ID PA21B_BOVIN Reviewed; 145 AA. AC P00593; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 02-SEP-2026, entry version 199. DE RecName: Full=Phospholipase A2; DE EC=3.1.1.4 {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055}; DE AltName: Full=Group IB phospholipase A2; DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B; DE Flags: Precursor; GN Name=PLA2G1B; 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 [MRNA]. RX PubMed=3562249; DOI=10.1093/nar/15.7.3178; RA Tanaka T., Kimura S., Ota Y.; RT "Sequence of a cDNA coding for bovine pancreatic phospholipase A2."; RL Nucleic Acids Res. 15:3178-3178(1987). RN [2] RP PROTEIN SEQUENCE OF 16-22, AND PYROGLUTAMATE FORMATION AT GLN-16. RC TISSUE=Pancreas; RA Dutilh C.E., van Doren P.J., Verheul F.E.A.M., de Haas G.H.; RT "Isolation and properties of prophospholipase A2 from ox and sheep RT pancreas."; RL Eur. J. Biochem. 53:91-97(1975). RN [3] RP PROTEIN SEQUENCE OF 23-145. RX PubMed=620674; DOI=10.1111/j.1432-1033.1978.tb12019.x; RA Fleer E.A.M., Verheij H.M., de Haas G.H.; RT "The primary structure of bovine pancreatic phospholipase A2."; RL Eur. J. Biochem. 82:261-269(1978). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=712836; DOI=10.1016/0022-2836(78)90146-8; RA Dijkstra B.W., Drenth J., Kalk K.H., Vandermaelen P.J.; RT "Three-dimensional structure and disulfide bond connections in bovine RT pancreatic phospholipase A2."; RL J. Mol. Biol. 124:53-60(1978). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), ACTIVE SITE, AND CATALYTIC RP MECHANISM. RX PubMed=7464926; DOI=10.1038/289604a0; RA Dijkstra B.W., Drenth J., Kalk K.H.; RT "Active site and catalytic mechanism of phospholipase A2."; RL Nature 289:604-606(1981). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 23-145 IN COMPLEX WITH CALCIUM RP ION, COFACTOR, AND DISULFIDE BONDS. RX PubMed=7265241; DOI=10.1016/0022-2836(81)90081-4; RA Dijkstra B.W., Kalk K.H., Hol W.G.J., Drenth J.; RT "Structure of bovine pancreatic phospholipase A2 at 1.7A resolution."; RL J. Mol. Biol. 147:97-123(1981). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 17-145 OF PROENZYME, AND RP DISULFIDE BONDS. RA Dijkstra B.W., van Nes G.J.H., Kalk K.H., Brandenburg N.P., Hol W.G.J., RA Drenth J.; RT "The structure of bovine pancreatic prophospholipase A2 at 3.0-A RT resolution."; RL Acta Crystallogr. B 38:793-799(1982). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 23-145 IN COMPLEX WITH CALCIUM RP ION, COFACTOR, AND DISULFIDE BONDS. RX PubMed=9115986; DOI=10.1021/bi961576x; RA Sekar K., Yu B.Z., Rogers J., Lutton J., Liu X., Chen X., Tsai M.-D., RA Jain M.K., Sundaralingam M.; RT "Phospholipase A2 engineering. Structural and functional roles of the RT highly conserved active site residue aspartate-99."; RL Biochemistry 36:3104-3114(1997). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). RX PubMed=9369492; DOI=10.1021/bi971370b; RA Sekar K., Eswaramoorthy S., Jain M.K., Sundaralingam M.; RT "Crystal structure of the complex of bovine pancreatic phospholipase A2 RT with the inhibitor 1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2- RT phosphomethanol."; RL Biochemistry 36:14186-14191(1997). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 23-145 OF MUTANTS IN COMPLEX WITH RP CALCIUM ION, COFACTOR, AND DISULFIDE BONDS. RX PubMed=10089353; DOI=10.1107/s0907444998013699; RA Sekar K., Biswas R., Li Y., Tsai M., Sundaralingam M.; RT "Structures of the catalytic site mutants D99A and H48Q and the calcium- RT loop mutant D49E of phospholipase A2."; RL Acta Crystallogr. D 55:443-447(1999). RN [11] RP STRUCTURE BY NMR. RX PubMed=10074343; DOI=10.1021/bi982211a; RA Yuan C., Byeon I.-J.L., Li Y., Tsai M.-D.; RT "Structural analysis of phospholipase A2 from functional perspective. 1. RT Functionally relevant solution structure and roles of the hydrogen-bonding RT network."; RL Biochemistry 38:2909-2918(1999). RN [12] RP STRUCTURE BY NMR OF MUTANTS. RX PubMed=10074344; DOI=10.1021/bi9822123; RA Yuan C., Byeon I.-J.L., Poi M.-J., Tsai M.-D.; RT "Structural analysis of phospholipase A2 from functional perspective. 