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}. 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; 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 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. DR Genevisible; P33435; MM. 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 //