Peptidylglycine alpha-hydroxylating monooxygenase
     (PHM)
     (EC 1.14.17.3)
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
     (EC 4.3.2.5)
     (Peptidylamidoglycolate lyase)
     (PAL)

Gene name

Name:

PAM

From

Bos taurus (Bovine)

[TaxID: 9913]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Pituitary; PubMed=3153462 [NCBI, ExPASy, EBI, Israel, Japan] Eipper B.A., Park L.P., Dickerson I.M., Keutmann H.T., Thiele E.A., Rodriguez H., Schofield P.R., Mains R.E.; "Structure of the precursor to an enzyme mediating COOH-terminal amidation in peptide biosynthesis."; Mol. Endocrinol. 1:777-790(1987).
[2]	PROTEIN SEQUENCE OF 478-499; 544-575; 611-630 AND 665-695, FUNCTION, AND SUBCELLULAR LOCATION. DOI=10.1021/bi00239a016; PubMed=2059626 [NCBI, ExPASy, EBI, Israel, Japan] Katopodis A.G., Ping D.S., Smith C.E., May S.W.; "Functional and structural characterization of peptidylamidoglycolate lyase, the enzyme catalyzing the second step in peptide amidation."; Biochemistry 30:6189-6194(1991).

Comments

FUNCTION: Bifunctional enzyme that catalyzes 2 sequencial steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
CATALYTIC ACTIVITY: Peptidylglycine + ascorbate + O₂ = peptidyl(2-hydroxyglycine) + dehydroascorbate + H₂O.
CATALYTIC ACTIVITY: Peptidylamidoglycolate = peptidyl amide + glyoxylate.
COFACTOR: Zinc; for the lyase reaction (By similarity).
COFACTOR: Binds 2 copper ions per subunit; For the monoxygenase reaction (By similarity).
SUBUNIT: Monomer. Interacts with RASSF9 (By similarity).
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein. Note=Secretory granules.
SIMILARITY: In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.
SIMILARITY: In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.
SIMILARITY: Contains 5 NHL repeats.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M18683; AAA30683.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A40063; URBOAP.

NP_776373.1; -.

3D structure databases

HSSP

P14925; 3PHM. [HSSP ENTRY / PDB]

SMR

P10731; 40-351.

ModBase

P10731.

Ontologies

GO:0031410;	Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0031418;	Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004598;	Molecular function: peptidylamidoglycolate lyase activity (inferred from electronic annotation from EC).
GO:0004504;	Molecular function: peptidylglycine monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006518;	Biological process: peptide metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR011042; 6-blade_b-propeller_TolB-like.
IPR014783; Cu2_ascorb_mOase_C.
IPR000323; Cu2_ascorb_mOase_N.
IPR001258; NHL_repeat.
IPR013017; NHL_repeat_subgr.
IPR000720; Pep_amidat_mOase.
Graphical view of domain structure.

Gene3D

G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.

Pfam

PF03712; Cu2_monoox_C; 1.
PF01082; Cu2_monooxygen; 1.
PF01436; NHL; 4.
Pfam graphical view of domain structure.

PRINTS

PR00790; PAMONOXGNASE.

PROSITE

PS00084; CU2_MONOOXYGENASE_1; 1.
PS00085; CU2_MONOOXYGENASE_2; 1.
PS51125; NHL; 5.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSBTAG00000012387; Bos taurus. [Contig view]

GeneID

280890; -.

KEGG

bta:280890; -.

Phylogenomic databases

HOVERGEN

P10731; -.