2. RT Characterization of a molten globule-like state induced by site-specific RT mutagenesis."; RL Biochemistry 38:2919-2929(1999). CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily CC targets dietary phospholipids in the intestinal tract. Hydrolyzes the CC ester bond of the fatty acyl group attached at sn-2 position of CC phospholipids (phospholipase A2 activity) with preference for CC phosphatidylethanolamines and phosphatidylglycerols over CC phosphatidylcholines. May play a role in the biosynthesis of N-acyl CC ethanolamines that regulate energy metabolism and inflammation in the CC intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl CC lysophosphatidylethanolamines, which are further cleaved by a CC lysophospholipase D to release N-acyl ethanolamines (By similarity). CC May act in an autocrine and paracrine manner (By similarity). Has anti- CC helminth activity in a process regulated by gut microbiota. Upon CC helminth infection of intestinal epithelia, directly affects CC phosphatidylethanolamine contents in the membrane of helminth larvae, CC likely controlling an array of phospholipid-mediated cellular processes CC such as membrane fusion and cell division while providing for better CC immune recognition, ultimately reducing larvae integrity and CC infectivity (By similarity). {ECO:0000250|UniProtKB:P04054, CC ECO:0000250|UniProtKB:P04055, ECO:0000250|UniProtKB:Q9Z0Y2}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; CC Evidence={ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055, CC ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE- CC ProRule:PRU10036}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1- CC tetradecanoyl-sn-glycero-3-phosphocholine + tetradecanoate + H(+); CC Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489; CC Evidence={ECO:0000250|UniProtKB:P04054}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1- CC hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H(+); CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine CC + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + (9Z)- CC octadecenoate + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, CC ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P04054}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; CC Evidence={ECO:0000250|UniProtKB:P04054}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+); Xref=Rhea:RHEA:40427, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'- CC sn-glycerol) + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn- CC glycerol) + (9Z)-octadecenoate + H(+); Xref=Rhea:RHEA:40919, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; CC Evidence={ECO:0000250|UniProtKB:P04054}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; CC Evidence={ECO:0000250|UniProtKB:P04054}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3- CC phosphoethanolamine + H2O = N-hexadecanoyl-1-(9Z-octadecenoyl)-sn- CC glycero-3-phosphoethanolamine + (9Z)-octadecenoate + H(+); CC Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphoethanolamine + H2O = 1-hexadecanoyl-sn-glycero-3- CC phosphoethanolamine + (9Z,12Z)-octadecadienoate + H(+); CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphoethanolamine + H2O = N,1-dihexadecanoyl-sn-glycero-3- CC phosphoethanolamine + (9Z,12Z)-octadecadienoate + H(+); CC Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425; CC Evidence={ECO:0000250|UniProtKB:P04055}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000305|PubMed:10089353, ECO:0000305|PubMed:7265241, CC ECO:0000305|PubMed:9115986}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305|PubMed:10089353, CC ECO:0000305|PubMed:7265241, ECO:0000305|PubMed:9115986}; CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000250|UniProtKB:P00592}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. CC Note=Secreted from pancreatic acinar cells in its inactive form. CC {ECO:0000250|UniProtKB:P04054}. CC -!- PTM: Activated by trypsin cleavage in the duodenum. Can also be CC activated by thrombin or autocatalytically. CC {ECO:0000250|UniProtKB:P04054}. