MMP16_HUMAN
ID MMP16_HUMAN Reviewed; 607 AA.
AC P51512; B2RAN7; Q14824; Q52H48;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Matrix metalloproteinase-16;
DE Short=MMP-16;
DE EC=3.4.24.-;
DE AltName: Full=MMP-X2;
DE AltName: Full=Membrane-type matrix metalloproteinase 3;
DE Short=MT-MMP 3;
DE Short=MTMMP3;
DE AltName: Full=Membrane-type-3 matrix metalloproteinase;
DE Short=MT3-MMP;
DE Short=MT3MMP;
DE Flags: Precursor;
GN Name=MMP16 {ECO:0000312|HGNC:HGNC:7162};
GN Synonyms=C8orf57 {ECO:0000312|HGNC:HGNC:7162}, MMPX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Placenta;
RX PubMed=7559440; DOI=10.1074/jbc.270.39.23013;
RA Takino T., Sato H., Shinagawa A., Seiki M.;
RT "Identification of the second membrane-type matrix metalloproteinase (MT-
RT MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique
RT membrane-type subclass in the MMP family.";
RL J. Biol. Chem. 270:23013-23020(1995).
RN [2]
RP SEQUENCE REVISION.
RA Seiki M.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=Ovary;
RX PubMed=9396633; DOI=10.1016/s0167-4781(97)00120-6;
RA Matsumoto S., Katoh M., Saito S., Watanabe T., Masuho Y.;
RT "Identification of soluble type of membrane-type matrix metalloproteinase-3
RT formed by alternatively spliced mRNA.";
RL Biochim. Biophys. Acta 1354:159-170(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Fetal brain;
RX PubMed=9092507; DOI=10.1074/jbc.272.15.9749;
RA Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.;
RT "Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in
RT rat vascular smooth muscle cells and characterization of MT3-MMPs with and
RT without transmembrane domain.";
RL J. Biol. Chem. 272:9749-9754(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Brain;
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 [9]
RP INTERACTION WITH CSPG4, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11278606; DOI=10.1074/jbc.m010053200;
RA Iida J., Pei D., Kang T., Simpson M.A., Herlyn M., Furcht L.T.,
RA McCarthy J.B.;
RT "Melanoma chondroitin sulfate proteoglycan regulates matrix
RT metalloproteinase-dependent human melanoma invasion into type I collagen.";
RL J. Biol. Chem. 276:18786-18794(2001).
RN [10] {ECO:0007744|PDB:1RM8}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 124-292 IN COMPLEX WITH INHIBITOR;
RP CALCIUM AND ZINC, ZINC-BINDING SITES, AND CALCIUM-BINDING SITES.
RX PubMed=14741217; DOI=10.1016/j.jmb.2003.12.022;
RA Lang R., Braun M., Sounni N.E., Noel A., Frankenne F., Foidart J.M.,
RA Bode W., Maskos K.;
RT "Crystal structure of the catalytic domain of MMP-16/MT3-MMP:
RT characterization of MT-MMP specific features.";
RL J. Mol. Biol. 336:213-225(2004).
CC -!- FUNCTION: Endopeptidase that degrades various components of the
CC extracellular matrix, such as collagen type III and fibronectin.
CC Activates progelatinase A. Involved in the matrix remodeling of blood
CC vessels. Isoform short cleaves fibronectin and also collagen type III,
CC but at lower rate. It has no effect on type I, II, IV and V collagen.
CC However, upon interaction with CSPG4, it may be involved in degradation
CC and invasion of type I collagen by melanoma cells.
CC {ECO:0000269|PubMed:11278606}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: TIMP-2 shows little inhibitory activity compared
CC to TIMP-1. TIMP-1 seems to have less binding affinity than TIMP-2 for
CC the short isoform.
CC -!- SUBUNIT: Interacts with CSPG4 through CSPG4 chondroitin sulfate
CC glycosaminoglycan. {ECO:0000269|PubMed:11278606,
CC ECO:0000269|PubMed:14741217}.
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}; Extracellular side
CC {ECO:0000305}. Note=Localized at the cell surface of melanoma cells.
CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Secreted, extracellular space,
CC extracellular matrix. Cell surface. Note=Localized at the cell surface
CC of melanoma cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P51512-1; Sequence=Displayed;
CC Name=Short; Synonyms=SM3;
CC IsoId=P51512-2; Sequence=VSP_005453, VSP_005454;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, ovary and
CC small intestine. Isoform Short is found in the ovary.
CC -!- DEVELOPMENTAL STAGE: Expressed in tissues undergoing reconstruction.
CC Present in fetal tissues, especially in brain. Expression seems to
CC decline with advanced development.
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 -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mmp16/";
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DR EMBL; AB009303; BAA23742.1; -; mRNA.
DR EMBL; D83646; BAA12022.1; -; mRNA.
DR EMBL; D83647; BAA12023.1; -; mRNA.
DR EMBL; D85511; BAA22226.1; -; mRNA.
DR EMBL; DQ003082; AAX84515.1; -; Genomic_DNA.
DR EMBL; AK314274; BAG36934.1; -; mRNA.
DR EMBL; CH471060; EAW91651.1; -; Genomic_DNA.
DR EMBL; BC069500; AAH69500.1; -; mRNA.
DR EMBL; BC075004; AAH75004.1; -; mRNA.
DR EMBL; BC075005; AAH75005.1; -; mRNA.
DR CCDS; CCDS6246.1; -. [P51512-1]
DR RefSeq; NP_005932.2; NM_005941.4. [P51512-1]
DR PDB; 1RM8; X-ray; 1.80 A; A=124-292.
