ID   MMP14_MOUSE             Reviewed;         582 AA.
AC   P53690; O08645; O35369; Q8BTX2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=Matrix metalloproteinase-14;
DE            Short=MMP-14;
DE            EC=3.4.24.80;
DE   AltName: Full=MMP-X1;
DE   AltName: Full=MT-MMP;
DE   AltName: Full=Membrane-type matrix metalloproteinase 1;
DE            Short=MT-MMP 1;
DE            Short=MTMMP1;
DE   AltName: Full=Membrane-type-1 matrix metalloproteinase;
DE            Short=MT1-MMP;
DE            Short=MT1MMP;
DE   Flags: Precursor;
GN   Name=Mmp14; Synonyms=Mtmmp;
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].
RX   PubMed=7708715; DOI=10.1073/pnas.92.7.2730;
RA   Okada A., Bellocq J.-P., Rouyer N., Chenard M.P., Rio M.C., Chambon P.,
RA   Basset P.;
RT   "Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in
RT   stromal cells of human colon, breast, and head and neck carcinomas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Odaka A.;
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=9325265; DOI=10.1074/jbc.272.41.25511;
RA   Apte S.S., Fukai N., Beier D.R., Olsen B.R.;
RT   "The matrix metalloproteinase-14 (MMP-14) gene is structurally distinct
RT   from other MMP genes and is co-expressed with the TIMP-2 gene during mouse
RT   embryogenesis.";
RL   J. Biol. Chem. 272:25511-25517(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1; TISSUE=Kidney;
RX   PubMed=9648071; DOI=10.1046/j.1523-1755.1998.00xxx.x;
RA   Ota K., Stetler-Stevenson W.G., Yang Q., Kumar A., Wada J., Kashihara N.,
RA   Wallner E.I., Kanwar Y.S.;
RT   "Cloning of murine membrane-type-1-matrix metalloproteinase (MT-1-MMP) and
RT   its metanephric developmental regulation with respect to MMP-2 and its
RT   inhibitor.";
RL   Kidney Int. 54:131-142(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/N;
RX   PubMed=16778201; DOI=10.1158/0008-5472.can-06-0539;
RA   Rozanov D.V., Savinov A.Y., Golubkov V.S., Tomlinson S., Strongin A.Y.;
RT   "Interference with the complement system by tumor cell membrane type-1
RT   matrix metalloproteinase plays a significant role in promoting metastasis
RT   in mice.";
RL   Cancer Res. 66:6258-6263(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Eye, Spinal cord, and Thymus;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION.
RX   PubMed=10520996; DOI=10.1016/s0092-8674(00)80064-1;
RA   Holmbeck K., Bianco P., Caterina J., Yamada S., Kromer M., Kuznetsov S.A.,
RA   Mankani M., Robey P.G., Poole A.R., Pidoux I., Ward J.M.,
RA   Birkedal-Hansen H.;
RT   "MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and
RT   connective tissue disease due to inadequate collagen turnover.";
RL   Cell 99:81-92(1999).
CC   -!- FUNCTION: Endopeptidase that degrades various components of the
CC       extracellular matrix such as collagen. Activates progelatinase A.
CC       Essential for pericellular collagenolysis and modeling of skeletal and
CC       extraskeletal connective tissues during development (PubMed:10520996).
CC       May be involved in actin cytoskeleton reorganization by cleaving PTK7
CC       (By similarity). Acts as a positive regulator of cell growth and
CC       migration via activation of MMP15. Involved in the formation of the
CC       fibrovascular tissues (By similarity). Cleaves ADGRB1 to release
CC       vasculostatin-40 which inhibits angiogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:P50281, ECO:0000269|PubMed:10520996}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase activity. Activates progelatinase A by cleavage
CC         of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include
CC         35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-
CC         Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan
CC         interglobular domain.; EC=3.4.24.80;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with BST2.
CC       Interacts with DLL1; inhibits DLL1-induced Notch signaling.
CC       {ECO:0000250|UniProtKB:P50281}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
CC       Melanosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Forms a complex
CC       with BST2 and localizes to the cytoplasm. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in placenta, kidney, heart, lung,
CC       embryonic skeletal and periskeletal tissues.
