MMP12_MOUSE
ID MMP12_MOUSE Reviewed; 473 AA.
AC P34960; Q3TB28; Q3TBV6; Q3TBV9; Q3TD61; Q3U1S8; Q3U1S9; Q3U2R8; Q3UBC5;
AC Q4FJM7; Q8BJ92; Q8BJB3; Q8BJB6; Q8BJB8; Q8BJB9; Q8VED6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Macrophage metalloelastase;
DE Short=MME;
DE EC=3.4.24.65;
DE AltName: Full=Matrix metalloproteinase-12;
DE Short=MMP-12;
DE Flags: Precursor;
GN Name=Mmp12; Synonyms=Mme, Mmel;
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 110-136.
RC TISSUE=Macrophage;
RX PubMed=1537850; DOI=10.1016/s0021-9258(18)42885-2;
RA Shapiro S.D., Griffin G.L., Gilbert D.J., Jenkins N.A., Copeland N.G.,
RA Welgus H.G., Senior R.M., Ley T.J.;
RT "Molecular cloning, chromosomal localization, and bacterial expression of a
RT murine macrophage metalloelastase.";
RL J. Biol. Chem. 267:4664-4671(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=B-cell, Dendritic cell, and Macrophage;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-473.
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in tissue injury and remodeling. Has
CC significant elastolytic activity. Can accept large and small amino
CC acids at the P1' site, but has a preference for leucine. Aromatic or
CC hydrophobic residues are preferred at the P1 site, with small
CC hydrophobic residues (preferably alanine) occupying P3 (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of soluble and insoluble elastin. Specific
CC cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in
CC the B chain of insulin.; EC=3.4.24.65;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {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 -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39526.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC40889.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M82831; AAA39526.1; ALT_INIT; mRNA.
DR EMBL; AK089309; BAC40836.1; -; mRNA.
DR EMBL; AK089335; BAC40846.1; -; mRNA.
DR EMBL; AK089452; BAC40889.1; ALT_INIT; mRNA.
DR EMBL; AK089523; BAC40913.1; -; mRNA.
DR EMBL; AK090051; BAC41067.1; -; mRNA.
DR EMBL; AK150596; BAE29689.1; -; mRNA.
DR EMBL; AK151021; BAE30039.1; -; mRNA.
DR EMBL; AK151273; BAE30260.1; -; mRNA.
DR EMBL; AK151933; BAE30809.1; -; mRNA.
DR EMBL; AK155139; BAE33072.1; -; mRNA.
DR EMBL; AK155743; BAE33411.1; -; mRNA.
DR EMBL; AK155747; BAE33414.1; -; mRNA.
DR EMBL; AK155748; BAE33415.1; -; mRNA.
DR EMBL; AK155865; BAE33469.1; -; mRNA.
DR EMBL; AK170360; BAE41743.1; -; mRNA.
DR EMBL; AK170364; BAE41746.1; -; mRNA.
DR EMBL; AK170798; BAE42035.1; -; mRNA.
DR EMBL; AK170804; BAE42039.1; -; mRNA.
DR EMBL; AK170976; BAE42154.1; -; mRNA.
DR EMBL; AK171006; BAE42177.1; -; mRNA.
DR EMBL; AK171032; BAE42198.1; -; mRNA.
DR EMBL; AK171036; BAE42201.1; -; mRNA.
DR EMBL; AK171176; BAE42294.1; -; mRNA.
DR EMBL; AK171428; BAE42446.1; -; mRNA.
DR EMBL; AK171447; BAE42457.1; -; mRNA.
DR EMBL; AK171448; BAE42458.1; -; mRNA.
DR EMBL; AK171449; BAE42459.1; -; mRNA.
DR EMBL; AK171450; BAE42460.1; -; mRNA.
DR EMBL; AK171466; BAE42472.1; -; mRNA.
DR EMBL; AK171468; BAE42474.1; -; mRNA.
DR EMBL; AK171470; BAE42476.1; -; mRNA.
DR EMBL; AK171472; BAE42478.1; -; mRNA.
DR EMBL; AK171485; BAE42486.1; -; mRNA.
DR EMBL; AK171518; BAE42502.1; -; mRNA.
DR EMBL; AK171542; BAE42516.1; -; mRNA.
DR EMBL; AK171570; BAE42531.1; -; mRNA.
DR EMBL; BC019135; AAH19135.2; -; mRNA.
DR EMBL; CT010377; CAJ18584.1; -; mRNA.
DR CCDS; CCDS22804.1; -.
DR PIR; A42401; A42401.
DR RefSeq; NP_001307005.1; NM_001320076.1.
DR RefSeq; NP_001307006.1; NM_001320077.1.
DR RefSeq; NP_032631.3; NM_008605.3.
DR AlphaFoldDB; P34960; -.
DR SMR; P34960; -.
DR STRING; 10090.ENSMUSP00000005950; -.
DR BindingDB; P34960; -.
DR ChEMBL; CHEMBL2594; -.
DR MEROPS; M10.009; -.
DR MoonProt; P34960; -.
DR GlyGen; P34960; 3 sites.
