AMD_BOVIN
ID AMD_BOVIN Reviewed; 972 AA.
AC P10731;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Peptidyl-glycine alpha-amidating monooxygenase {ECO:0000250|UniProtKB:P19021};
DE Short=PAM {ECO:0000303|PubMed:2059626};
DE Includes:
DE RecName: Full=Peptidylglycine alpha-hydroxylating monooxygenase {ECO:0000250|UniProtKB:P19021};
DE Short=PHM {ECO:0000250|UniProtKB:P19021};
DE EC=1.14.17.3 {ECO:0000269|PubMed:2059626};
DE Includes:
DE RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase;
DE EC=4.3.2.5 {ECO:0000269|PubMed:2059626};
DE AltName: Full=Peptidylamidoglycolate lyase {ECO:0000250|UniProtKB:P19021};
DE Short=PAL {ECO:0000250|UniProtKB:P19021};
DE Flags: Precursor;
GN Name=PAM;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Pituitary;
RX PubMed=3153462; DOI=10.1210/mend-1-11-777;
RA Eipper B.A., Park L.P., Dickerson I.M., Keutmann H.T., Thiele E.A.,
RA Rodriguez H., Schofield P.R., Mains R.E.;
RT "Structure of the precursor to an enzyme mediating COOH-terminal amidation
RT in peptide biosynthesis.";
RL Mol. Endocrinol. 1:777-790(1987).
RN [2]
RP PROTEIN SEQUENCE OF 478-499; 544-575; 611-630 AND 665-695, FUNCTION,
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=2059626; DOI=10.1021/bi00239a016;
RA Katopodis A.G., Ping D.S., Smith C.E., May S.W.;
RT "Functional and structural characterization of peptidylamidoglycolate
RT lyase, the enzyme catalyzing the second step in peptide amidation.";
RL Biochemistry 30:6189-6194(1991).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the post-translational
CC modification of inactive peptidylglycine precursors to the
CC corresponding bioactive alpha-amidated peptides, a terminal
CC modification in biosynthesis of many neural and endocrine peptides
CC (PubMed:2059626). Alpha-amidation involves two sequential reactions,
CC both of which are catalyzed by separate catalytic domains of the
CC enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating
CC monooxygenase (PHM) domain, is the copper-, ascorbate-, and
CC O2- dependent stereospecific hydroxylation (with S stereochemistry) at
CC the alpha-carbon (C-alpha) of the C-terminal glycine of the
CC peptidylglycine substrate (PubMed:2059626). The second step, catalyzed
CC by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-
CC dependent cleavage of the N-C-alpha bond, producing the alpha-amidated
CC peptide and glyoxylate (PubMed:2059626). Similarly, catalyzes the two-
CC step conversion of an N-fatty acylglycine to a primary fatty acid amide
CC and glyoxylate (By similarity). {ECO:0000250|UniProtKB:P14925,
CC ECO:0000269|PubMed:2059626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a
CC [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-
CC ascorbate radical; Xref=Rhea:RHEA:21452, Rhea:RHEA-COMP:13486,
CC Rhea:RHEA-COMP:15321, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:137000,
CC ChEBI:CHEBI:142768; EC=1.14.17.3;
CC Evidence={ECO:0000269|PubMed:2059626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-
CC terminal amide + glyoxylate; Xref=Rhea:RHEA:20924, Rhea:RHEA-
CC COMP:13485, Rhea:RHEA-COMP:15321, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:137001, ChEBI:CHEBI:142768; EC=4.3.2.5;
CC Evidence={ECO:0000269|PubMed:2059626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-dodecanoylglycine + O2 = H2O + 2
CC monodehydro-L-ascorbate radical + N-dodecanoyl-(2S)-hydroxyglycine;
CC Xref=Rhea:RHEA:58540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:142678,
CC ChEBI:CHEBI:142693; Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-dodecanoyl-(2S)-hydroxyglycine = dodecanamide + glyoxylate;
CC Xref=Rhea:RHEA:58624, ChEBI:CHEBI:34726, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:142693; Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-(9Z,12Z,15Z)-octadecatrienoylglycine + O2 =
CC H2O + 2 monodehydro-L-ascorbate radical + N-(9Z,12Z,15Z)-
CC octadecatrienoyl-(2S)-hydroxyglycine; Xref=Rhea:RHEA:58548,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:59513, ChEBI:CHEBI:142679, ChEBI:CHEBI:142697;
