D2MP_DROME
ID D2MP_DROME Reviewed; 758 AA.
AC Q8MPP3; A0A0B4KFG9; A0A0C4DHC9; Q5BIL2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Matrix metalloproteinase-2 {ECO:0000303|PubMed:11967260};
DE Short=Dm2-MMP {ECO:0000303|PubMed:11967260};
DE EC=3.4.24.- {ECO:0000305};
DE Flags: Precursor;
GN Name=Mmp2 {ECO:0000312|FlyBase:FBgn0033438};
GN ORFNames=CG1794 {ECO:0000312|FlyBase:FBgn0033438};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:CAC81969.1};
RN [1] {ECO:0000312|EMBL:CAC81969.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11967260; DOI=10.1074/jbc.m200121200;
RA Llano E., Adam G., Pendas A.M., Quesada V., Sanchez L.M., Santamaria I.,
RA Noselli S., Lopez-Otin C.;
RT "Structural and enzymatic characterization of Drosophila Dm2-MMP, a
RT membrane-bound matrix metalloproteinase with tissue-specific expression.";
RL J. Biol. Chem. 277:23321-23329(2002).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAX33360.1, ECO:0000312|EMBL:AGV77141.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12530966; DOI=10.1016/s1534-5807(02)00400-8;
RA Page-McCaw A., Serano J., Sante J.M., Rubin G.M.;
RT "Drosophila matrix metalloproteinases are required for tissue remodeling,
RT but not embryonic development.";
RL Dev. Cell 4:95-106(2003).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18045838; DOI=10.1242/dev.011072;
RA Miller C.M., Page-McCaw A., Broihier H.T.;
RT "Matrix metalloproteinases promote motor axon fasciculation in the
RT Drosophila embryo.";
RL Development 135:95-109(2008).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=19751719; DOI=10.1016/j.ydbio.2009.09.005;
RA Guha A., Lin L., Kornberg T.B.;
RT "Regulation of Drosophila matrix metalloprotease Mmp2 is essential for wing
RT imaginal disc:trachea association and air sac tubulogenesis.";
RL Dev. Biol. 335:317-326(2009).
RN [8] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=20412776; DOI=10.1016/j.devcel.2010.02.010;
RA Yasunaga K., Kanamori T., Morikawa R., Suzuki E., Emoto K.;
RT "Dendrite reshaping of adult Drosophila sensory neurons requires matrix
RT metalloproteinase-mediated modification of the basement membranes.";
RL Dev. Cell 18:621-632(2010).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=21471368; DOI=10.1523/jneurosci.4811-10.2011;
RA Miller C.M., Liu N., Page-McCaw A., Broihier H.T.;
RT "Drosophila MMP2 regulates the matrix molecule faulty attraction (Frac) to
RT promote motor axon targeting in Drosophila.";
RL J. Neurosci. 31:5335-5347(2011).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=22262460; DOI=10.1091/mbc.e11-09-0745;
RA Stevens L.J., Page-McCaw A.;
RT "A secreted MMP is required for reepithelialization during wound healing.";
RL Mol. Biol. Cell 23:1068-1079(2012).
RN [11] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25267296; DOI=10.1083/jcb.201403084;
RA Wang X., Page-McCaw A.;
RT "A matrix metalloproteinase mediates long-distance attenuation of stem cell
RT proliferation.";
RL J. Cell Biol. 206:923-936(2014).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=25520167; DOI=10.1038/srep07535;
RA Jia Q., Liu Y., Liu H., Li S.;
RT "Mmp1 and Mmp2 cooperatively induce Drosophila fat body cell dissociation
RT with distinct roles.";
RL Sci. Rep. 4:7535-7535(2014).
RN [13] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25695427; DOI=10.1371/journal.pgen.1004989;
RA Deady L.D., Shen W., Mosure S.A., Spradling A.C., Sun J.;
RT "Matrix metalloproteinase 2 is required for ovulation and corpus luteum
RT formation in Drosophila.";
RL PLoS Genet. 11:E1004989-E1004989(2015).
CC -!- FUNCTION: Has metalloproteinase activity (PubMed:11967260). Required
CC for larval tissue histolysis during metamorphosis and is involved in
CC pupal head eversion and fusion of the wing imaginal tissue
CC (PubMed:12530966). Required for growth of the dorsal air sac primordium
CC and development of the dorsal air sacs (PubMed:19751719). Promotes
CC embryonic motor axon fasciculation (PubMed:18045838). Cleaves and
CC activates frac to promote motor axon bundling during outgrowth
CC (PubMed:21471368). Promotes the reshaping of adult sensory neuron
CC dendrites from a radial to lattice-like shape which occurs after
CC eclosion by degrading the basement membrane on which the dendrites grow
CC (PubMed:20412776). Involved in inhibition of follicle stem cell
CC proliferation by cleaving Dlp, inhibiting its interaction with wg and
CC preventing Dlp-mediated spreading of wg to follicle stem cells to
CC enhance their proliferation (PubMed:25267296). Plays a role in wound
CC healing (PubMed:22262460). Involved in fat body dissociation which
CC occurs during metamorphosis by degrading basement membrane components,
CC leading to destruction of cell-basement membrane junctions
CC (PubMed:25520167). Required for posterior follicle cell degradation and
CC ovulation (PubMed:25695427). {ECO:0000269|PubMed:11967260,
CC ECO:0000269|PubMed:12530966, ECO:0000269|PubMed:18045838,
CC ECO:0000269|PubMed:19751719, ECO:0000269|PubMed:20412776,
CC ECO:0000269|PubMed:21471368, ECO:0000269|PubMed:22262460,
CC ECO:0000269|PubMed:25267296, ECO:0000269|PubMed:25520167,
CC ECO:0000269|PubMed:25695427}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:11967260};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:11967260};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11967260,
CC ECO:0000269|PubMed:25267296}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B {ECO:0000312|FlyBase:FBgn0033438};
CC IsoId=Q8MPP3-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0033438};
CC IsoId=Q8MPP3-2; Sequence=VSP_057940;
CC Name=D {ECO:0000312|FlyBase:FBgn0033438};
CC IsoId=Q8MPP3-3; Sequence=VSP_057941;
CC -!- TISSUE SPECIFICITY: Widely expressed during embryogenesis including in
CC the mesoderm, developing gut, central and peripheral nervous systems
CC and imaginal disks (PubMed:12530966). In the embryonic nervous system,
CC expressed in neurons and glia (PubMed:18045838). In third instar
CC larvae, strongly expressed in the morphogenetic furrow of eye imaginal
CC disks and in the optic lobe region of the brain (PubMed:11967260).
CC Expressed in posterior follicle cells in all mature stage 14 follicles
CC but not in earlier follicles and is also expressed in some anterior
CC follicle cells that help form dorsal eggshell structures
CC (PubMed:25695427). {ECO:0000269|PubMed:11967260,
CC ECO:0000269|PubMed:12530966, ECO:0000269|PubMed:18045838,
CC ECO:0000269|PubMed:25695427}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos beginning at 8-12 hours, in
CC first instar larvae, in pupae and in male and female adults with
CC highest expression in early pupae (PubMed:11967260, PubMed:12530966).
CC In epithelial cells, weakly expressed at late pupal stages with
CC significantly elevated expression at the early adult stage of 0-4 hours
CC after eclosion and levels returning to normal by 3 days after eclosion
CC (PubMed:20412776). {ECO:0000269|PubMed:11967260,
CC ECO:0000269|PubMed:12530966, ECO:0000269|PubMed:20412776}.
CC -!- DISRUPTION PHENOTYPE: Defective larval tissue histolysis and epithelial
CC fusion during metamorphosis (PubMed:12530966). Impaired fasciculation
CC of ISNb nerves (PubMed:18045838). {ECO:0000269|PubMed:12530966,
CC ECO:0000269|PubMed:18045838}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; AJ289232; CAC81969.1; -; mRNA.
DR EMBL; AE013599; AAF58911.6; -; Genomic_DNA.
DR EMBL; AE013599; AAS64885.1; -; Genomic_DNA.
DR EMBL; AE013599; AGB93363.1; -; Genomic_DNA.
DR EMBL; BT021212; AAX33360.1; -; mRNA.
DR EMBL; BT150239; AGV77141.1; -; mRNA.
DR RefSeq; NP_001260830.1; NM_001273901.1. [Q8MPP3-2]
DR RefSeq; NP_610511.3; NM_136667.3. [Q8MPP3-3]
DR RefSeq; NP_995788.1; NM_206066.3. [Q8MPP3-1]
DR AlphaFoldDB; Q8MPP3; -.
DR STRING; 7227.FBpp0087585; -.
DR MEROPS; M10.036; -.
DR PaxDb; Q8MPP3; -.
DR EnsemblMetazoa; FBtr0088501; FBpp0087585; FBgn0033438. [Q8MPP3-1]
DR EnsemblMetazoa; FBtr0334807; FBpp0306848; FBgn0033438. [Q8MPP3-2]
DR EnsemblMetazoa; FBtr0334808; FBpp0306849; FBgn0033438. [Q8MPP3-3]
DR GeneID; 35997; -.
DR KEGG; dme:Dmel_CG1794; -.
DR UCSC; CG1794-RB; d. melanogaster. [Q8MPP3-1]
DR CTD; 4313; -.
DR FlyBase; FBgn0033438; Mmp2.
DR VEuPathDB; VectorBase:FBgn0033438; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; Q8MPP3; -.
DR OMA; YPERPNY; -.
DR PhylomeDB; Q8MPP3; -.
DR Reactome; R-DME-1442490; Collagen degradation.
DR Reactome; R-DME-1474228; Degradation of the extracellular matrix.
DR Reactome; R-DME-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-DME-210991; Basigin interactions.
