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Alkaline phosphatase, placental type (EC 3.1.3.1) (Alkaline phosphatase Regan isozyme) (Placental alkaline phosphatase 1) (PLAP-1)

 PPB1_HUMAN              Reviewed;         535 AA.
P05187; P05188; P06861; Q53S78; Q96DB7;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
30-AUG-2017, entry version 196.
RecName: Full=Alkaline phosphatase, placental type;
EC=3.1.3.1;
AltName: Full=Alkaline phosphatase Regan isozyme;
AltName: Full=Placental alkaline phosphatase 1;
Short=PLAP-1;
Flags: Precursor;
Name=ALPP; Synonyms=PLAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3042787;
Knoll B.J., Rothblum K.N., Longley M.A.;
"Nucleotide sequence of the human placental alkaline phosphatase gene.
Evolution of the 5' flanking region by deletion/substitution.";
J. Biol. Chem. 263:12020-12027(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-231.
PubMed=3512548;
Millan J.L.;
"Molecular cloning and sequence analysis of human placental alkaline
phosphatase.";
J. Biol. Chem. 261:3112-3115(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS LEU-25
AND HIS-263, AND POLYMORPHISM.
PubMed=3461452; DOI=10.1073/pnas.83.15.5597;
Henthorn P.S., Knoll B.J., Raducha M., Rothblum K.N., Slaughter C.,
Weiss M., Lafferty M.A., Fischer T., Harris H.;
"Products of two common alleles at the locus for human placental
alkaline phosphatase differ by seven amino acids.";
Proc. Natl. Acad. Sci. U.S.A. 83:5597-5601(1986).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-89.
TISSUE=Cervix, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-535, AND VARIANT LEU-25.
PubMed=3001717; DOI=10.1073/pnas.82.24.8715;
Kam W., Clauser E., Kim Y.S., Kan Y.W., Rutter W.J.;
"Cloning, sequencing, and chromosomal localization of human term
placental alkaline phosphatase cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 82:8715-8719(1985).
[7]
PROTEIN SEQUENCE OF 23-64.
PubMed=6651840; DOI=10.1016/S0006-291X(83)80252-6;
Ezra E., Blacher R., Udenfriend S.;
"Purification and partial sequencing of human placental alkaline
phosphatase.";
Biochem. Biophys. Res. Commun. 116:1076-1083(1983).
[8]
NUCLEOTIDE SEQUENCE OF 382-535.
PubMed=3459156; DOI=10.1073/pnas.83.11.3781;
Ovitt C.E., Strauss A.W., Alpers D.H., Chou J.Y., Boime I.;
"Expression of different-sized placental alkaline phosphatase mRNAs in
placenta and choriocarcinoma cells.";
Proc. Natl. Acad. Sci. U.S.A. 83:3781-3785(1986).
[9]
PROTEIN SEQUENCE OF 485-535.
PubMed=3422741; DOI=10.1073/pnas.85.5.1398;
Micanovic R., Bailey C.A., Brink L., Gerber L., Pan Y.C.E.,
Hulmes J.D., Udenfriend S.;
"Aspartic acid-484 of nascent placental alkaline phosphatase condenses
with a phosphatidylinositol glycan to become the carboxyl terminus of
the mature enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 85:1398-1402(1988).
[10]
GPI-ANCHOR AT ASP-506.
PubMed=2153284; DOI=10.1073/pnas.87.1.157;
Micanovic R., Gerber L.D., Berger J., Kodukula K., Udenfriend S.;
"Selectivity of the cleavage/attachment site of phosphatidylinositol-
glycan-anchored membrane proteins determined by site-specific
mutagenesis at Asp-484 of placental alkaline phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 87:157-161(1990).
[11]
EFFECT OF MUTAGENESIS OF C-TERMINAL PEPTIDE ON GPI-ANCHORING.
PubMed=1730777; DOI=10.1083/jcb.116.3.799;
Lowe M.E.;
"Site-specific mutations in the COOH-terminus of placental alkaline
phosphatase: a single amino acid change converts a
phosphatidylinositol-glycan-anchored protein to a secreted protein.";
J. Cell Biol. 116:799-807(1992).
[12]
DISULFIDE BONDS.
PubMed=11937510; DOI=10.1074/jbc.M202298200;
Kozlenkov A., Manes T., Hoylaerts M.F., Millan J.L.;
"Function assignment to conserved residues in mammalian alkaline
phosphatases.";
J. Biol. Chem. 277:22992-22999(2002).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 23-535 IN COMPLEX WITH
MAGNESIUM AND ZINC, COFACTOR, DISULFIDE BOND, AND SUBUNIT.
PubMed=11124260; DOI=10.1074/jbc.M009250200;
Le Du M.H., Stigbrand T., Taussig M.J., Menez A., Stura E.A.;
"Crystal structure of alkaline phosphatase from human placenta at 1.8
A resolution. Implication for a substrate specificity.";
J. Biol. Chem. 276:9158-9165(2001).
[15]
X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 23-506 IN COMPLEX WITH
MAGNESIUM AND ZINC, GLYCOSYLATION AT ASN-144 AND ASN-271, COFACTOR,
DISULFIDE BOND, AND SUBUNIT.
PubMed=15946677; DOI=10.1016/j.jmb.2005.04.068;
Llinas P., Stura E.A., Menez A., Kiss Z., Stigbrand T., Millan J.L.,
Le Du M.H.;
"Structural studies of human placental alkaline phosphatase in complex
with functional ligands.";
J. Mol. Biol. 350:441-451(2005).
[16]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 23-506 IN COMPLEX WITH
MAGNESIUM AND ZINC, GLYCOSYLATION AT ASN-144 AND ASN-271, COFACTOR,
DISULFIDE BOND, AND SUBUNIT.
PubMed=16815919; DOI=10.1110/ps.062123806;
Llinas P., Masella M., Stigbrand T., Menez A., Stura E.A., Le Du M.H.;
"Structural studies of human alkaline phosphatase in complex with
strontium: implication for its secondary effect in bones.";
Protein Sci. 15:1691-1700(2006).
[17]
X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 23-506 IN COMPLEX WITH
MAGNESIUM AND ZINC, GLYCOSYLATION AT ASN-144 AND ASN-271, COFACTOR,
DISULFIDE BOND, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=20693656; DOI=10.1107/S1744309110019767;
Stec B., Cheltsov A., Millan J.L.;
"Refined structures of placental alkaline phosphatase show a
consistent pattern of interactions at the peripheral site.";
Acta Crystallogr. F 66:866-870(2010).
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677, ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656};
Note=Binds 1 Mg(2+) ion. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677, ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677, ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656};
Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677, ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677, ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
-!- INTERACTION:
P49639:HOXA1; NbExp=4; IntAct=EBI-1211484, EBI-740785;
Q07627:KRTAP1-1; NbExp=4; IntAct=EBI-1211484, EBI-11959885;
Q9BQ66:KRTAP4-12; NbExp=3; IntAct=EBI-1211484, EBI-739863;
P26371:KRTAP5-9; NbExp=5; IntAct=EBI-1211484, EBI-3958099;
Q5TCM9:LCE5A; NbExp=4; IntAct=EBI-1211484, EBI-11955689;
P32242:OTX1; NbExp=4; IntAct=EBI-1211484, EBI-740446;
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- TISSUE SPECIFICITY: Detected in placenta (at protein level).
{ECO:0000269|PubMed:20693656}.
-!- POLYMORPHISM: Placental ALP is highly polymorphic, there are at
least three common alleles. {ECO:0000269|PubMed:3461452}.
-!- MISCELLANEOUS: In most mammals there are four different isozymes:
placental, placental-like, intestinal and tissue non-specific
(liver/bone/kidney).
-!- SIMILARITY: Belongs to the alkaline phosphatase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA51708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Alkaline phosphatase entry;
URL="https://en.wikipedia.org/wiki/Alkaline_phosphatase";
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EMBL; M19159; AAA51710.1; -; Genomic_DNA.