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y00120; CAA68303.1; -; mRNA. DR PIR; A27508; PSBOA. DR RefSeq; NP_777071.2; NM_174646.3. DR PDB; 1BP2; X-ray; 1.70 A; A=23-145. DR PDB; 1BPQ; X-ray; 1.80 A; A=23-145. DR PDB; 1BVM; NMR; -; A=23-145. DR PDB; 1C74; X-ray; 1.90 A; A=23-145. DR PDB; 1CEH; X-ray; 1.90 A; A=23-145. DR PDB; 1FDK; X-ray; 1.91 A; A=23-145. DR PDB; 1G4I; X-ray; 0.97 A; A=23-145. DR PDB; 1GH4; X-ray; 1.90 A; A=23-145. DR PDB; 1IRB; X-ray; 1.90 A; A=23-145. DR PDB; 1KVW; X-ray; 1.95 A; A=23-145. DR PDB; 1KVX; X-ray; 1.90 A; A=23-145. DR PDB; 1KVY; X-ray; 1.90 A; A=23-145. DR PDB; 1MKS; X-ray; 1.90 A; A=23-145. DR PDB; 1MKT; X-ray; 1.72 A; A=23-145. DR PDB; 1MKU; X-ray; 1.80 A; A=23-145. DR PDB; 1MKV; X-ray; 1.89 A; A=23-145. DR PDB; 1O2E; X-ray; 2.60 A; A=23-145. DR PDB; 1O3W; X-ray; 1.85 A; A=23-145. DR PDB; 1UNE; X-ray; 1.50 A; A=23-145. DR PDB; 1VKQ; X-ray; 1.60 A; A=23-145. DR PDB; 1VL9; X-ray; 0.97 A; A=23-145. DR PDB; 2B96; X-ray; 1.70 A; A=23-145. DR PDB; 2BAX; X-ray; 1.10 A; A=23-145. DR PDB; 2BCH; X-ray; 1.10 A; A=23-145. DR PDB; 2BD1; X-ray; 1.90 A; A/B=23-145. DR PDB; 2BP2; X-ray; 3.00 A; A=16-145. DR PDB; 2BPP; X-ray; 1.80 A; A=23-145. DR PDB; 2ZP3; X-ray; 1.90 A; A=23-145. DR PDB; 2ZP4; X-ray; 1.90 A; A=23-145. DR PDB; 2ZP5; X-ray; 1.90 A; A=23-145. DR PDB; 3BP2; X-ray; 2.10 A; A=24-145. DR PDB; 4BP2; X-ray; 1.60 A; A=16-145. DR AlphaFoldDB; P00593; -. DR PCDDB; P00593; -. DR SMR; P00593; -. DR FunCoup; P00593; 248. DR STRING; 9913.ENSBTAP00000037960; -. DR ChEMBL; CHEMBL5710; -. DR PaxDb; 9913-ENSBTAP00000037960; -. DR Ensembl; ENSBTAT00000038144.4; ENSBTAP00000037960.4; ENSBTAG00000026732.6. DR Ensembl; ENSBTAT00085079569; ENSBTAP00085003146; ENSBTAG00085008291. DR Ensembl; ENSBTAT00090055020; ENSBTAP00090028636; ENSBTAG00090026169. DR GeneID; 282457; -. DR KEGG; bta:282457; -. DR CTD; 5319; -. DR VEuPathDB; HostDB:ENSBTAG00000026732; -. DR VGNC; VGNC:106868; PLA2G1B. DR eggNOG; KOG4087; Eukaryota. DR GeneTree; ENSGT00940000154885; -. DR HOGENOM; CLU_2579890_0_0_1; -. DR InParanoid; P00593; -. DR OMA; CEAFLCN; -. DR OrthoDB; 5841574at2759; -. DR BRENDA; 3.1.1.4; 908. DR Reactome; R-BTA-1482788; Acyl chain remodelling of PC. DR Reactome; R-BTA-1482801; Acyl chain remodelling of PS. DR Reactome; R-BTA-1482839; Acyl chain remodelling of PE. DR Reactome; R-BTA-1482922; Acyl chain remodelling of PI. DR Reactome; R-BTA-1482925; Acyl chain remodelling of PG. DR Reactome; R-BTA-1483166; Synthesis of PA. DR EvolutionaryTrace; P00593; -. DR PRO; PR:P00593; -. DR Proteomes; UP000009136; Chromosome 17. DR Bgee; ENSBTAG00000026732; Expressed in dorsal thalamus and 59 other cell types or tissues. DR ExpressionAtlas; P00593; baseline. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0004623; F:A2-type glycerophospholipase activity; ISS:UniProtKB. DR GO; GO:0032052; F:bile acid binding; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0019731; P:antibacterial humoral response; IEA:Ensembl. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl. DR GO; GO:0050482; P:arachidonate secretion; IEA:InterPro. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:Ensembl. DR GO; GO:0002227; P:innate immune response in mucosa; IEA:Ensembl. DR GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central. DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISS:UniProtKB. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl. DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; ISS:UniProtKB. DR CDD; cd00125; PLA2c; 1. DR FunFam; 1.20.90.10:FF:000011; Phospholipase A(2); 1. DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1. DR InterPro; IPR001211; PLA2. DR InterPro; IPR016090; PLA2-like_dom. DR InterPro; IPR033112; PLA2_Asp_AS. DR InterPro; IPR033113; PLA2_histidine. DR InterPro; IPR036444; PLipase_A2_dom_sf. DR PANTHER; PTHR11716:SF94; PHOSPHOLIPASE A2; 1. DR PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1. DR PROSITE; PS00119; PA2_ASP; 1. DR PROSITE; PS00118; PA2_HIS; 1. DR PDBsum; 1BP2; -. DR PDBsum; 1BPQ; -. DR PDBsum; 1BVM; -. DR PDBsum; 1C74; -. DR PDBsum; 1CEH; -. DR PDBsum; 1FDK; -. DR PDBsum; 1G4I; -. DR PDBsum; 1GH4; -. DR PDBsum; 1IRB; -. DR PDBsum; 1KVW; -. DR PDBsum; 1KVX; -. DR PDBsum; 1KVY; -. DR PDBsum; 1MKS; -. DR PDBsum; 1MKT; -. DR PDBsum; 1MKU; -. DR PDBsum; 1MKV; -. DR PDBsum; 1O2E; -. DR PDBsum; 1O3W; -. DR PDBsum; 1UNE; -. DR PDBsum; 1VKQ; -. DR PDBsum; 1VL9; -. DR PDBsum; 2B96; -. DR