DR Reactome; R-DME-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 35997; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Mmp2; fly.
DR GenomeRNAi; 35997; -.
DR PRO; PR:Q8MPP3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033438; Expressed in saliva-secreting gland and 30 other tissues.
DR Genevisible; Q8MPP3; DM.
DR GO; GO:0030425; C:dendrite; IMP:FlyBase.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:FlyBase.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0004175; F:endopeptidase activity; IDA:FlyBase.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; IDA:FlyBase.
DR GO; GO:0007505; P:adult fat body development; IMP:FlyBase.
DR GO; GO:0034769; P:basement membrane disassembly; IMP:FlyBase.
DR GO; GO:0071711; P:basement membrane organization; IMP:FlyBase.
DR GO; GO:0003319; P:cardioblast migration to the midline involved in heart rudiment formation; IMP:FlyBase.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:FlyBase.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0003144; P:embryonic heart tube formation; IMP:FlyBase.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0097156; P:fasciculation of motor neuron axon; IMP:FlyBase.
DR GO; GO:0007561; P:imaginal disc eversion; IMP:FlyBase.
DR GO; GO:0046529; P:imaginal disc fusion, thorax closure; IMP:FlyBase.
DR GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:FlyBase.
DR GO; GO:1901202; P:negative regulation of extracellular matrix assembly; IMP:FlyBase.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0030728; P:ovulation; IMP:FlyBase.
DR GO; GO:0016485; P:protein processing; IMP:FlyBase.
DR GO; GO:0006929; P:substrate-dependent cell migration; IMP:FlyBase.
DR GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IMP:FlyBase.
DR GO; GO:0035202; P:tracheal pit formation in open tracheal system; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
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; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR Pfam; PF00045; Hemopexin; 3.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 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; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell membrane;
KW Cleavage on pair of basic residues; Disulfide bond; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..?
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434511"
FT CHAIN ?..758
FT /note="Matrix metalloproteinase-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434512"
FT TOPO_DOM ?..738
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 739..756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..758
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 513..561
FT /note="Hemopexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01011"
FT REPEAT 565..610
FT /note="Hemopexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01011"
FT REPEAT 612..659
FT /note="Hemopexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01011"
FT REPEAT 660..707
FT /note="Hemopexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01011"
FT REGION 335..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT DISULFID 516..707
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform C)"
FT /id="VSP_057940"
FT VAR_SEQ 1..152
FT /note="MFSKYVLATLLALFAQSMCIQELSLPPEGSHSTAATRSKKAKTAISEDIMYN
FT YLMQFDYLPKSDLETGALRTEDQLKEAIRSLQSFGNITVTGEIDSATARLIQKPRCGVG
FT DRRSADSFSPDNLYHEIGSNVRVRRFALQGPKWSRTDLTWS -> MLSLWPRRQFSAAA
FT VLLHFGCTWSLVLATRLAVISWRLFLCFLR (in isoform D)"
FT /id="VSP_057941"
FT CONFLICT 43
FT /note="T -> N (in Ref. 4; AAX33360)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="K -> E (in Ref. 4; AAX33360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 89137 MW; 0F06C262A5F4CB4A CRC64;
MFSKYVLATL LALFAQSMCI QELSLPPEGS HSTAATRSKK AKTAISEDIM YNYLMQFDYL
PKSDLETGAL RTEDQLKEAI RSLQSFGNIT VTGEIDSATA RLIQKPRCGV GDRRSADSFS
PDNLYHEIGS NVRVRRFALQ GPKWSRTDLT WSMVNRSMPD ASKVERMVQT ALDVWANHSK
LTFREVYSDQ ADIQILFARR AHGDGYKFDG PGQVLAHAFY PGEGRGGDAH FDADETWNFD
GESDDSHGTN FLNVALHELG HSLGLAHSAI PDAVMFPWYQ NNEVAGNLPD DDRYGIQQLY
GTKEKTWGPY KPQTTTTTTT TTTMRAMIYR ADKPAYWPWN NPSNNPNNDR NRARERQEEE
RRRQEKERRR QEEERRHQEE ERRRQVEERQ RQEEERWRQE QERQEEENRR RKIEHKSQWE
RNPSKERNRP RERQEMERRR QEQERQEQER QEQEDRRRER ERDRQLEWER RNRNGAREPV
TPTANTTPRP TNKPYPTVHR QHHHHNKPRK PKPDSCMTYY DAISIIRGEL FIFRGPYLWR
IGTSGLYNGY PTEIRRHWSA LPENLTKVDA VYENKQRQIV FFIGREYYVF NSVMLAPGFP
KPLASLGLPP TLTHIDASFV WGHNNRTYMT SGTLYWRIDD YTGQVELDYP RDMSIWSGVG
YNIDAAFQYL DGKTYFFKNL GYWEFNDDRM KVAHARAKLS ARRWMQCARS ANEVDDEQRW
TASLVSEGEE TGRSGSRELR INHFILSILL LAIANWRS
