGY; 1637; -.
DR MEROPS; M10.013; -.
DR GlyGen; P45452; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P45452; -.
DR PhosphoSitePlus; P45452; -.
DR BioMuta; MMP13; -.
DR DMDM; 1168998; -.
DR MassIVE; P45452; -.
DR PaxDb; P45452; -.
DR PeptideAtlas; P45452; -.
DR PRIDE; P45452; -.
DR ProteomicsDB; 55677; -.
DR Antibodypedia; 18066; 1082 antibodies from 40 providers.
DR DNASU; 4322; -.
DR Ensembl; ENST00000260302.8; ENSP00000260302.3; ENSG00000137745.13.
DR GeneID; 4322; -.
DR KEGG; hsa:4322; -.
DR MANE-Select; ENST00000260302.8; ENSP00000260302.3; NM_002427.4; NP_002418.1.
DR UCSC; uc001phl.4; human.
DR CTD; 4322; -.
DR DisGeNET; 4322; -.
DR GeneCards; MMP13; -.
DR HGNC; HGNC:7159; MMP13.
DR HPA; ENSG00000137745; Tissue enriched (urinary).
DR MalaCards; MMP13; -.
DR MIM; 250400; phenotype.
DR MIM; 600108; gene.
DR MIM; 602111; phenotype.
DR neXtProt; NX_P45452; -.
DR OpenTargets; ENSG00000137745; -.
DR Orphanet; 1040; Metaphyseal anadysplasia.
DR Orphanet; 2501; Metaphyseal chondrodysplasia, Spahr type.
DR Orphanet; 93356; Spondyloepimetaphyseal dysplasia, Missouri type.
DR PharmGKB; PA30871; -.
DR VEuPathDB; HostDB:ENSG00000137745; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000157450; -.
DR InParanoid; P45452; -.
DR OMA; RVMPTNS; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P45452; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.17; 2681.
DR BRENDA; 3.4.24.35; 2681.
DR BRENDA; 3.4.24.65; 2681.
DR BRENDA; 3.4.24.B4; 2681.
DR PathwayCommons; P45452; -.
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-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-8941332; RUNX2 regulates genes involved in cell migration.
DR SignaLink; P45452; -.
DR SIGNOR; P45452; -.
DR BioGRID-ORCS; 4322; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; MMP13; human.
DR EvolutionaryTrace; P45452; -.
DR GeneWiki; Matrix_metallopeptidase_13; -.
DR GenomeRNAi; 4322; -.
DR Pharos; P45452; Tchem.
DR PRO; PR:P45452; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P45452; protein.
DR Bgee; ENSG00000137745; Expressed in periodontal ligament and 43 other tissues.
DR ExpressionAtlas; P45452; baseline and differential.
DR Genevisible; P45452; HS.
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; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0060349; P:bone morphogenesis; IDA:UniProtKB.
DR GO; GO:0030574; P:collagen catabolic process; IDA:UniProtKB.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0003417; P:growth plate cartilage development; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:1904645; P:response to amyloid-beta; TAS:ARUK-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; IPR028711; Collagenase_3.