EMBL; M13077; AAC97139.1; -; mRNA.
EMBL; M14169; AAA51708.1; ALT_INIT; mRNA.
EMBL; M14170; AAA51709.1; -; mRNA.
EMBL; AC068134; AAY24087.1; -; Genomic_DNA.
EMBL; BC009647; AAH09647.1; -; mRNA.
EMBL; BC068501; AAH68501.1; -; mRNA.
EMBL; BC094743; AAH94743.1; -; mRNA.
EMBL; M12551; AAA51706.1; -; mRNA.
CCDS; CCDS2490.1; -.
PIR; A31074; PAHUA.
RefSeq; NP_001623.3; NM_001632.4.
UniGene; Hs.284255; -.
PDB; 1EW2; X-ray; 1.82 A; A=23-535.
PDB; 1ZEB; X-ray; 1.90 A; A=23-506.
PDB; 1ZED; X-ray; 1.57 A; A=23-506.
PDB; 1ZEF; X-ray; 1.90 A; A=23-506.
PDB; 2GLQ; X-ray; 1.60 A; A=23-506.
PDB; 3MK0; X-ray; 1.90 A; A=23-506.
PDB; 3MK1; X-ray; 1.57 A; A=23-506.
PDB; 3MK2; X-ray; 1.89 A; A=23-503.
PDBsum; 1EW2; -.
PDBsum; 1ZEB; -.
PDBsum; 1ZED; -.
PDBsum; 1ZEF; -.
PDBsum; 2GLQ; -.
PDBsum; 3MK0; -.
PDBsum; 3MK1; -.
PDBsum; 3MK2; -.
ProteinModelPortal; P05187; -.
SMR; P05187; -.
BioGrid; 106751; 26.
IntAct; P05187; 38.
MINT; MINT-4054397; -.
STRING; 9606.ENSP00000375881; -.
BindingDB; P05187; -.
ChEMBL; CHEMBL4458; -.
DrugBank; DB08413; METHYL-PHOSPHONIC ACID MONO-(4-NITRO-PHENYL) ESTER.
DEPOD; P05187; -.
iPTMnet; P05187; -.
PhosphoSitePlus; P05187; -.
BioMuta; ALPP; -.
DMDM; 130737; -.
EPD; P05187; -.
MaxQB; P05187; -.
PaxDb; P05187; -.
PeptideAtlas; P05187; -.
PRIDE; P05187; -.
DNASU; 250; -.
Ensembl; ENST00000392027; ENSP00000375881; ENSG00000163283.
GeneID; 250; -.
KEGG; hsa:250; -.
UCSC; uc002vsq.4; human.
CTD; 250; -.
DisGeNET; 250; -.
GeneCards; ALPP; -.
HGNC; HGNC:439; ALPP.
HPA; CAB026327; -.
HPA; HPA038764; -.
HPA; HPA038765; -.
HPA; HPA051699; -.
MIM; 171800; gene.
neXtProt; NX_P05187; -.
OpenTargets; ENSG00000163283; -.
PharmGKB; PA24730; -.
eggNOG; KOG4126; Eukaryota.
eggNOG; COG1785; LUCA.
GeneTree; ENSGT00390000008704; -.
HOGENOM; HOG000099118; -.
HOVERGEN; HBG007345; -.
InParanoid; P05187; -.
KO; K01077; -.
OMA; MFRMGTP; -.
OrthoDB; EOG091G067H; -.
PhylomeDB; P05187; -.
TreeFam; TF323513; -.
BRENDA; 3.1.3.1; 2681.
Reactome; R-HSA-6811438; Intra-Golgi traffic.
SABIO-RK; P05187; -.
ChiTaRS; ALPP; human.
EvolutionaryTrace; P05187; -.
GeneWiki; Placental_alkaline_phosphatase; -.
GenomeRNAi; 250; -.
PRO; PR:P05187; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163283; -.
