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; 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 Genevisible; P53690; MM.
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.
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
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