P19021 (AMD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-glycine alpha-amidating monooxygenase
Short name=PAM

Including the following 2 domains:

1. Peptidylglycine alpha-hydroxylating monooxygenase
   Short name=PHM
   EC=1.14.17.3
2. Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
   EC=4.3.2.5
   Alternative name(s):
   Peptidylamidoglycolate lyase
   Short name=PAL

Gene names

Name:

PAM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	973 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes 2 sequential 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. Peptidylamidoglycolate = peptidyl amide + glyoxylate.
Cofactor	Zinc; for the lyase reaction. Ref.3 Binds 2 copper ions per subunit; For the monoxygenase reaction. Ref.3
Enzyme regulation	Inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate. Ref.3
Subunit structure	Monomer. Interacts with RASSF9 By similarity.
Subcellular location	Isoform 1: Membrane; Single-pass type I membrane protein. Isoform 2: Membrane; Single-pass type I membrane protein. Isoform 3: Secreted. Note: Secreted from secretory granules. Isoform 4: Secreted. Note: Secreted from secretory granules.
Sequence similarities	In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family. In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family. Contains 5 NHL repeats.
Sequence caution	The sequence AAD01439.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Copper Metal-binding Vitamin C Zinc
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Sulfation
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Traceable author statement Ref.1. Source: ProtInc central nervous system development Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara limb development Inferred from electronic annotation. Source: Compara long-chain fatty acid metabolic process Inferred from electronic annotation. Source: Compara maternal process involved in female pregnancy Inferred from electronic annotation. Source: Compara odontogenesis Inferred from electronic annotation. Source: Compara ovulation cycle process Inferred from electronic annotation. Source: Compara peptide amidation Inferred from electronic annotation. Source: Compara peptide metabolic process Non-traceable author statement Ref.2. Source: UniProtKB protein amidation Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: Compara regulation of actin cytoskeleton organization Inferred from electronic annotation. Source: Compara regulation of protein secretion Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara response to copper ion Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to pH Inferred from electronic annotation. Source: Compara toxin metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW neuron projection Inferred from electronic annotation. Source: Compara perikaryon Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara secretory granule Non-traceable author statement Ref.2. Source: UniProtKB secretory granule membrane Inferred from electronic annotation. Source: Compara trans-Golgi network Inferred from electronic annotation. Source: Compara
Molecular_function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: Compara copper ion binding Inferred from electronic annotation. Source: Compara peptidylamidoglycolate lyase activity Inferred from electronic annotation. Source: EC peptidylglycine monooxygenase activity Non-traceable author statement Ref.2. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P19021-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P19021-2)

The sequence of this isoform differs from the canonical sequence as follows:
     388-494: Missing.

Isoform 3 (identifier: P19021-3)

The sequence of this isoform differs from the canonical sequence as follows:
     829-896: Missing.

Isoform 4 (identifier: P19021-4)

The sequence of this isoform differs from the canonical sequence as follows:
     829-914: Missing.

Isoform 5 (identifier: P19021-5)

The sequence of this isoform differs from the canonical sequence as follows:
     896-896: G → GA

Isoform 6 (identifier: P19021-6)

