ENPP2_BOVIN
ID ENPP2_BOVIN Reviewed; 888 AA.
AC A1A4K5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 2;
DE Short=E-NPP 2;
DE EC=3.1.4.39 {ECO:0000269|PubMed:12119361};
DE AltName: Full=Autotaxin {ECO:0000303|PubMed:12119361};
DE AltName: Full=Extracellular lysophospholipase D;
DE Short=LysoPLD {ECO:0000303|PubMed:12119361};
DE Flags: Precursor;
GN Name=ENPP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 250-266; 749-777 AND 847-866, CATALYTIC ACTIVITY,
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal blood;
RX PubMed=12119361; DOI=10.1083/jcb.200204026;
RA Umezu-Goto M., Kishi Y., Taira A., Hama K., Dohmae N., Takio K., Yamori T.,
RA Mills G.B., Inoue K., Aoki J., Arai H.;
RT "Autotaxin has lysophospholipase D activity leading to tumor cell growth
RT and motility by lysophosphatidic acid production.";
RL J. Cell Biol. 158:227-233(2002).
CC -!- FUNCTION: Hydrolyzes lysophospholipids to produce the signaling
CC molecule lysophosphatidic acid (LPA) in extracellular fluids. Major
CC substrate is lysophosphatidylcholine (PubMed:12119361). Can also act on
CC sphingosylphosphorylcholine producing sphingosine-1-phosphate, a
CC modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some
CC extent pNP-TMP, and barely ATP. Involved in several motility-related
CC processes such as angiogenesis and neurite outgrowth. Acts as an
CC angiogenic factor by stimulating migration of smooth muscle cells and
CC microtubule formation. Stimulates migration of melanoma cells, probably
CC via a pertussis toxin-sensitive G protein. May have a role in induction
CC of parturition. Possible involvement in cell proliferation and adipose
CC tissue development. Tumor cell motility-stimulating factor (By
CC similarity). Required for LPA production in activated platelets,
CC cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic
CC acids containing predominantly 18:2 and 20:4 fatty acids (By
CC similarity). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-
CC alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (By similarity).
CC {ECO:0000250|UniProtKB:Q13822, ECO:0000269|PubMed:12119361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-alkyl-
CC sn-glycero-3-phosphate + ethanolamine + H(+); Xref=Rhea:RHEA:15965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:58014, ChEBI:CHEBI:76168; EC=3.1.4.39;
CC Evidence={ECO:0000269|PubMed:12119361};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(9Z-octadecenyl)-sn-glycero-3-phosphocholine + H2O = 1-O-
CC (9Z-octadecenyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41684, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64396, ChEBI:CHEBI:78402;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41685;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:41712,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57875, ChEBI:CHEBI:64982;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41713;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn-
CC glycerol 3-phosphate + H(+) + L-serine; Xref=Rhea:RHEA:41716,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:64982, ChEBI:CHEBI:65214;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41717;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + H2O = 1-dodecanoyl-
CC sn-glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:38991,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72682, ChEBI:CHEBI:74966;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38992;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphing-4-enine-phosphocholine = choline + H(+) + sphing-
CC 4-enine 1-phosphate; Xref=Rhea:RHEA:38919, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58906,
CC ChEBI:CHEBI:60119; Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38920;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38915, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:74544;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38916;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC tetradecanoyl-sn-glycerol 3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38983, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64489, ChEBI:CHEBI:72683;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38984;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-decanoyl-sn-glycero-3-phosphocholine + H2O = 1-decanoyl-sn-
CC glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41131,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:77724, ChEBI:CHEBI:77726;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41132;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38975, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38976;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC octadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38979, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73858, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38980;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41135, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28733, ChEBI:CHEBI:74547;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41136;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate +
CC choline + H(+); Xref=Rhea:RHEA:41139, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74344,
CC ChEBI:CHEBI:74938; Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41140;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC hexadecyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41143, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64496, ChEBI:CHEBI:77580;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41144;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexanoyl-sn-
CC glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41400,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:78215, ChEBI:CHEBI:78223;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41401;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC dioctanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41416, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78228, ChEBI:CHEBI:78229;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41417;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC didecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41412, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78226, ChEBI:CHEBI:78227;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41413;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = 1-O-(1Z-
CC alkenyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41588, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:77283, ChEBI:CHEBI:77287;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41589;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ethanolamine + H(+);
CC Xref=Rhea:RHEA:38927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:74544, ChEBI:CHEBI:74971;
CC Evidence={ECO:0000250|UniProtKB:Q64610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38928;
CC Evidence={ECO:0000250|UniProtKB:Q64610};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + L-serine;
CC Xref=Rhea:RHEA:38931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:74544, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000250|UniProtKB:Q64610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38932;
CC Evidence={ECO:0000250|UniProtKB:Q64610};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q13822};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q13822};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12119361}.
CC -!- TISSUE SPECIFICITY: Detected in fetal serum (at protein level).
CC {ECO:0000269|PubMed:12119361}.