Other

ProtoNet

P10731.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cleavage on pair of basic residues; Copper; Cytoplasmic vesicle; Direct protein sequencing; Glycoprotein; Lyase; Membrane; Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase; Phosphoprotein; Repeat; Signal; Sulfation; Transmembrane; Vitamin C; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`PROPEP`	`21 30`	`10`	`Potential.`	`PRO_0000006359`
`CHAIN`	`31 972`	`942`	`Peptidyl-glycine alpha-amidating monooxygenase.`	`PRO_0000006360`
`TOPO_DOM`	`31 873`	`843`	`Intragranular (Potential).`
`TRANSMEM`	`874 897`	`24`	`Potential.`
`TOPO_DOM`	`898 972`	`75`	`Cytoplasmic (Potential).`
`REPEAT`	`498 541`	`44`	`NHL 1.`
`REPEAT`	`567 608`	`42`	`NHL 2.`
`REPEAT`	`617 662`	`46`	`NHL 3.`
`REPEAT`	`670 714`	`45`	`NHL 4.`
`REPEAT`	`766 809`	`44`	`NHL 5.`
`REGION`	`1 494`	`494`	`Peptidylglycine alpha-hydroxylating monooxygenase (By similarity).`
`REGION`	`495 817`	`323`	`Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (By similarity).`
`REGION`	`925 942`	`18`	`Interaction with RASSF9 (By similarity).`
`METAL`	`102 102`		`Copper A (By similarity).`
`METAL`	`103 103`		`Copper A (By similarity).`
`METAL`	`167 167`		`Copper A (By similarity).`
`METAL`	`237 237`		`Copper B (By similarity).`
`METAL`	`239 239`		`Copper B (By similarity).`
`METAL`	`309 309`		`Copper B (By similarity).`
`MOD_RES`	`929 929`		`Phosphoserine (By similarity).`
`MOD_RES`	`955 955`		`Phosphoserine (By similarity).`
`MOD_RES`	`957 957`		`Phosphoserine (By similarity).`
`MOD_RES`	`961 961`		`Sulfotyrosine (By similarity).`
`CARBOHYD`	`762 762`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`42 181`		`By similarity.`
`DISULFID`	`76 121`		`By similarity.`
`DISULFID`	`109 126`		`By similarity.`
`DISULFID`	`222 329`		`By similarity.`
`DISULFID`	`288 310`		`By similarity.`
`DISULFID`	`631 652`		`By similarity.`
`DISULFID`	`699 710`		`By similarity.`

Sequence information

Length: 972 AA [This is the length of the unprocessed precursor]

Molecular weight: 108177 Da [This is the MW of the unprocessed precursor]

CRC64: EBD41F83E341BAF1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGFRSLLVL LLVFPSGCVG FRSPLSVFKR FKETTRSFSN ECLGTTRPVI PIDSSDFALD 

        70         80         90        100        110        120 
IRMPGVTPKQ SDTYFCMSVR LPMDEEAFVI DFKPRASMDT VHHMLLFGCN MPASTGNYWF 

       130        140        150        160        170        180 
CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNHKD 

       190        200        210        220        230        240 
CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP PGGKVVNSDI SCHYKKYPMH VFAYRVHTHH 

       250        260        270        280        290        300 
LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVEHPVDVSF GDILAARCVF TGEGRTEVTH 

       310        320        330        340        350        360 
IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDIFRT IPPEANIPIP VKSDMVMMHG 

       370        380        390        400        410        420 
HHKETENKDK TSLLQQPKRE EEGVLEQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES 

       430        440        450        460        470        480 
DLVAEIANVV QKKDLGRSDT RESAEQERGN AILVRDRIHK FHRLVSTLRP AESRVLSLQQ 

       490        500        510        520        530        540 
PLPGEGTWEP EHTGDFHVEE ALDWPGVYLL PGQVSGVALD PQNNLVIFHR GDHVWDGNSF 

       550        560        570        580        590        600 
DSKFVYQQRG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 

       610        620        630        640        650        660 
QVFKLDPKSK EGPLLTLGRS MQPGSDQNHF CQPTDVAVDP DTGTIYVSDG YCNSRLVQFS 

       670        680        690        700        710        720 
PSGKFITQWG EASLESSPKP GQFRVPHSLA LVPPLGQLCV ADRENGRIQC FKTDTKEFVR 

       730        740        750        760        770        780 
EIKHPSFGRN VFAISYIPGL LFAVNGKPYF EDQEPVQGFV MNFSSGEIID VFKPVRKHFD 

       790        800        810        820        830        840 
MPHDIAASED GTVYVGDAHT NTVWKFTSTE KMEHRSVKKA GIEVQEIKES EAVVETKMEN 

       850        860        870        880        890        900 
KPASSELQKI QEKQKLVKEP GSGVPAVLIT TLLVIPVVVL LAIALFIRWK KSRAFGDSER 

       910        920        930        940        950        960 
KLEASSGRVL GRLRGKGGGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK DEDASESEEE 

       970 
YSAPPPAPAP SS

P10731 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools