MMP2_RAT
ID MMP2_RAT Reviewed; 662 AA.
AC P33436; P97581; Q6GMM9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=72 kDa type IV collagenase;
DE EC=3.4.24.24 {ECO:0000250|UniProtKB:P08253};
DE AltName: Full=72 kDa gelatinase;
DE AltName: Full=Gelatinase A;
DE AltName: Full=Matrix metalloproteinase-2;
DE Short=MMP-2;
DE Contains:
DE RecName: Full=PEX;
DE Flags: Precursor;
GN Name=Mmp2;
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].
RX PubMed=7916617; DOI=10.1042/bj2910441;
RA Marti H.P., McNeil L., Davies M., Martin J., Lovett D.H.;
RT "Homology cloning of rat 72 kDa type IV collagenase: cytokine and second-
RT messenger inducibility in glomerular mesangial cells.";
RL Biochem. J. 291:441-446(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Skin;
RA Okada A., Basset P.;
RT "The cloning of the cDNA encoding rat gelatinase A from a rat skin wound
RT cDNA library.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-29, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
CC -!- FUNCTION: Ubiquitinous metalloproteinase that is involved in diverse
CC functions such as remodeling of the vasculature, angiogenesis, tissue
CC repair, tumor invasion, inflammation, and atherosclerotic plaque
CC rupture. As well as degrading extracellular matrix proteins, can also
CC act on several nonmatrix proteins such as big endothelial 1 and beta-
CC type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu
CC bond. Appears to have a role in myocardial cell death pathways.
CC Contributes to myocardial oxidative stress by regulating the activity
CC of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of
CC the fibrovascular tissues (By similarity). {ECO:0000250}.
CC -!- FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2, posseses
CC anti-angiogenic and anti-tumor properties and inhibits cell migration
CC and cell adhesion to FGF2 and vitronectin. Ligand for integrin alpha-
CC v/beta3 on the surface of blood vessels (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X.
CC Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.;
CC EC=3.4.24.24; Evidence={ECO:0000250|UniProtKB:P08253};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P08253};
CC Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P08253};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08253};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P08253};
CC -!- SUBUNIT: Interacts (via the C-terminal hemopexin-like domains-
CC containing region) with the integrin alpha-V/beta-3; the interaction
CC promotes vascular invasion in angiogenic vessels and melamoma cells.
CC Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-
CC terminal); the interaction inhibits the degradation activity. Interacts
CC with GSK3B (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in
CC angiogenic blood vessels and melanomas. Found in mitochondria, along
CC microfibrils, and in nuclei of cardiomyocytes (By similarity).
CC {ECO:0000250}.
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.
CC -!- PTM: Phosphorylation on multiple sites modulates enzymatic activity.
CC Phosphorylated by PKC in vitro (By similarity). {ECO:0000250}.
CC -!- PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3)
CC (By similarity). Autocatalytic cleavage in the C-terminal produces the
CC anti-angiogenic peptide, PEX. This processing appears to be facilitated
CC by binding integrin integrinv/beta3 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; X71466; CAA50583.1; -; mRNA.
DR EMBL; U65656; AAB41692.1; -; mRNA.
DR EMBL; BC074013; AAH74013.1; -; mRNA.
DR PIR; S34780; S34780.
DR RefSeq; NP_112316.2; NM_031054.2.
DR AlphaFoldDB; P33436; -.
DR SMR; P33436; -.
DR CORUM; P33436; -.
DR STRING; 10116.ENSRNOP00000022679; -.
DR BindingDB; P33436; -.
DR ChEMBL; CHEMBL1075175; -.
DR MEROPS; M10.003; -.
DR GlyGen; P33436; 2 sites.
DR PaxDb; P33436; -.
DR Ensembl; ENSRNOT00000022679; ENSRNOP00000022679; ENSRNOG00000016695.
DR GeneID; 81686; -.
DR KEGG; rno:81686; -.
DR CTD; 4313; -.
DR RGD; 621316; Mmp2.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000158511; -.
DR InParanoid; P33436; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P33436; -.
DR BRENDA; 3.4.24.24; 5301.
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-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P33436; -.
DR Proteomes; UP000002494; Chromosome 19.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0030017; C:sarcomere; ISO:RGD.