DR PDBsum; 1RM8; -.
DR AlphaFoldDB; P51512; -.
DR SMR; P51512; -.
DR BioGRID; 110468; 1.
DR IntAct; P51512; 1.
DR MINT; P51512; -.
DR STRING; 9606.ENSP00000286614; -.
DR BindingDB; P51512; -.
DR ChEMBL; CHEMBL2200; -.
DR DrugBank; DB03880; Batimastat.
DR DrugBank; DB00786; Marimastat.
DR GuidetoPHARMACOLOGY; 1640; -.
DR MEROPS; M10.016; -.
DR GlyGen; P51512; 1 site.
DR iPTMnet; P51512; -.
DR PhosphoSitePlus; P51512; -.
DR BioMuta; MMP16; -.
DR DMDM; 3041669; -.
DR EPD; P51512; -.
DR MassIVE; P51512; -.
DR PaxDb; P51512; -.
DR PeptideAtlas; P51512; -.
DR PRIDE; P51512; -.
DR ProteomicsDB; 56313; -. [P51512-1]
DR ProteomicsDB; 56314; -. [P51512-2]
DR Antibodypedia; 12678; 417 antibodies from 38 providers.
DR DNASU; 4325; -.
DR Ensembl; ENST00000286614.11; ENSP00000286614.6; ENSG00000156103.16. [P51512-1]
DR GeneID; 4325; -.
DR KEGG; hsa:4325; -.
DR MANE-Select; ENST00000286614.11; ENSP00000286614.6; NM_005941.5; NP_005932.2.
DR UCSC; uc003yeb.5; human. [P51512-1]
DR CTD; 4325; -.
DR DisGeNET; 4325; -.
DR GeneCards; MMP16; -.
DR HGNC; HGNC:7162; MMP16.
DR HPA; ENSG00000156103; Tissue enhanced (brain).
DR MIM; 602262; gene.
DR neXtProt; NX_P51512; -.
DR OpenTargets; ENSG00000156103; -.
DR PharmGKB; PA30874; -.
DR VEuPathDB; HostDB:ENSG00000156103; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000157532; -.
DR HOGENOM; CLU_015489_8_1_1; -.
DR InParanoid; P51512; -.
DR OMA; DFMGCEG; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P51512; -.
DR TreeFam; TF352396; -.
DR PathwayCommons; P51512; -.
DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR SignaLink; P51512; -.
DR BioGRID-ORCS; 4325; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; MMP16; human.
DR EvolutionaryTrace; P51512; -.
DR GeneWiki; MMP16; -.
DR GenomeRNAi; 4325; -.
DR Pharos; P51512; Tchem.
DR PRO; PR:P51512; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P51512; protein.
DR Bgee; ENSG00000156103; Expressed in endothelial cell and 146 other tissues.
DR ExpressionAtlas; P51512; baseline and differential.
DR Genevisible; P51512; HS.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; IEA:Ensembl.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
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; IPR028697; MMP16.
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 PANTHER; PTHR10201:SF26; PTHR10201:SF26; 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; 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 3D-structure; Alternative splicing; Calcium; Cell membrane;
KW Cleavage on pair of basic residues; Collagen degradation; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..119
FT /evidence="ECO:0000250"
FT /id="PRO_0000028812"
FT CHAIN 120..607
FT /note="Matrix metalloproteinase-16"
FT /id="PRO_0000028813"
FT TOPO_DOM 120..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 340..388
FT /note="Hemopexin 1"
FT REPEAT 389..434
FT /note="Hemopexin 2"
FT REPEAT 436..484
FT /note="Hemopexin 3"
FT REPEAT 485..532
FT /note="Hemopexin 4"
FT REGION 281..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 99..106
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 292..313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT BINDING 101
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 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:1RM8"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:1RM8"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 343..532
FT /evidence="ECO:0000250"
FT VAR_SEQ 408..457
FT /note="GNKYWVFKDTTLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGD
FT -> VKGDTLSVIQDGWLYKYHWKWILEQRQSVPVLSRQTEKHKTYEELSSITY (in
FT isoform Short)"
FT /evidence="ECO:0000303|PubMed:9396633"
FT /id="VSP_005453"
FT VAR_SEQ 458..607
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9396633"
FT /id="VSP_005454"
FT CONFLICT 521
FT /note="Y -> H (in Ref. 1; BAA23742)"
FT /evidence="ECO:0000305"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:1RM8"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1RM8"
FT HELIX 145..160
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1RM8"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:1RM8"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:1RM8"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1RM8"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:1RM8"
SQ SEQUENCE 607 AA; 69521 MW; 30D6247D9CB21663 CRC64;
MILLTFSTGR RLDFVHHSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY GYLPPTDPRM
SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR CGVPDQTRGS SKFHIRRKRY
ALTGQKWQHK HITYSIKNVT PKVGDPETRK AIRRAFDVWQ NVTPLTFEEV PYSELENGKR
DVDITIIFAS GFHGDSSPFD GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL
FLVAVHELGH ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT
RPLPTVPPHR SIPPADPRKN DRPKPPRPPT GRPSYPGAKP NICDGNFNTL AILRREMFVF
KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD GNFVFFKGNK YWVFKDTTLQ
PGYPHDLITL GSGIPPHGID SAIWWEDVGK TYFFKGDRYW RYSEEMKTMD PGYPKPITVW
KGIPESPQGA FVHKENGFTY FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRVK
EGHSPPDDVD IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK
RSMQEWV
