MMP9_RAT
ID MMP9_RAT Reviewed; 708 AA.
AC P50282;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Matrix metalloproteinase-9;
DE Short=MMP-9;
DE EC=3.4.24.35 {ECO:0000250|UniProtKB:P14780};
DE AltName: Full=92 kDa gelatinase;
DE AltName: Full=92 kDa type IV collagenase;
DE AltName: Full=Gelatinase B;
DE Short=GELB;
DE Flags: Precursor;
GN Name=Mmp9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=7590350; DOI=10.1016/0378-1119(95)00447-e;
RA Okada A., Santavicca M., Basset P.;
RT "The cDNA cloning and expression of the gene encoding rat gelatinase B.";
RL Gene 164:317-321(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344;
RX PubMed=8605986; DOI=10.1016/0014-5793(96)00185-8;
RA Xia Y., Garcia G., Chen S., Wilson C.B., Feng L.;
RT "Cloning of rat 92-kDa type IV collagenase and expression of an active
RT recombinant catalytic domain.";
RL FEBS Lett. 382:285-288(1996).
CC -!- FUNCTION: Matrix metalloproteinase that plays an essential role in
CC local proteolysis of the extracellular matrix and in leukocyte
CC migration (By similarity). Could play a role in bone osteoclastic
CC resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By
CC similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By
CC similarity). Cleaves type IV and type V collagen into large C-terminal
CC three quarter fragments and shorter N-terminal one quarter fragments.
CC Degrades fibronectin but not laminin or Pz-peptide (By similarity).
CC {ECO:0000250|UniProtKB:P14780, ECO:0000250|UniProtKB:P41245}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of gelatin types I and V and collagen types IV and
CC V.; EC=3.4.24.35; Evidence={ECO:0000250|UniProtKB:P14780};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P14780};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P14780};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780};
CC -!- SUBUNIT: Exists as monomer or homodimer; disulfide-linked. Exists also
CC as heterodimer with LCN2. Macrophages and transformed cell lines
CC produce only the monomeric form. Interacts with ECM1.
CC {ECO:0000250|UniProtKB:P14780}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P14780}.
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:0000250|UniProtKB:P14780}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P14780}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; U24441; AAA90911.1; -; mRNA.
DR EMBL; U36476; AAB01721.1; -; mRNA.
DR PIR; JC4364; JC4364.
DR PIR; S62907; S62907.
DR RefSeq; NP_112317.1; NM_031055.1.
DR AlphaFoldDB; P50282; -.
DR SMR; P50282; -.
DR STRING; 10116.ENSRNOP00000023965; -.
DR BindingDB; P50282; -.
DR ChEMBL; CHEMBL3870; -.
DR MEROPS; M10.004; -.
DR GlyGen; P50282; 2 sites.
DR PaxDb; P50282; -.
DR PRIDE; P50282; -.
DR ABCD; P50282; 2 sequenced antibodies.
DR GeneID; 81687; -.
DR KEGG; rno:81687; -.
DR CTD; 4318; -.
DR RGD; 621320; Mmp9.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; P50282; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P50282; -.
DR BRENDA; 3.4.24.35; 5301.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-1442490; Collagen degradation.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P50282; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
DR GO; GO:0001968; F:fibronectin binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:RGD.
DR GO; GO:0008233; F:peptidase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:RGD.
DR GO; GO:0071460; P:cellular response to cell-matrix adhesion; IMP:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071283; P:cellular response to iron(III) ion; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEP:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0071492; P:cellular response to UV-A; ISO:RGD.
DR GO; GO:0030574; P:collagen catabolic process; IDA:RGD.
DR GO; GO:0007566; P:embryo implantation; ISO:RGD.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0007507; P:heart development; IDA:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0050900; P:leukocyte migration; IEA:InterPro.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001258; P:negative regulation of cation channel activity; ISO:RGD.
DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2000697; P:negative regulation of epithelial cell differentiation involved in kidney development; ISO:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:RGD.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEP:RGD.