DR GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
DR GO; GO:0001968; F:fibronectin binding; IPI:RGD.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:RGD.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; 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:0001525; P:angiogenesis; IEP:RGD.
DR GO; GO:0001955; P:blood vessel maturation; ISO:RGD.
DR GO; GO:0060346; P:bone trabecula formation; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IMP:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IMP:RGD.
DR GO; GO:0071498; P:cellular response to fluid shear stress; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0007507; P:heart development; IDA:RGD.
DR GO; GO:0001957; P:intramembranous ossification; ISO:RGD.
DR GO; GO:0001553; P:luteinization; IEP:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:RGD.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IDA:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IDA:RGD.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IEP:RGD.
DR GO; GO:0007567; P:parturition; IEP:RGD.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IDA:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IDA:RGD.
DR GO; GO:0035094; P:response to nicotine; 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:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0048771; P:tissue remodeling; IDA:RGD.
DR CDD; cd00062; FN2; 3.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.10.10.10; -; 2.
DR Gene3D; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 2.
DR InterPro; IPR028708; 72kDa_collagenase.
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; 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:SF29; PTHR10201:SF29; 1.
DR Pfam; PF00040; fn2; 3.
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; 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; 3.
DR PROSITE; PS51092; FN2_2; 3.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Autocatalytic cleavage; Calcium; Collagen degradation;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:26479776"
FT PROPEP 30..109
FT /note="Activation peptide"
FT /id="PRO_0000028720"
FT CHAIN 110..662
FT /note="72 kDa type IV collagenase"
FT /id="PRO_0000028721"
FT CHAIN 445..662
FT /note="PEX"
FT /evidence="ECO:0000250"
FT /id="PRO_0000391629"
FT DOMAIN 228..276
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 286..334
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 344..392
FT /note="Fibronectin type-II 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT REPEAT 474..518
FT /note="Hemopexin 1"
FT REPEAT 519..565
FT /note="Hemopexin 2"
FT REPEAT 567..615
FT /note="Hemopexin 3"
FT REPEAT 616..662
FT /note="Hemopexin 4"
FT REGION 110..221
FT /note="Collagenase-like 1"
FT REGION 222..396
FT /note="Collagen-binding"
FT REGION 397..467
FT /note="Collagenase-like 2"
FT REGION 414..662
FT /note="Required for inhibitor TIMP2 binding"
FT /evidence="ECO:0000250"
FT MOTIF 100..107
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 523
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 571
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT BINDING 620
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08253"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 233..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 247..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 291..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 305..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 349..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 363..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 471..662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT CONFLICT 42
FT /note="S -> A (in Ref. 1; CAA50583)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="G -> A (in Ref. 1; CAA50583)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="S -> N (in Ref. 1; CAA50583)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="N -> H (in Ref. 1; CAA50583)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="S -> A (in Ref. 1; CAA50583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 74149 MW; C56BD787473FC03E CRC64;
MEARLVWGVL VGPLRVLCVL CCLLGHAIAA PSPIIKFPGD VSPKTDKELA VQYLNTFYGC
PKESCNLFVL KDTLKKMQKF FGLPQTGDLD QNTIETMRKP RCGNPDVANY NFFPRKPKWD
KNQITYRIIG YTPDLDPETV DDAFARALKV WSDVTPLRFS RIHDGEADIM INFGRWEHGD
GYPFDGKDGL LAHAFAPGTG VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN
GREYSSCTDT GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNGDGQP CKFPFRFQGT
SYNSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTV GGNSEGAPCV FPFTFLGNKY
ESCTSAGRSD GKVWCATTTN YDDDRKWGFC PDQGYSLFLV AAHEFGHAMG LEHSQDPGAL
MAPIYTYTKN FRLSNDDIKG IQELYGPSPD ADTDTGTGPT PTLGPVTPEI CKQDIVFDGI
AQIRGEIFFF KDRFIWRTVT PRDKPTGPLL VATFWPELPE KIDAVYEAPQ EEKAVFFAGN
EYWVYSASTL ERGYPKPLTS LGLPPDVQQV DAAFNWSKNK KTYIFSGDKF WRYNEVKKKM
DPGFPKLIAD SWNAIPDNLD AVVDLQGGGH SYFFKGAYYL KLENQSLKSV KFGSIKSDWL
GC
