ID MMP13_MOUSE Reviewed; 472 AA.
AC P33435;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 24-JAN-2024, entry version 193.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 105-119 AND 266-275.
RC STRAIN=NMRI; TISSUE=Calvaria;
RX PubMed=1383028; DOI=10.1016/0014-5793(92)81323-e;
RA Henriet P., Rousseau G.G., Eeckhout Y.;
RT "Cloning and sequencing of mouse collagenase cDNA. Divergence of mouse and
RT rat collagenases from the other mammalian collagenases.";
RL FEBS Lett. 310:175-178(1992).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=15539485; DOI=10.1242/dev.01461;
RA Stickens D., Behonick D.J., Ortega N., Heyer B., Hartenstein B., Yu Y.,
RA Fosang A.J., Schorpp-Kistner M., Angel P., Werb Z.;
RT "Altered endochondral bone development in matrix metalloproteinase 13-
RT deficient mice.";
RL Development 131:5883-5895(2004).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15563592; DOI=10.1073/pnas.0407788101;
RA Inada M., Wang Y., Byrne M.H., Rahman M.U., Miyaura C., Lopez-Otin C.,
RA Krane S.M.;
RT "Critical roles for collagenase-3 (Mmp13) in development of growth plate
RT cartilage and in endochondral ossification.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17192-17197(2004).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17987127; DOI=10.1371/journal.pone.0001150;
RA Behonick D.J., Xing Z., Lieu S., Buckley J.M., Lotz J.C., Marcucio R.S.,
RA Werb Z., Miclau T., Colnot C.;
RT "Role of matrix metalloproteinase 13 in both endochondral and
RT intramembranous ossification during skeletal regeneration.";
RL PLoS ONE 2:E1150-E1150(2007).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19590036; DOI=10.2353/ajpath.2009.081080;
RA Hattori N., Mochizuki S., Kishi K., Nakajima T., Takaishi H.,
RA D'Armiento J., Okada Y.;
RT "MMP-13 plays a role in keratinocyte migration, angiogenesis, and
RT contraction in mouse skin wound healing.";
RL Am. J. Pathol. 175:533-546(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22880047; DOI=10.1371/journal.pone.0042596;
RA Toriseva M., Laato M., Carpen O., Ruohonen S.T., Savontaus E., Inada M.,
RA Krane S.M., Kahari V.M.;
RT "MMP-13 regulates growth of wound granulation tissue and modulates gene
RT expression signatures involved in inflammation, proteolysis, and cell
RT viability.";
RL PLoS ONE 7:E42596-E42596(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 105-268 IN COMPLEX WITH ZINC AND
RP CALCIUM IONS, AND COFACTOR.
RX PubMed=10525409; DOI=10.1006/jmbi.1999.3068;
RA Botos I., Meyer E., Swanson S.M., Lemaitre V., Eeckhout Y., Meyer E.F.;
RT "Structure of recombinant mouse collagenase-3 (MMP-13).";
RL J. Mol. Biol. 292:837-844(1999).
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:15539485, ECO:0000269|PubMed:15563592,
CC ECO:0000269|PubMed:17987127, ECO:0000269|PubMed:19590036,
CC ECO:0000269|PubMed:22880047}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10525409};
CC Note=Can bind about 5 Ca(2+) ions per subunit.
CC {ECO:0000269|PubMed:10525409};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10525409};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:10525409};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}. Secreted.
CC -!- TISSUE SPECIFICITY: Detected in epidermal cells and stromal fibroblasts
CC in wounded skin, but not in normal skin (at protein level). Detected in
CC embryonic hypertrophic chondrocytes and newly recruited bone cells at
CC primary ossification centers. After adult bone fracture, detected in
CC periosteum and in chondrocytes in the cartilage. Detected in immature
CC and mature osteoblasts in the fracture callus. Detected in calvaria
CC from neonates. Detected in wounded skin, but not in normal skin.
CC {ECO:0000269|PubMed:15563592, ECO:0000269|PubMed:17987127,
CC ECO:0000269|PubMed:19590036}.
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. {ECO:0000250}.
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 vitro)
CC (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC {ECO:0000250|UniProtKB:P45452}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are born at the
CC expected Mendelian rate, are fertile and have a normal life span.
CC Mutant embryos show a delay in the development of the primary
CC ossification centers. Besides, they display an increased length of the
CC growth plates of the long bones from the hind limbs (PubMed:15563592).
CC Three week old mutant mice display an increased trabecular bone volume
CC due to an increase in the length of the hypertrophic chondrocyte zone
CC of the growth plate. This phenotype persists during several months
CC (PubMed:15563592, PubMed:15539485), but one year old mutant mice
CC display no longer any difference relative to wild-type
CC (PubMed:15539485). After bone fractures, mutant mice show delays in
CC carticage remodeling and resorption, as well as an increased volume of
CC spongy bone mass. In addition, mutant mice show delayed healing of
CC cutaneous wounds that is most evident three to seven days after
CC wounding. The delay in wound healing and in re-epithelialization is
CC exacerbated in mice lacking both Mmp13 and Mmp9.