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:SF165; PTHR10201:SF165; 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; 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; Calcium; Collagen degradation; Direct protein sequencing;
KW Disease variant; Disulfide bond; Dwarfism; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8576151"
FT PROPEP 20..103
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8576151"
FT /id="PRO_0000028788"
FT CHAIN 104..471
FT /note="Collagenase 3"
FT /id="PRO_0000028789"
FT REPEAT 281..330
FT /note="Hemopexin 1"
FT REPEAT 331..377
FT /note="Hemopexin 2"
FT REPEAT 379..427
FT /note="Hemopexin 3"
FT REPEAT 428..471
FT /note="Hemopexin 4"
FT REGION 176..246
FT /note="Interaction with TIMP2"
FT REGION 263..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..471
FT /note="Interaction with collagen"
FT MOTIF 94..101
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /evidence="ECO:0000305|PubMed:23913860"
FT BINDING 96
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:0000250"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
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:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:10926524,
FT ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
FT ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
FT ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
FT ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
FT ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
FT ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305"
FT MOD_RES 366
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000303|PubMed:25171405"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8576151"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 284..471
FT /evidence="ECO:0000269|PubMed:23913860,
FT ECO:0000269|PubMed:8969305"
FT VARIANT 2
FT /note="H -> L (in dbSNP:rs554797)"
FT /id="VAR_011971"
FT VARIANT 74
FT /note="F -> S (in MANDP1; dbSNP:rs121909498)"
FT /evidence="ECO:0000269|PubMed:19615667"
FT /id="VAR_063432"
FT VARIANT 75
FT /note="F -> S (in SEMDM; abnormal intracellular
FT autoactivation and autodegradation within the ER/Golgi
FT resulting in the secretion of small and inactive fragments;
FT dbSNP:rs121909497)"
FT /evidence="ECO:0000269|PubMed:16167086"
FT /id="VAR_032753"
FT VARIANT 91
FT /note="M -> T (in MANDP1; dbSNP:rs121909499)"
FT /evidence="ECO:0000269|PubMed:19615667"
FT /id="VAR_063433"
FT VARIANT 207
FT /note="W -> G (in MDST; dbSNP:rs140059558)"
FT /evidence="ECO:0000269|PubMed:24648384"
FT /id="VAR_073418"
FT VARIANT 232
FT /note="H -> N (in MANDP1; dbSNP:rs121909500)"
FT /evidence="ECO:0000269|PubMed:19615667"
FT /id="VAR_063434"
FT VARIANT 390
FT /note="D -> G (in dbSNP:rs17860568)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020534"
FT MUTAGEN 223
FT /note="E->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:23913860"
FT CONFLICT 147
FT /note="D -> G (in Ref. 3; BAF84900)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="P -> L (in Ref. 5; AAH67523)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="N -> D (in Ref. 3; BAG37740)"
FT /evidence="ECO:0000305"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:4FVL"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:4G0D"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3ZXH"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3I7I"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3O2X"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:5B5O"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:5B5O"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1EUB"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3KRY"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:5B5O"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1PEX"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:4FVL"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:4FVL"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:4FVL"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:4FVL"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:4FVL"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:4FVL"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 448..453
FT /evidence="ECO:0007829|PDB:4FVL"
FT TURN 454..457
FT /evidence="ECO:0007829|PDB:4FVL"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:4FVL"
FT HELIX 465..469
FT /evidence="ECO:0007829|PDB:4FVL"
SQ SEQUENCE 471 AA; 53820 MW; E110F50628B57B60 CRC64;
MHPGVLAAFL FLSWTHCRAL PLPSGGDEDD LSEEDLQFAE RYLRSYYHPT NLAGILKENA
ASSMTERLRE MQSFFGLEVT GKLDDNTLDV MKKPRCGVPD VGEYNVFPRT LKWSKMNLTY
RIVNYTPDMT HSEVEKAFKK AFKVWSDVTP LNFTRLHDGI ADIMISFGIK EHGDFYPFDG
PSGLLAHAFP PGPNYGGDAH FDDDETWTSS SKGYNLFLVA AHEFGHSLGL DHSKDPGALM
FPIYTYTGKS HFMLPDDDVQ GIQSLYGPGD EDPNPKHPKT PDKCDPSLSL DAITSLRGET
MIFKDRFFWR LHPQQVDAEL FLTKSFWPEL PNRIDAAYEH PSHDLIFIFR GRKFWALNGY
DILEGYPKKI SELGLPKEVK KISAAVHFED TGKTLLFSGN QVWRYDDTNH IMDKDYPRLI
EEDFPGIGDK VDAVYEKNGY IYFFNGPIQF EYSIWSNRIV RVMPANSILW C