CC   -!- DEVELOPMENTAL STAGE: Not detected before day 10.5. At day 12.5,
CC       prominently expressed in large arteries and the umbilical arteries,
CC       expressed at lower levels in the myocardium, craniofacial mesenchyme,
CC       nasal epithelium and liver capsule. At days 14.5 and 17.5, expressed in
CC       the musculoskeletal system, and ossification areas, with continued
CC       expression in the arterial tunica media.
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: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC   -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC       {ECO:0000250|UniProtKB:P50281}.
CC   -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR   EMBL; X83536; CAA58520.2; -; mRNA.
DR   EMBL; AF022432; AAB86602.1; -; Genomic_DNA.
DR   EMBL; AF022424; AAB86602.1; JOINED; Genomic_DNA.
DR   EMBL; AF022425; AAB86602.1; JOINED; Genomic_DNA.
DR   EMBL; AF022426; AAB86602.1; JOINED; Genomic_DNA.
DR   EMBL; AF022427; AAB86602.1; JOINED; Genomic_DNA.
DR   EMBL; AF022428; AAB86602.1; JOINED; Genomic_DNA.
DR   EMBL; AF022429; AAB86602.1; JOINED; Genomic_DNA.
DR   EMBL; AF022430; AAB86602.1; JOINED; Genomic_DNA.
DR   EMBL; AF022431; AAB86602.1; JOINED; Genomic_DNA.
DR   EMBL; U54984; AAB51753.1; -; mRNA.
DR   EMBL; DQ249870; ABB45784.1; -; mRNA.
DR   EMBL; AK088476; BAC40377.1; -; mRNA.
DR   EMBL; AK138611; BAE23719.1; -; mRNA.
DR   EMBL; AK149907; BAE29158.1; -; mRNA.
DR   EMBL; AK149988; BAE29216.1; -; mRNA.
DR   EMBL; AK165014; BAE38000.1; -; mRNA.
DR   EMBL; CH466535; EDL36348.1; -; Genomic_DNA.
DR   CCDS; CCDS36922.1; -.
DR   PIR; I48673; I48673.
DR   RefSeq; NP_032634.3; NM_008608.4.
DR   AlphaFoldDB; P53690; -.
DR   BMRB; P53690; -.
DR   SMR; P53690; -.
DR   BioGRID; 201446; 7.
DR   IntAct; P53690; 1.
DR   MINT; P53690; -.
DR   STRING; 10090.ENSMUSP00000087119; -.
DR   ChEMBL; CHEMBL4295783; -.
DR   MEROPS; M10.014; -.
DR   iPTMnet; P53690; -.
DR   PhosphoSitePlus; P53690; -.
DR   SwissPalm; P53690; -.
DR   MaxQB; P53690; -.
DR   PaxDb; 10090-ENSMUSP00000087119; -.
DR   PeptideAtlas; P53690; -.
DR   ProteomicsDB; 291371; -.
DR   Pumba; P53690; -.
DR   Antibodypedia; 4088; 1159 antibodies from 45 providers.
DR   DNASU; 17387; -.
DR   Ensembl; ENSMUST00000089688.6; ENSMUSP00000087119.5; ENSMUSG00000000957.12.
DR   GeneID; 17387; -.
DR   KEGG; mmu:17387; -.
DR   UCSC; uc007twc.2; mouse.
DR   AGR; MGI:101900; -.
DR   CTD; 4323; -.
DR   MGI; MGI:101900; Mmp14.
DR   VEuPathDB; HostDB:ENSMUSG00000000957; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   GeneTree; ENSGT00940000157808; -.
DR   HOGENOM; CLU_015489_8_1_1; -.
DR   InParanoid; P53690; -.
DR   OMA; DIKVWEG; -.
DR   OrthoDB; 2225278at2759; -.
DR   PhylomeDB; P53690; -.
DR   TreeFam; TF352396; -.
DR   BRENDA; 3.4.24.80; 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   BioGRID-ORCS; 17387; 0 hits in 80 CRISPR screens.
DR   ChiTaRS; Mmp14; mouse.
DR   PRO; PR:P53690; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; P53690; Protein.
DR   Bgee; ENSMUSG00000000957; Expressed in vault of skull and 255 other cell types or tissues.
DR   ExpressionAtlas; P53690; baseline and differential.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR   GO; GO:0044354; C:macropinosome; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; ISO:MGI.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0043615; P:astrocyte cell migration; IEA:Ensembl.
DR   GO; GO:0060348; P:bone development; IGI:MGI.
DR   GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0035988; P:chondrocyte proliferation; IGI:MGI.
DR   GO; GO:0030574; P:collagen catabolic process; IGI:MGI.
DR   GO; GO:0097094; P:craniofacial suture morphogenesis; IGI:MGI.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IGI:MGI.
DR   GO; GO:0001958; P:endochondral ossification; IGI:MGI.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0060322; P:head development; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:UniProtKB.
DR   GO; GO:0001503; P:ossification; IGI:MGI.
DR   GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:1905523; P:positive regulation of macrophage migration; IMP:BHF-UCL.
DR   GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:UniProtKB.
DR   GO; GO:0010954; P:positive regulation of protein processing; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; ISO:MGI.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0009725; P:response to hormone; ISO:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:1990834; P:response to odorant; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   GO; GO:0048771; P:tissue remodeling; ISO:MGI.
DR   GO; GO:0031638; P:zymogen activation; IMP: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   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 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; IPR021805; Pept_M10A_metallopeptidase_C.
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; IPR036366; PGBDSf.
DR   PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF24; MATRIX METALLOPROTEINASE-14; 1.
DR   Pfam; PF11857; DUF3377; 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; P53690; MM.
PE   2: Evidence at transcript level;
KW   Calcium; Cleavage on pair of basic residues; Collagen degradation;
KW   Cytoplasm; Disulfide bond; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..111
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028800"
FT   CHAIN           112..582
FT                   /note="Matrix metalloproteinase-14"
FT                   /id="PRO_0000028801"
FT   TOPO_DOM        112..541
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        542..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        563..582
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          316..364
FT                   /note="Hemopexin 1"
FT   REPEAT          365..410
FT                   /note="Hemopexin 2"
FT   REPEAT          412..460
FT                   /note="Hemopexin 3"
FT   REPEAT          461..508
FT                   /note="Hemopexin 4"
FT   REGION          280..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           91..98
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   MOD_RES         399
FT                   /note="Phosphotyrosine; by PKDCC"
FT                   /evidence="ECO:0000250|UniProtKB:P50281"
FT   DISULFID        319..508
FT                   /evidence="ECO:0000250"
FT   CONFLICT        133
FT                   /note="P -> S (in Ref. 3; AAB86602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255
FT                   /note="A -> D (in Ref. 1; CAA58520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258
FT                   /note="A -> S (in Ref. 1; CAA58520 and 4; AAB51753)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341
FT                   /note="F -> L (in Ref. 1; CAA58520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346
FT                   /note="N -> P (in Ref. 3; AAB86602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="K -> T (in Ref. 1; CAA58520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        390..391
FT                   /note="FD -> CV (in Ref. 1; CAA58520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400..401
FT                   /note="PK -> AN (in Ref. 1; CAA58520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        407
FT                   /note="G -> V (in Ref. 1; CAA58520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412
FT                   /note="T -> S (in Ref. 1; CAA58520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        417
FT                   /note="A -> T (in Ref. 1; CAA58520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        512
FT                   /note="G -> R (in Ref. 4; AAB51753)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   582 AA;  65919 MW;  6CA95CFD5811B093 CRC64;
     MSPAPRPSRS LLLPLLTLGT ALASLGWAQG SNFSPEAWLQ QYGYLPPGDL RTHTQRSPQS
     LSAAIAAMQK FYGLQVTGKA DLATMMAMRR PRCGVPDKFG TEIKANVRRK RYAIQGLKWQ
     HNEITFCIQN YTPKVGEYAT FEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIL
     FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVQNEDLNG NDIFLVAVHE
     LGHALGLEHS NDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT
     SRPSVPDKPK NPAYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF
     WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF
     WMPNGKTYFF RGNKYYRFNE EFRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG
     NKYWKFNNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA
     AVVLPVLLLL LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV
//