PDBsum; 2BAX; -. DR PDBsum; 2BCH; -. DR PDBsum; 2BD1; -. DR PDBsum; 2BP2; -. DR PDBsum; 2BPP; -. DR PDBsum; 2ZP3; -. DR PDBsum; 2ZP4; -. DR PDBsum; 2ZP5; -. DR PDBsum; 3BP2; -. DR PDBsum; 4BP2; -. PE 1: Evidence at protein level; KW 3D-structure; Autocatalytic cleavage; Calcium; Direct protein sequencing; KW Disulfide bond; Hydrolase; Lipid metabolism; Metal-binding; KW Phospholipid metabolism; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal; Zymogen. FT SIGNAL 1..15 FT /evidence="ECO:0000269|Ref.2" FT PROPEP 16..22 FT /note="Removed by trypsin" FT /evidence="ECO:0000269|PubMed:620674" FT /id="PRO_0000022731" FT CHAIN 23..145 FT /note="Phospholipase A2" FT /evidence="ECO:0000269|PubMed:620674" FT /id="PRO_0000022732" FT ACT_SITE 70 FT /evidence="ECO:0000269|PubMed:7464926" FT ACT_SITE 121 FT /evidence="ECO:0000269|PubMed:7464926" FT BINDING 50 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, FT ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, FT ECO:0007744|PDB:1MKS" FT BINDING 52 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, FT ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, FT ECO:0007744|PDB:1MKS" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, FT ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, FT ECO:0007744|PDB:1MKS" FT BINDING 71 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, FT ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, FT ECO:0007744|PDB:1MKS" FT MOD_RES 16 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|Ref.2" FT DISULFID 33..99 FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:712836, ECO:0000269|PubMed:7265241, FT ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, FT ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS" FT DISULFID 49..145 FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:712836, ECO:0000269|PubMed:7265241, FT ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, FT ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS" FT DISULFID 51..67 FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:712836, ECO:0000269|PubMed:7265241, FT ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, FT ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS" FT DISULFID 66..127 FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:712836, ECO:0000269|PubMed:7265241, FT ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, FT ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS" FT DISULFID 73..120 FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:712836, ECO:0000269|PubMed:7265241, FT ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, FT ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS" FT DISULFID 83..113 FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:712836, ECO:0000269|PubMed:7265241, FT ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, FT ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS" FT DISULFID 106..118 FT /evidence="ECO:0000269|PubMed:10089353, FT ECO:0000269|PubMed:712836, ECO:0000269|PubMed:7265241, FT ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, FT ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS" FT CONFLICT 144 FT /note="N -> K (in Ref. 1; CAA68303)" FT /evidence="ECO:0000305" FT HELIX 24..34 FT /evidence="ECO:0007829|PDB:1G4I" FT HELIX 40..43 FT /evidence="ECO:0007829|PDB:1G4I" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:1G4I" FT TURN 48..50 FT /evidence="ECO:0007829|PDB:1G4I" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:1G4I" FT HELIX 62..79 FT /evidence="ECO:0007829|PDB:1G4I" FT HELIX 81..85 FT /evidence="ECO:0007829|PDB:1G4I" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:2BAX" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:1G4I" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:1G4I" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:1G4I" FT HELIX 112..129 FT /evidence="ECO:0007829|PDB:1G4I" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:1G4I" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:1G4I" SQ SEQUENCE 145 AA; 16002 MW; 17A1E04B0C22F668 CRC64; MRLLVLAALL TVGAGQAGLN SRALWQFNGM IKCKIPSSEP LLDFNNYGCY CGLGGSGTPV DDLDRCCQTH DNCYKQAKKL DSCKVLVDNP YTNNYSYSCS NNEITCSSEN NACEAFICNC DRNAAICFSK VPYNKEHKNL DKKNC //