CleanEx; HS_ALPP; -.
Genevisible; P05187; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0004035; F:alkaline phosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
CDD; cd16012; ALP; 1.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR001952; Alkaline_phosphatase.
InterPro; IPR018299; Alkaline_phosphatase_AS.
InterPro; IPR017850; Alkaline_phosphatase_core.
PANTHER; PTHR11596; PTHR11596; 1.
Pfam; PF00245; Alk_phosphatase; 1.
PRINTS; PR00113; ALKPHPHTASE.
SMART; SM00098; alkPPc; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
Polymorphism; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Zinc.
SIGNAL 1 22 {ECO:0000269|PubMed:6651840}.
CHAIN 23 506 Alkaline phosphatase, placental type.
/FTId=PRO_0000024031.
PROPEP 507 535 Removed in mature form.
/FTId=PRO_0000024032.
TRANSMEM 513 529 Helical.
ACT_SITE 114 114 Phosphoserine intermediate.
METAL 64 64 Magnesium. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
METAL 64 64 Zinc 1. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
METAL 114 114 Zinc 1. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
METAL 177 177 Magnesium. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
METAL 333 333 Magnesium. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
METAL 338 338 Zinc 2. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
METAL 342 342 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
METAL 379 379 Zinc 1. {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
METAL 380 380 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
METAL 454 454 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
LIPID 506 506 GPI-anchor amidated aspartate.
{ECO:0000269|PubMed:2153284}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
DISULFID 143 205 {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:11937510,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
DISULFID 489 496 {ECO:0000269|PubMed:11124260,
ECO:0000269|PubMed:11937510,
ECO:0000269|PubMed:15946677,
ECO:0000269|PubMed:16815919,
ECO:0000269|PubMed:20693656}.
VARIANT 25 25 P -> L (in dbSNP:rs1130335).
{ECO:0000269|PubMed:3001717,
ECO:0000269|PubMed:3461452}.
/FTId=VAR_017419.
VARIANT 89 89 I -> L (in dbSNP:rs13026692).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_050520.
VARIANT 231 231 R -> P (in dbSNP:rs1048988).
{ECO:0000269|PubMed:3512548}.
/FTId=VAR_050521.
VARIANT 263 263 R -> H (in dbSNP:rs2853378).
{ECO:0000269|PubMed:3461452}.
/FTId=VAR_050522.
VARIANT 451 451 E -> G (in dbSNP:rs1048994).
/FTId=VAR_050523.
CONFLICT 66 66 M -> V (in Ref. 3; AAA51709).
{ECO:0000305}.
CONFLICT 261 262 AK -> GE (in Ref. 6; AAA51706).
{ECO:0000305}.
CONFLICT 277 277 Q -> R (in Ref. 3; AAA51709).
{ECO:0000305}.
CONFLICT 285 285 T -> A (in Ref. 3; AAA51709).
{ECO:0000305}.
CONFLICT 324 324 N -> H (in Ref. 6; AAA51706).
{ECO:0000305}.
CONFLICT 389 389 Y -> C (in Ref. 3; AAA51709).
{ECO:0000305}.
CONFLICT 394 394 S -> G (in Ref. 3; AAA51709).
{ECO:0000305}.
CONFLICT 396 397 IF -> FI (in Ref. 6; AAA51706).
{ECO:0000305}.
CONFLICT 401 401 P -> A (in Ref. 6; AAA51706).
{ECO:0000305}.
CONFLICT 436 436 S -> T (in Ref. 8). {ECO:0000305}.
HELIX 26 29 {ECO:0000244|PDB:1ZED}.
HELIX 31 47 {ECO:0000244|PDB:1ZED}.
STRAND 56 63 {ECO:0000244|PDB:1ZED}.
HELIX 68 81 {ECO:0000244|PDB:1ZED}.
HELIX 93 95 {ECO:0000244|PDB:1ZED}.
STRAND 97 103 {ECO:0000244|PDB:1ZED}.