DR iPTMnet; P34960; -.
DR PhosphoSitePlus; P34960; -.
DR CPTAC; non-CPTAC-3481; -.
DR MaxQB; P34960; -.
DR PaxDb; P34960; -.
DR PRIDE; P34960; -.
DR ProteomicsDB; 291370; -.
DR Antibodypedia; 61960; 627 antibodies from 41 providers.
DR DNASU; 17381; -.
DR Ensembl; ENSMUST00000005950; ENSMUSP00000005950; ENSMUSG00000049723.
DR GeneID; 17381; -.
DR KEGG; mmu:17381; -.
DR UCSC; uc009och.1; mouse.
DR CTD; 4321; -.
DR MGI; MGI:97005; Mmp12.
DR VEuPathDB; HostDB:ENSMUSG00000049723; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000162085; -.
DR InParanoid; P34960; -.
DR OMA; VDNQYWR; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P34960; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.65; 3474.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 17381; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Mmp12; mouse.
DR PRO; PR:P34960; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P34960; protein.
DR Bgee; ENSMUSG00000049723; Expressed in animal zygote and 48 other tissues.
DR ExpressionAtlas; P34960; baseline and differential.
DR Genevisible; P34960; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0060435; P:bronchiole development; IDA:MGI.
DR GO; GO:0098586; P:cellular response to virus; IMP:CAFA.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0060309; P:elastin catabolic process; ISO:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:1904905; P:negative regulation of endothelial cell-matrix adhesion via fibronectin; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:CAFA.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:CAFA.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IMP:CAFA.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IMP:CAFA.
DR GO; GO:0006606; P:protein import into nucleus; IMP:CAFA.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0050691; P:regulation of defense response to virus by host; IMP:CAFA.
DR GO; GO:1901163; P:regulation of trophoblast cell migration; ISO:MGI.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISO:MGI.
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; 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 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 Calcium; Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000305"
FT PROPEP 29..109
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1537850"
FT /id="PRO_0000028778"
FT CHAIN 110..473
FT /note="Macrophage metalloelastase"
FT /id="PRO_0000028779"
FT REPEAT 289..332
FT /note="Hemopexin 1"
FT REPEAT 333..379
FT /note="Hemopexin 2"
FT REPEAT 381..429
FT /note="Hemopexin 3"
FT REPEAT 430..473
FT /note="Hemopexin 4"
FT MOTIF 94..101
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
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:0000250"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..473
FT /evidence="ECO:0000250"
FT CONFLICT 65
FT /note="K -> E (in Ref. 3; AAH19135 and 4; CAJ18584)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="E -> V (in Ref. 2; BAE30809/BAE30260/BAE30039/
FT BAE29689)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="T -> N (in Ref. 2; BAE33415)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="T -> A (in Ref. 2; BAE42486)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="H -> N (in Ref. 2; BAE42198)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> V (in Ref. 1; AAA39526)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> T (in Ref. 2; BAC40836)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="Y -> D (in Ref. 3; AAH19135 and 4; CAJ18584)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="L -> F (in Ref. 2; BAE33072)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="S -> N (in Ref. 3; AAH19135 and 4; CAJ18584)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="A -> P (in Ref. 2; BAC40846)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="P -> T (in Ref. 3; AAH19135 and 4; CAJ18584)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="F -> L (in Ref. 1; AAA39526)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="F -> Y (in Ref. 2; BAC40889/BAC40913)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="A -> D (in Ref. 2; BAE33415)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="T -> I (in Ref. 3; AAH19135 and 4; CAJ18584)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="I -> T (in Ref. 2; BAE41743)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="G -> A (in Ref. 1; AAA39526)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="H -> Q (in Ref. 3; AAH19135 and 4; CAJ18584)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="K -> R (in Ref. 2; BAC40836)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="S -> G (in Ref. 2; BAE42201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 54971 MW; D377250610BA249E CRC64;
MSCTLLKGVC TMKFLMMIVF LQVSACGAAP MNDSEFAEWY LSRFYDYGKD RIPMTKTKTN
RNFLKEKLQE MQQFFGLEAT GQLDNSTLAI MHIPRCGVPD VQHLRAVPQR SRWMKRYLTY
RIYNYTPDMK REDVDYIFQK AFQVWSDVTP LRFRKLHKDE ADIMILFAFG AHGDFNYFDG
KGGTLAHAFY PGPGIQGDAH FDEAETWTKS FQGTNLFLVA VHELGHSLGL QHSNNPKSIM
YPTYRYLNPS TFRLSADDIR NIQSLYGAPV KPPSLTKPSS PPSTFCHQSL SFDAVTTVGE
KIFFFKDWFF WWKLPGSPAT NITSISSIWP SIPSGIQAAY EIESRNQLFL FKDEKYWLIN
NLVPEPHYPR SIYSLGFSAS VKKVDAAVFD PLRQKVYFFV DKHYWRYDVR QELMDPAYPK
LISTHFPGIK PKIDAVLYFK RHYYIFQGAY QLEYDPLFRR VTKTLKSTSW FGC