DR GO; GO:0007567; P:parturition; IEP:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:RGD.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:RGD.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IDA:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:1900122; P:positive regulation of receptor binding; ISO:RGD.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; IMP:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0009644; P:response to high light intensity; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0048771; P:tissue remodeling; IDA:RGD.
DR GO; GO:0019087; P:transformation of host cell by virus; IDA:RGD.
DR CDD; cd00062; FN2; 3.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.10.10.10; -; 3.
DR Gene3D; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
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; IPR013806; Kringle-like.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR028688; MMP9.
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 InterPro; IPR006970; PT.
DR PANTHER; PTHR10201:SF30; PTHR10201:SF30; 1.
DR Pfam; PF00040; fn2; 3.
DR Pfam; PF00045; Hemopexin; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF04886; PT; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00059; FN2; 3.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR SUPFAM; SSF57440; SSF57440; 3.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00023; FN2_1; 2.
DR PROSITE; PS51092; FN2_2; 3.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen degradation; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT PROPEP 20..107
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT /id="PRO_0000028762"
FT CHAIN 108..708
FT /note="Matrix metalloproteinase-9"
FT /id="PRO_0000028763"
FT DOMAIN 226..274
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 284..332
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 343..391
FT /note="Fibronectin type-II 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT REPEAT 521..566
FT /note="Hemopexin 1"
FT REPEAT 567..611
FT /note="Hemopexin 2"
FT REPEAT 613..660
FT /note="Hemopexin 3"
FT REPEAT 661..707
FT /note="Hemopexin 4"
FT REGION 441..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 98..105
FT /note="Cysteine switch"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT COMPBIAS 455..474
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 100
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|UniProtKB:P14780"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 231..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 245..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 289..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 303..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 348..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 362..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 519..707
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT CONFLICT 2
FT /note="S -> N (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="D -> E (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 326..327
FT /note="AD -> LY (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="S -> G (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="H -> Q (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="S -> P (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="D -> V (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="N -> S (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="F -> L (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="S -> A (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="P -> S (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 586..589
FT /note="LWAQ -> SGRK (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="S -> T (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="Q -> H (in Ref. 1; AAA90911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 78611 MW; D57DC0D1B93A778C CRC64;
MSPWQPLLLV LLALGYSFAA PHQRQPTYVV FPRDLKTSNL TDTQLAEDYL YRYGYTRAAQ
MMGEKQSLRP ALLMLQKQLS LPQTGELDSE TLKAIRSPRC GVPDVGKFQT FDGDLKWHHH
NITYWIQSYT EDLPRDVIDD SFARAFAVWS AVTPLTFTRV YGLEADIVIQ FGVAEHGDGY
PFDGKDGLLA HAFPPGPGIQ GDAHFDDDEL WSLGKGAVVP TYFGNANGAP CHFPFTFEGR
SYLSCTTDGR NDGKPWCGTT ADYDTDRKYG FCPSENLYTE HGNGDGKPCV FPFIFEGHSY
SACTTKGRSD GYRWCATTAN YDQDKADGFC PTRADVTVTG GNSAGEMCVF PFVFLGKQYS
TCTSEGRSDG RLWCATTSNF DADKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM
YPMYHYHEDS PLHEDDIKGI HHLYGRGSKP DPRPPATTAA EPQPTAPPTM CSTAPPMAYP
TGGPTVAPTG APSPGPTGPP TAGPSEAPTE SSTPDDNPCN VDVFDAIADI QGALHFFKDG
RYWKFSNHGG NQLQGPFLIA RTWPAFPSKL NSAFEDPQPK KIFFFLWAQM WVYTGQSVLG
PRSLDKLGLG SEVTLVTGLL PRRGGKALLI SRERIWKFDL KSQKVDPQSV TRLDNEFSGV
PWNSHNVFQY QDKAYFCHDK YFWRVSFHNR VNQVDHVAYV TYDLLQCP