CC {ECO:0000269|PubMed:15539485, ECO:0000269|PubMed:15563592,
CC ECO:0000269|PubMed:17987127, ECO:0000269|PubMed:19590036,
CC ECO:0000269|PubMed:22880047}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; X66473; CAA47102.1; -; mRNA.
DR CCDS; CCDS22803.1; -.
DR PIR; S29243; S29243.
DR RefSeq; NP_032633.1; NM_008607.2.
DR PDB; 1CXV; X-ray; 2.00 A; A/B=105-268.
DR PDBsum; 1CXV; -.
DR AlphaFoldDB; P33435; -.
DR SMR; P33435; -.
DR STRING; 10090.ENSMUSP00000015394; -.
DR BindingDB; P33435; -.
DR ChEMBL; CHEMBL3638350; -.
DR MEROPS; M10.013; -.
DR GlyCosmos; P33435; 3 sites, No reported glycans.
DR GlyGen; P33435; 3 sites.
DR PhosphoSitePlus; P33435; -.
DR PaxDb; 10090-ENSMUSP00000015394; -.
DR ProteomicsDB; 291474; -.
DR Antibodypedia; 18066; 1203 antibodies from 40 providers.
DR DNASU; 17386; -.
DR Ensembl; ENSMUST00000015394.10; ENSMUSP00000015394.9; ENSMUSG00000050578.11.
DR GeneID; 17386; -.
DR KEGG; mmu:17386; -.
DR UCSC; uc009ocg.2; mouse.
DR AGR; MGI:1340026; -.
DR CTD; 4322; -.
DR MGI; MGI:1340026; Mmp13.
DR VEuPathDB; HostDB:ENSMUSG00000050578; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000157450; -.
DR HOGENOM; CLU_015489_6_0_1; -.
DR InParanoid; P33435; -.
DR OMA; MEAGYPR; -.
DR OrthoDB; 391167at2759; -.
DR PhylomeDB; P33435; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.B4; 3474.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR BioGRID-ORCS; 17386; 1 hit in 80 CRISPR screens.
DR ChiTaRS; Mmp13; mouse.
DR EvolutionaryTrace; P33435; -.
DR PRO; PR:P33435; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P33435; Protein.
DR Bgee; ENSMUSG00000050578; Expressed in diaphysis of femur and 102 other cell types or tissues.
DR ExpressionAtlas; P33435; baseline and differential.
DR Genevisible; P33435; MM.
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; ISO:MGI.
DR GO; GO:0046581; C:intercellular canaliculus; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0030282; P:bone mineralization; IMP:UniProtKB.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0030574; P:collagen catabolic process; IDA:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:UniProtKB.
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; IGI:MGI.
DR GO; GO:0007507; P:heart development; ISO:MGI.
DR GO; GO:1904244; P:positive regulation of pancreatic trypsinogen secretion; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0019538; P:protein metabolic process; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0009725; P:response to hormone; ISO:MGI.
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:SF165; COLLAGENASE 3; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Collagen degradation; Direct protein sequencing;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..104
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1383028"
FT /id="PRO_0000028790"
FT CHAIN 105..472
FT /note="Collagenase 3"
FT /id="PRO_0000028791"
FT REPEAT 282..331
FT /note="Hemopexin 1"
FT REPEAT 332..378
FT /note="Hemopexin 2"
FT REPEAT 380..428
FT /note="Hemopexin 3"
FT REPEAT 429..472
FT /note="Hemopexin 4"
FT REGION 177..247
FT /note="Interaction with TIMP2"
FT /evidence="ECO:0000250"
FT REGION 269..472
FT /note="Interaction with collagen"
FT /evidence="ECO:0000250"
FT MOTIF 95..102
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 224
FT BINDING 97
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 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10525409"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10525409"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10525409"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10525409"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10525409"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10525409"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10525409"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT MOD_RES 367
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000250|UniProtKB:P45452"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 285..472
FT /evidence="ECO:0000250"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1CXV"
FT HELIX 132..147
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1CXV"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:1CXV"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:1CXV"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1CXV"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:1CXV"
SQ SEQUENCE 472 AA; 54182 MW; 67F437B89B4D0DBD CRC64;
MHSAILATFF LLSWTPCWSL PLPYGDDDDD DLSEEDLVFA EHYLKSYYHP ATLAGILKKS
TVTSTVDRLR EMQSFFGLEV TGKLDDPTLD IMRKPRCGVP DVGEYNVFPR TLKWSQTNLT
YRIVNYTPDM SHSEVEKAFR KAFKVWSDVT PLNFTRIYDG TADIMISFGT KEHGDFYPFD
GPSGLLAHAF PPGPNYGGDA HFDDDETWTS SSKGYNLFIV AAHELGHSLG LDHSKDPGAL
MFPIYTYTGK SHFMLPDDDV QGIQFLYGPG DEDPNPKHPK TPEKCDPALS LDAITSLRGE
TMIFKDRFFW RLHPQQVEAE LFLTKSFWPE LPNHVDAAYE HPSRDLMFIF RGRKFWALNG
YDILEGYPRK ISDLGFPKEV KRLSAAVHFE NTGKTLFFSE NHVWSYDDVN QTMDKDYPRL
IEEEFPGIGN KVDAVYEKNG YIYFFNGPIQ FEYSIWSNRI VRVMPTNSIL WC
//