CC Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(9Z,12Z,15Z)-octadecatrienoyl-(2S)-hydroxyglycine =
CC (9Z,12Z,15Z)-octadecatrienamide + glyoxylate; Xref=Rhea:RHEA:58644,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:142684, ChEBI:CHEBI:142697;
CC Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-(9Z-octadecenoyl)glycine + O2 = H2O + 2
CC monodehydro-L-ascorbate radical + N-(9Z-octadecenoyl)-(2S)-
CC hydroxyglycine; Xref=Rhea:RHEA:58600, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513,
CC ChEBI:CHEBI:133992, ChEBI:CHEBI:142696;
CC Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(9Z-octadecenoyl)-(2S)-hydroxyglycine = (9Z)-octadecenamide
CC + glyoxylate; Xref=Rhea:RHEA:58636, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:116314, ChEBI:CHEBI:142696;
CC Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-tetradecanoylglycine + O2 = H2O + 2
CC monodehydro-L-ascorbate radical + N-tetradecanoyl-(2S)-
CC hydroxyglycine; Xref=Rhea:RHEA:58544, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513,
CC ChEBI:CHEBI:86500, ChEBI:CHEBI:142694;
CC Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-tetradecanoyl-(2S)-hydroxyglycine = glyoxylate +
CC tetradecamide; Xref=Rhea:RHEA:58632, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:137125, ChEBI:CHEBI:142694;
CC Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-decanoylglycine + O2 = H2O + 2 monodehydro-
CC L-ascorbate radical + N-decanoyl-(2S)-hydroxyglycine;
CC Xref=Rhea:RHEA:58608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:142680,
CC ChEBI:CHEBI:142692; Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-decanoyl-(2S)-hydroxyglycine = decanamide + glyoxylate;
CC Xref=Rhea:RHEA:58620, ChEBI:CHEBI:36655, ChEBI:CHEBI:38833,
CC ChEBI:CHEBI:142692; Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-ascorbate + N-octanoylglycine + O2 = H2O + 2 monodehydro-
CC L-ascorbate radical + N-octanoyl-(2S)-hydroxyglycine;
CC Xref=Rhea:RHEA:58612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:142681,
CC ChEBI:CHEBI:142691; Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-octanoyl-(2S)-hydroxyglycine = glyoxylate + octanamide;
CC Xref=Rhea:RHEA:58616, ChEBI:CHEBI:36655, ChEBI:CHEBI:142682,
CC ChEBI:CHEBI:142691; Evidence={ECO:0000250|UniProtKB:P14925};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P14925};
CC Note=Binds one Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14925};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:2059626};
CC Note=Binds 2 Cu(2+) ions per subunit. {ECO:0000250|UniProtKB:P14925};
CC -!- ACTIVITY REGULATION: PAM activity is inhibited by EDTA, phenylglyoxal
CC and diethyl pyrocarbonate (By similarity). PAL activity is stimulated
CC by cadmium and inhibited by mercury (By similarity).
CC {ECO:0000250|UniProtKB:P14925, ECO:0000250|UniProtKB:P19021}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimally active at acidic pHs. {ECO:0000269|PubMed:2059626};
CC -!- SUBUNIT: Monomer. Interacts with RASSF9.
CC {ECO:0000250|UniProtKB:P14925}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:2059626}; Single-pass membrane protein
CC {ECO:0000269|PubMed:2059626}. Note=Secretory granules.
CC {ECO:0000269|PubMed:2059626}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidyl-alpha-
CC hydroxyglycine alpha-amidating lyase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the copper type II
CC ascorbate-dependent monooxygenase family. {ECO:0000305}.
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DR EMBL; M18683; AAA30683.1; -; mRNA.
DR PIR; A40063; URBOAP.
DR RefSeq; NP_776373.1; NM_173948.2.
DR AlphaFoldDB; P10731; -.
DR SMR; P10731; -.
DR MINT; P10731; -.
DR STRING; 9913.ENSBTAP00000016466; -.
DR PaxDb; P10731; -.
DR PRIDE; P10731; -.
DR GeneID; 280890; -.
DR KEGG; bta:280890; -.
DR CTD; 5066; -.
DR eggNOG; KOG3567; Eukaryota.
DR InParanoid; P10731; -.
DR OrthoDB; 476471at2759; -.
