ID   PPBT_BOVIN              Reviewed;         524 AA.
AC   P09487; Q17QS5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Alkaline phosphatase, tissue-nonspecific isozyme {ECO:0000303|PubMed:19098289};
DE            Short=AP-TNAP;
DE            Short=TNAP {ECO:0000303|PubMed:19098289};
DE            Short=TNSALP;
DE            EC=3.1.3.1 {ECO:0000250|UniProtKB:P05186};
DE   AltName: Full=Alkaline phosphatase liver/bone/kidney isozyme;
DE   AltName: Full=Phosphoamidase {ECO:0000305};
DE   AltName: Full=Phosphocreatine phosphatase {ECO:0000250|UniProtKB:P09242};
DE            EC=3.9.1.1 {ECO:0000250|UniProtKB:P09242};
DE   Flags: Precursor;
GN   Name=ALPL;
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=3436527; DOI=10.1016/0378-1119(87)90264-2;
RA   Garattini E., Hua J.-C., Udenfriend S.;
RT   "Cloning and sequencing of bovine kidney alkaline phosphatase cDNA.";
RL   Gene 59:41-46(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 18-50.
RX   PubMed=3458202; DOI=10.1073/pnas.83.8.2368;
RA   Hua J.-C., Berger J., Pan Y.C.E., Hulmes J.D., Udenfriend S.;
RT   "Partial sequencing of human adult, human fetal, and bovine intestinal
RT   alkaline phosphatases: comparison with the human placental and liver
RT   isozymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:2368-2372(1986).
RN   [4]
RP   FUNCTION.
RX   PubMed=19098289; DOI=10.1074/jbc.m803205200;
RA   Price P.A., Toroian D., Chan W.S.;
RT   "Tissue-nonspecific alkaline phosphatase is required for the calcification
RT   of collagen in serum: a possible mechanism for biomineralization.";
RL   J. Biol. Chem. 284:4594-4604(2009).
CC   -!- FUNCTION: Alkaline phosphatase that metabolizes various phosphate
CC       compounds and plays a key role in skeletal mineralization and adaptive
CC       thermogenesis (By similarity). Has broad substrate specificity and can
CC       hydrolyze a considerable variety of compounds: however, only a few
CC       substrates, such as diphosphate (inorganic pyrophosphate; PPi),
CC       pyridoxal 5'-phosphate (PLP) and N-phosphocreatine are natural
CC       substrates (By similarity). Plays an essential role in skeletal and
CC       dental mineralization via its ability to hydrolyze extracellular
CC       diphosphate, a potent mineralization inhibitor, to phosphate: it
CC       thereby promotes hydroxyapatite crystal formation and increases
CC       inorganic phosphate concentration (PubMed:19098289). Acts in a non-
CC       redundant manner with PHOSPHO1 in skeletal mineralization: while
CC       PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in
CC       the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of
CC       hydroxyapatite crystallization in the extracellular matrix (By
CC       similarity). Also promotes dephosphorylation of osteopontin (SSP1), an
CC       inhibitor of hydroxyapatite crystallization in its phosphorylated
CC       state; it is however unclear whether ALPL/TNAP mediates SSP1
CC       dephosphorylation via a direct or indirect manner (By similarity).
CC       Catalyzes dephosphorylation of PLP to pyridoxal (PL), the transportable
CC       form of vitamin B6, in order to provide a sufficient amount of PLP in
CC       the brain, an essential cofactor for enzymes catalyzing the synthesis
CC       of diverse neurotransmitters (By similarity). Additionally, also able
CC       to mediate ATP degradation in a stepwise manner to adenosine, thereby
CC       regulating the availability of ligands for purinergic receptors (By
CC       similarity). Also capable of dephosphorylating microbial products, such
CC       as lipopolysaccharides (LPS) as well as other phosphorylated small-
CC       molecules, such as poly-inosine:cytosine (poly I:C) (By similarity).
