PA21B_BOVIN
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 03-AUG-2022, entry version 184.
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 + H(+) + tetradecanoate;
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 + H(+) + hexadecanoate;
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 = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + 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 = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, 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 = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + 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=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
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 = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + 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=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) +
CC N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine;
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}.
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DR EMBL; Y00120; CAA68303.1; -; mRNA.
DR PIR; A27508; PSBOA.
DR RefSeq; NP_777071.2; NM_174646.3.
DR RefSeq; XP_010812367.1; XM_010814065.2.
DR RefSeq; XP_015322603.1; XM_015467117.1.
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=17-145.
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 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; -.
DR AlphaFoldDB; P00593; -.
DR PCDDB; P00593; -.
DR SMR; P00593; -.
DR STRING; 9913.ENSBTAP00000037960; -.
DR ChEMBL; CHEMBL5710; -.
DR PaxDb; P00593; -.
DR Ensembl; ENSBTAT00000038144; ENSBTAP00000037960; ENSBTAG00000026732.
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; ELDTCCQ; -.
DR OrthoDB; 1422829at2759; -.
DR BRENDA; 3.1.1.4; 908.
DR EvolutionaryTrace; P00593; -.
DR PRO; PR:P00593; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000026732; Expressed in dorsal thalamus and 59 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0032052; F:bile acid binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISS:UniProtKB.
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:arachidonic acid 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; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IBA:GO_Central.
DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; ISS:UniProtKB.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
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:1FDK"
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