DR SABIO-RK; P10731; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030667; C:secretory granule membrane; IDA:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IDA:UniProtKB.
DR GO; GO:0004504; F:peptidylglycine monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0062112; P:fatty acid primary amide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001519; P:peptide amidation; IDA:UniProtKB.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.60.120.230; -; 1.
DR Gene3D; 2.60.120.310; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
DR InterPro; IPR014783; Cu2_ascorb_mOase_CS-2.
DR InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR InterPro; IPR024548; Cu2_monoox_C.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000720; PHM/PAL.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR Pfam; PF01436; NHL; 3.
DR PRINTS; PR00790; PAMONOXGNASE.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
DR PROSITE; PS51125; NHL; 5.
PE 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Copper; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Lipid metabolism;
KW Lyase; Membrane; Metal-binding; Monooxygenase; Multifunctional enzyme;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Vitamin C; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..30
FT /evidence="ECO:0000255"
FT /id="PRO_0000006359"
FT CHAIN 31..972
FT /note="Peptidyl-glycine alpha-amidating monooxygenase"
FT /id="PRO_0000006360"
FT TOPO_DOM 31..873
FT /note="Intragranular"
FT /evidence="ECO:0000255"
FT TRANSMEM 874..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 898..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 498..541
FT /note="NHL 1"
FT REPEAT 567..608
FT /note="NHL 2"
FT REPEAT 617..662
FT /note="NHL 3"
FT REPEAT 670..714
FT /note="NHL 4"
FT REPEAT 766..809
FT /note="NHL 5"
FT REGION 1..494
FT /note="Peptidylglycine alpha-hydroxylating monooxygenase"
FT /evidence="ECO:0000250"
FT REGION 495..817
FT /note="Peptidyl-alpha-hydroxyglycine alpha-amidating lyase"
FT /evidence="ECO:0000250"
FT REGION 925..942
FT /note="Interaction with RASSF9"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT REGION 937..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 103
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 167
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 237
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 239
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 309
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 530
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 584
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 651
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 703
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 783
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT BINDING 784
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 943
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 946
FT /note="Phosphoserine; by UHMK1"
FT /evidence="ECO:0000250|UniProtKB:P19021"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..181
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 76..121
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 109..126
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 222..329
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 288..310
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 631..652
FT /evidence="ECO:0000250|UniProtKB:P14925"
FT DISULFID 699..710
FT /evidence="ECO:0000250|UniProtKB:P14925"
SQ SEQUENCE 972 AA; 108177 MW; EBD41F83E341BAF1 CRC64;
MAGFRSLLVL LLVFPSGCVG FRSPLSVFKR FKETTRSFSN ECLGTTRPVI PIDSSDFALD
IRMPGVTPKQ SDTYFCMSVR LPMDEEAFVI DFKPRASMDT VHHMLLFGCN MPASTGNYWF
CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNHKD
CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP PGGKVVNSDI SCHYKKYPMH VFAYRVHTHH
LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVEHPVDVSF GDILAARCVF TGEGRTEVTH
IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDIFRT IPPEANIPIP VKSDMVMMHG
HHKETENKDK TSLLQQPKRE EEGVLEQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES
DLVAEIANVV QKKDLGRSDT RESAEQERGN AILVRDRIHK FHRLVSTLRP AESRVLSLQQ
PLPGEGTWEP EHTGDFHVEE ALDWPGVYLL PGQVSGVALD PQNNLVIFHR GDHVWDGNSF
DSKFVYQQRG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH
QVFKLDPKSK EGPLLTLGRS MQPGSDQNHF CQPTDVAVDP DTGTIYVSDG YCNSRLVQFS
PSGKFITQWG EASLESSPKP GQFRVPHSLA LVPPLGQLCV ADRENGRIQC FKTDTKEFVR
EIKHPSFGRN VFAISYIPGL LFAVNGKPYF EDQEPVQGFV MNFSSGEIID VFKPVRKHFD
MPHDIAASED GTVYVGDAHT NTVWKFTSTE KMEHRSVKKA GIEVQEIKES EAVVETKMEN
KPASSELQKI QEKQKLVKEP GSGVPAVLIT TLLVIPVVVL LAIALFIRWK KSRAFGDSER
KLEASSGRVL GRLRGKGGGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK DEDASESEEE
YSAPPPAPAP SS