CC       Acts as a key regulator of adaptive thermogenesis as part of the futile
CC       creatine cycle: localizes to the mitochondria of thermogenic fat cells
CC       and acts by mediating hydrolysis of N-phosphocreatine to initiate a
CC       futile cycle of creatine dephosphorylation and phosphorylation (By
CC       similarity). During the futile creatine cycle, creatine and N-
CC       phosphocreatine are in a futile cycle, which dissipates the high energy
CC       charge of N-phosphocreatine as heat without performing any mechanical
CC       or chemical work (By similarity). {ECO:0000250|UniProtKB:P05186,
CC       ECO:0000250|UniProtKB:P09242, ECO:0000269|PubMed:19098289}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC         Evidence={ECO:0000250|UniProtKB:P09242, ECO:0000255|PROSITE-
CC         ProRule:PRU10042};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC         Evidence={ECO:0000250|UniProtKB:P09242};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:P09242};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577;
CC         Evidence={ECO:0000250|UniProtKB:P09242};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal;
CC         Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P05186};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534;
CC         Evidence={ECO:0000250|UniProtKB:P05186};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + phosphoethanolamine = ethanolamine + phosphate;
CC         Xref=Rhea:RHEA:16089, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57603, ChEBI:CHEBI:58190;
CC         Evidence={ECO:0000250|UniProtKB:P05186};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16090;
CC         Evidence={ECO:0000250|UniProtKB:P05186};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-phosphocreatine = creatine + phosphate;
CC         Xref=Rhea:RHEA:12977, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57947, ChEBI:CHEBI:58092; EC=3.9.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P09242};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12978;
CC         Evidence={ECO:0000250|UniProtKB:P09242};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P09242};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:P09242};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P09242};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC         Evidence={ECO:0000250|UniProtKB:P09242};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + H2O = adenosine + phosphate; Xref=Rhea:RHEA:29375,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P09242};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29376;
CC         Evidence={ECO:0000250|UniProtKB:P09242};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P05187};
CC       Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P05187};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P05187};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P05187};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P05186};
CC   -!- ACTIVITY REGULATION: Phosphatase activity is specifically inhibited by
CC       5-((5-chloro-2-methoxyphenyl)sulfonamido)nicotinamide (SBI-425).
CC       {ECO:0000250|UniProtKB:P09242}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P05186}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05186};
CC       Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P05186}. Extracellular
CC       vesicle membrane {ECO:0000250|UniProtKB:P09242}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250|UniProtKB:P09242}. Mitochondrion membrane
CC       {ECO:0000250|UniProtKB:P09242}; Lipid-anchor, GPI-anchor
CC       {ECO:0000250|UniProtKB:P09242}. Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:P09242}. Note=Localizes to special class of
CC       extracellular vesicles, named matrix vesicles (MVs), which are released
CC       by osteogenic cells. Localizes to the mitochondria of thermogenic fat
CC       cells: tethered to mitochondrial membranes via a GPI-anchor and
CC       probably resides in the mitochondrion intermembrane space.
CC       {ECO:0000250|UniProtKB:P09242}.
CC   -!- DOMAIN: Calcium-binding is structural and does not influence the
CC       alkaline phosphatase activity. At very high concentrations, calcium can
CC       however substitute for zinc at zinc-binding sites, leading to strongly
CC       reduced enzyme activity. {ECO:0000250|UniProtKB:P05186}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P05186}.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR   EMBL; M18443; AAA30380.1; -; mRNA.
DR   EMBL; BC118208; AAI18209.1; -; mRNA.
DR   PIR; A29600; A29600.
DR   RefSeq; NP_789828.2; NM_176858.2.
DR   AlphaFoldDB; P09487; -.
DR   SMR; P09487; -.
DR   STRING; 9913.ENSBTAP00000067523; -.
DR   BindingDB; P09487; -.
DR   ChEMBL; CHEMBL2406894; -.
DR   DrugCentral; P09487; -.
DR   GlyCosmos; P09487; 5 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000011783; -.
DR   Ensembl; ENSBTAT00000011783.6; ENSBTAP00000011783.5; ENSBTAG00000008951.6.
DR   Ensembl; ENSBTAT00000066596.1; ENSBTAP00000065772.1; ENSBTAG00000008951.6.
DR   Ensembl; ENSBTAT00000071091.1; ENSBTAP00000063499.1; ENSBTAG00000008951.6.
DR   Ensembl; ENSBTAT00000071575.1; ENSBTAP00000067523.1; ENSBTAG00000008951.6.
DR   GeneID; 280994; -.
DR   KEGG; bta:280994; -.