CC -!- PTM: N-glycosylation, but not furin-cleavage, plays a critical role on
CC secretion and on lysoPLD activity. {ECO:0000250|UniProtKB:Q9R1E6}.
CC -!- PTM: The interdomain disulfide bond between Cys-414 and Cys-831 is
CC essential for catalytic activity. {ECO:0000250|UniProtKB:Q9R1E6}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; BC126631; AAI26632.1; -; mRNA.
DR RefSeq; NP_001073762.1; NM_001080293.1.
DR AlphaFoldDB; A1A4K5; -.
DR SMR; A1A4K5; -.
DR STRING; 9913.ENSBTAP00000036974; -.
DR ChEMBL; CHEMBL2021747; -.
DR PaxDb; A1A4K5; -.
DR PRIDE; A1A4K5; -.
DR Ensembl; ENSBTAT00000037135; ENSBTAP00000036974; ENSBTAG00000013165.
DR GeneID; 532663; -.
DR KEGG; bta:532663; -.
DR CTD; 5168; -.
DR VEuPathDB; HostDB:ENSBTAG00000013165; -.
DR VGNC; VGNC:28505; ENPP2.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000155778; -.
DR HOGENOM; CLU_012256_0_0_1; -.
DR InParanoid; A1A4K5; -.
DR OMA; TNYHVVC; -.
DR OrthoDB; 999163at2759; -.
DR TreeFam; TF330032; -.
DR PRO; PR:A1A4K5; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000013165; Expressed in midbrain and 106 other tissues.
DR ExpressionAtlas; A1A4K5; baseline and differential.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004551; F:nucleotide diphosphatase activity; IEA:InterPro.
DR GO; GO:0004528; F:phosphodiesterase I activity; IBA:GO_Central.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0044849; P:estrous cycle; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0045765; P:regulation of angiogenesis; IEA:InterPro.
DR GO; GO:0030149; P:sphingolipid catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.570.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR029881; ENPP2.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR10151:SF21; PTHR10151:SF21; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR SUPFAM; SSF90188; SSF90188; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Chemotaxis; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Obesity;
KW Reference proteome; Repeat; Secreted; Signal; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:Q64610"
FT PROPEP 28..35
FT /note="Removed by furin"
FT /evidence="ECO:0000250|UniProtKB:Q64610"
FT /id="PRO_0000281647"
FT CHAIN 36..888
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT family member 2"
FT /id="PRO_0000281648"
FT DOMAIN 55..98
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 99..143
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT REGION 855..876
FT /note="Required for secretion"
FT /evidence="ECO:0000250"
FT MOTIF 127..129
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 211..214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 244..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 765
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 767
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 769
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 771
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 773
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT SITE 878
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 63..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 74..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 80..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 103..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 108..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 118..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 124..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 149..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 157..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 367..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 414..831
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 567..692
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 569..677
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 800..810
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT CONFLICT 775
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 888 AA; 101717 MW; C349950572B2BADF CRC64;
MARRRSCQLH QVISLFTFAV GVNICLGVTA NRIKRAEGWG EGPPTVLSDS PSINISGSCK
GRCFELQEAG PPDCRCDNLC KSYSSCCLDF DELCLKTAGG WECTKDRCGE VRNEDHACHC
SEDCLARGDC CTNYQVVCKG ESHWVDDDCE EIKTPECPAG FVRPPLIIFS VDGFRASYMK
KGSKVMPNIE KLRSCGTHSP YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA
HFNLRGREKF NHRWWGGQPL WITATKQGVI AGTFFWPVVI PHERRILTIL QWLTLPDHER
PSVYAFYSEQ PDFSGHKYGP FGPEMTNPLR DIDKTVGQLM DGLKQLKLHR CVNVIFVGDH
GMEDVTCDRT EFLSNYLTNV DDIILVPGTL GRIRPKFNNH AKYDPKVIIA NLTCKKPDQH
FKPYLKQHLP KRLHYANNRR IEDVHLLVER RWHVARKPLE VYKKPSGKCF FQGDHGFDNK
VNSMQTVFVG YGPTFKYKTK VPPFENIELY NVMCDLLGLK PAPNNGTHGS LNHLLRTNTF
RPTVPEEVTR PNYPGVMYLQ SDFDLGCTCD DKAEPKNKLD ELNKHLHIKE STEAETRKFR
GSKNEIKENV NGNFEPRKER HLLYGRPAVL YRTRYDILYH TDFESGYSEI FLMPLWTSYT
VSKQADVSDI PAHLTNCVRP DVRVSPSFSQ SCLAYKNDKQ MSYGFLFPPY LSSSPEAKYD
AFLVTNMVPM YPAFKRIWNY FQRVLVKKYA SERNGVNVIS GPIFDYDYDG LHDTQDKIKQ
YVEGSSVPVP THYYSILTSC LDFTQPADRC DGPLSVSAFV LPHRPDNDES CNSSEDESKW
VEELLKMHTA RVRDIEHLTS LDFFRKTSRS YPEILTLKTY LQTYESEI