HELIX 114 123 {ECO:0000244|PDB:1ZED}.
STRAND 132 134 {ECO:0000244|PDB:1ZED}.
HELIX 143 145 {ECO:0000244|PDB:1ZED}.
HELIX 154 160 {ECO:0000244|PDB:1ZED}.
STRAND 164 172 {ECO:0000244|PDB:1ZED}.
HELIX 176 179 {ECO:0000244|PDB:1ZED}.
TURN 180 182 {ECO:0000244|PDB:1ZED}.
HELIX 193 195 {ECO:0000244|PDB:1ZED}.
HELIX 198 202 {ECO:0000244|PDB:1ZED}.
HELIX 208 214 {ECO:0000244|PDB:1ZED}.
STRAND 219 224 {ECO:0000244|PDB:1ZED}.
HELIX 226 229 {ECO:0000244|PDB:1ZED}.
HELIX 243 245 {ECO:0000244|PDB:1ZED}.
STRAND 249 251 {ECO:0000244|PDB:1ZED}.
HELIX 255 261 {ECO:0000244|PDB:1ZED}.
STRAND 266 269 {ECO:0000244|PDB:1ZED}.
HELIX 272 279 {ECO:0000244|PDB:1ZED}.
STRAND 285 290 {ECO:0000244|PDB:1ZED}.
STRAND 292 295 {ECO:0000244|PDB:1ZED}.
HELIX 299 301 {ECO:0000244|PDB:1ZED}.
TURN 304 306 {ECO:0000244|PDB:1ZED}.
HELIX 310 321 {ECO:0000244|PDB:1ZED}.
STRAND 328 334 {ECO:0000244|PDB:1ZED}.
HELIX 337 342 {ECO:0000244|PDB:1ZED}.
HELIX 346 366 {ECO:0000244|PDB:1ZED}.
TURN 369 371 {ECO:0000244|PDB:1ZED}.
STRAND 372 379 {ECO:0000244|PDB:1ZED}.
STRAND 381 386 {ECO:0000244|PDB:1ZED}.
STRAND 411 418 {ECO:0000244|PDB:1ZED}.
HELIX 433 436 {ECO:0000244|PDB:1ZED}.
STRAND 445 447 {ECO:0000244|PDB:1ZED}.
STRAND 459 465 {ECO:0000244|PDB:1ZED}.
HELIX 468 470 {ECO:0000244|PDB:1ZED}.
STRAND 473 476 {ECO:0000244|PDB:1ZED}.
HELIX 479 487 {ECO:0000244|PDB:1ZED}.
HELIX 491 493 {ECO:0000244|PDB:1ZED}.
SEQUENCE 535 AA; 57954 MW; 13C136679A70C76B CRC64;
MLGPCMLLLL LLLGLRLQLS LGIIPVEEEN PDFWNREAAE ALGAAKKLQP AQTAAKNLII
FLGDGMGVST VTAARILKGQ KKDKLGPEIP LAMDRFPYVA LSKTYNVDKH VPDSGATATA
YLCGVKGNFQ TIGLSAAARF NQCNTTRGNE VISVMNRAKK AGKSVGVVTT TRVQHASPAG
TYAHTVNRNW YSDADVPASA RQEGCQDIAT QLISNMDIDV ILGGGRKYMF RMGTPDPEYP
DDYSQGGTRL DGKNLVQEWL AKRQGARYVW NRTELMQASL DPSVTHLMGL FEPGDMKYEI
HRDSTLDPSL MEMTEAALRL LSRNPRGFFL FVEGGRIDHG HHESRAYRAL TETIMFDDAI
ERAGQLTSEE DTLSLVTADH SHVFSFGGYP LRGSSIFGLA PGKARDRKAY TVLLYGNGPG
YVLKDGARPD VTESESGSPE YRQQSAVPLD EETHAGEDVA VFARGPQAHL VHGVQEQTFI
AHVMAFAACL EPYTACDLAP PAGTTDAAHP GRSVVPALLP LLAGTLLLLE TATAP


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