DR   CTD; 249; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008951; -.
DR   VGNC; VGNC:25850; ALPL.
DR   eggNOG; KOG4126; Eukaryota.
DR   GeneTree; ENSGT00950000183063; -.
DR   HOGENOM; CLU_008539_4_0_1; -.
DR   InParanoid; P09487; -.
DR   OMA; LRYETHG; -.
DR   TreeFam; TF323513; -.
DR   BRENDA; 3.1.3.1; 908.
DR   Reactome; R-BTA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   PRO; PR:P09487; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000008951; Expressed in olfactory segment of nasal mucosa and 104 other cell types or tissues.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0065010; C:extracellular membrane-bounded organelle; IDA:AgBase.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043262; F:ADP phosphatase activity; IEA:RHEA.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IDA:MGI.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:RHEA.
DR   GO; GO:0050187; F:phosphoamidase activity; ISS:UniProtKB.
DR   GO; GO:0052732; F:phosphoethanolamine phosphatase activity; IEA:Ensembl.
DR   GO; GO:0033883; F:pyridoxal phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0016462; F:pyrophosphatase activity; ISS:UniProtKB.
DR   GO; GO:0031214; P:biomineral tissue development; IDA:AgBase.
DR   GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
DR   GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0019725; P:cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   GO; GO:0003006; P:developmental process involved in reproduction; IEA:Ensembl.
DR   GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR   GO; GO:0140651; P:futile creatine cycle; IEA:Ensembl.
DR   GO; GO:0140928; P:inhibition of non-skeletal tissue mineralization; IEA:Ensembl.
DR   GO; GO:0055062; P:phosphate ion homeostasis; IEA:Ensembl.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:UniProtKB.
DR   GO; GO:0042822; P:pyridoxal phosphate metabolic process; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:1904383; P:response to sodium phosphate; IEA:Ensembl.
DR   GO; GO:0034516; P:response to vitamin B6; IEA:Ensembl.
DR   GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF74; ALKALINE PHOSPHATASE, TISSUE-NONSPECIFIC ISOZYME; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Biomineralization; Calcium; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
KW   Magnesium; Membrane; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:3458202"
FT   CHAIN           18..499
FT                   /note="Alkaline phosphatase, tissue-nonspecific isozyme"
FT                   /id="PRO_0000024019"
FT   PROPEP          500..524
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000024020"
FT   ACT_SITE        110
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P05187,
FT                   ECO:0000255|PROSITE-ProRule:PRU10042"
FT   BINDING         60
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   BINDING         235
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P05186"
FT   BINDING         290
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P05186"
FT   BINDING         291
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P05186"
FT   BINDING         306
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P05186"
FT   BINDING         332
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   BINDING         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   BINDING         379
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   BINDING         454
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09242"
FT   LIPID           499
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        139..201
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   DISULFID        489..497
FT                   /evidence="ECO:0000250|UniProtKB:P05187"
FT   CONFLICT        210
FT                   /note="H -> Y (in Ref. 1; AAA30380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        475
FT                   /note="H -> Q (in Ref. 1; AAA30380)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   524 AA;  57193 MW;  21A66F10E8ADDFC2 CRC64;
     MISPFLLLAI GTCFASSLVP EKEKDPKYWR DQAQQTLKNA LRLQTLNTNV AKNVIMFLGD
     GMGVSTVTAA RILKGQLHHS PGEETKLEMD KFPYVALSKT YNTNAQVPDS AGTATAYLCG
     VKANEGTVGV SAATQRSQCN TTQGNEVTSI LRWAKDAGKS VGIVTTTRVN HATPSASYAH
     SADRDWYSDN EMPPEALSQG CKDIAYQLMH NIKDIEVIMG GGRKYMFPKN RTDVEYELDE
     KARGTRLDGL NLIDIWKSFK PKHKHSHYVW NRTDLLALDP HSVDYLLGLF EPGDMQYELN
     RNNATDPSLS EMVEMAIRIL NKNPKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDQAIG
     QAGAMTSVED TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MVSDTDKKPF TAILYGNGPG
     YKVVGGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFAKGPMAHL LHGVHEQNYI
     PHVMAYAACI GANRDHCASA SSSGSPSPGP LLLLLALLPL GSLF
//