The sequence of this isoform differs from the canonical sequence as follows:
     897-914: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Probable
	Propeptide	21 – 30	10	Probable		PRO_0000006361
	Chain	31 – 973	943	Peptidyl-glycine alpha-amidating monooxygenase		PRO_0000006362
Regions
	Topological domain	31 – 863	833	Intragranular Potential
	Transmembrane	864 – 887	24	Helical; Potential
	Topological domain	888 – 973	86	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
Sites
	Metal binding	102	1	Copper A By similarity
	Metal binding	103	1	Copper A By similarity
	Metal binding	167	1	Copper A By similarity
	Metal binding	237	1	Copper B By similarity
	Metal binding	239	1	Copper B By similarity
	Metal binding	309	1	Copper B By similarity
Amino acid modifications
	Modified residue	918	1	Phosphoserine By similarity
	Modified residue	929	1	Phosphoserine Ref.14
	Modified residue	942	1	Phosphoserine Ref.15
	Modified residue	943	1	Phosphothreonine Ref.12
	Modified residue	946	1	Phosphoserine; by UHMK1; in vitro Ref.12 Ref.13 Ref.15
	Modified residue	961	1	Sulfotyrosine Ref.11
	Glycosylation	762	1	N-linked (GlcNAc...) Potential
	Disulfide bond	42 ↔ 181		By similarity
	Disulfide bond	76 ↔ 121		By similarity
	Disulfide bond	109 ↔ 126		By similarity
	Disulfide bond	222 ↔ 329		By similarity
	Disulfide bond	288 ↔ 310		By similarity
	Disulfide bond	631 ↔ 652		By similarity
	Disulfide bond	699 ↔ 710		By similarity
Natural variations
	Alternative sequence	388 – 494	107	Missing in isoform 2.		VSP_001227
	Alternative sequence	829 – 914	86	Missing in isoform 4.		VSP_001229
	Alternative sequence	829 – 896	68	Missing in isoform 3.		VSP_001228
	Alternative sequence	896	1	G → GA in isoform 5.		VSP_038691
	Alternative sequence	897 – 914	18	Missing in isoform 6.		VSP_042209
	Natural variant	49	1	V → L. Corresponds to variant rs2230458 [ dbSNP | Ensembl ].		VAR_055694
Experimental info
	Sequence conflict	26	1	S → P in BAF82847. Ref.4
	Sequence conflict	574	1	G → E in AAA36414. Ref.1
	Sequence conflict	774	1	P → L in BAF82847. Ref.4
	Sequence conflict	830 – 831	2	Missing in AAB32775. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: 8A089B657F56EE39	FASTA	973	108,332
	10 20 30 40 50 60 MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV PIDSSDFALD 70 80 90 100 110 120 IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT VHHMLLFGCN MPSSTGSYWF 130 140 150 160 170 180 CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNNKD 190 200 210 220 230 240 CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH 250 260 270 280 290 300 LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 310 320 330 340 350 360 IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP VKSDMVMMHE 370 380 390 400 410 420 HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES 430 440 450 460 470 480 DLVAEIANVV QKKDLGRSDA REGAEHERGN AILVRDRIHK FHRLVSTLRP PESRVFSLQQ 490 500 510 520 530 540 PPPGEGTWEP EHTGDFHMEE ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF 550 560 570 580 590 600 DSKFVYQQIG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 610 620 630 640 650 660 QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG YCNSRIVQFS 670 680 690 700 710 720 PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV ADRENGRIQC FKTDTKEFVR 730 740 750 760 770 780 EIKHSSFGRN VFAISYIPGL LFAVNGKPHF GDQEPVQGFV MNFSNGEIID IFKPVRKHFD 790 800 810 820 830 840 MPHDIVASED GTVYIGDAHT NTVWKFTLTE KLEHRSVKKA GIEVQEIKEA EAVVETKMEN 850 860 870 880 890 900 KPTSSELQKM QEKQKLIKEP GSGVPVVLIT TLLVIPVVVL LAIAIFIRWK KSRAFGDSEH 910 920 930 940 950 960 KLETSSGRVL GRFRGKGSGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK EDDGSESEEE 970 YSAPLPALAP SSS
	Isoform 2 [UniParc]. Checksum: 41F0822F95AC3B0E	FASTA	866	96,258
	10 20 30 40 50 60 MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV PIDSSDFALD 70 80 90 100 110 120 IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT VHHMLLFGCN MPSSTGSYWF 130 140 150 160 170 180 CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNNKD 190 200 210 220 230 240 CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH 250 260 270 280 290 300 LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 310 320 330 340 350 360 IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP VKSDMVMMHE 370 380 390 400 410 420 HHKETEYKDK IPLLQQPKRE EEEVLDQDFH MEEALDWPGV YLLPGQVSGV ALDPKNNLVI 430 440 450 460 470 480 FHRGDHVWDG NSFDSKFVYQ QIGLGPIEED TILVIDPNNA AVLQSSGKNL FYLPHGLSID 490 500 510 520 530 540 KDGNYWVTDV ALHQVFKLDP NNKEGPVLIL GRSMQPGSDQ NHFCQPTDVA VDPGTGAIYV 550 560 570 580 590 600 SDGYCNSRIV QFSPSGKFIT QWGEESSGSS PLPGQFTVPH SLALVPLLGQ LCVADRENGR 610 620 630 640 650 660 IQCFKTDTKE FVREIKHSSF GRNVFAISYI PGLLFAVNGK PHFGDQEPVQ GFVMNFSNGE 670 680 690 700 710 720 IIDIFKPVRK HFDMPHDIVA SEDGTVYIGD AHTNTVWKFT LTEKLEHRSV KKAGIEVQEI 730 740 750 760 770 780 KEAEAVVETK MENKPTSSEL QKMQEKQKLI KEPGSGVPVV LITTLLVIPV VVLLAIAIFI 790 800 810 820 830 840 RWKKSRAFGD SEHKLETSSG RVLGRFRGKG SGGLNLGNFF ASRKGYSRKG FDRLSTEGSD 850 860 QEKEDDGSES EEEYSAPLPA LAPSSS
	Isoform 3 [UniParc]. Checksum: 5A5EAAC529E267AE	FASTA	905	100,818
	10 20 30 40 50 60 MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV PIDSSDFALD 70 80 90 100 110 120 IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT VHHMLLFGCN MPSSTGSYWF 130 140 150 160 170 180 CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNNKD 190 200 210 220 230 240 CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH 250 260 270 280 290 300 LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 310 320 330 340 350 360 IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP VKSDMVMMHE 370 380 390 400 410 420 HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES 430 440 450 460 470 480 DLVAEIANVV QKKDLGRSDA REGAEHERGN AILVRDRIHK FHRLVSTLRP PESRVFSLQQ 490 500 510 520 530 540 PPPGEGTWEP EHTGDFHMEE ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF 550 560 570 580 590 600 DSKFVYQQIG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 610 620 630 640 650 660 QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG YCNSRIVQFS 670 680 690 700 710 720 PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV ADRENGRIQC FKTDTKEFVR 730 740 750 760 770 780 EIKHSSFGRN VFAISYIPGL LFAVNGKPHF GDQEPVQGFV MNFSNGEIID IFKPVRKHFD 790 800 810 820 830 840 MPHDIVASED GTVYIGDAHT NTVWKFTLTE KLEHRSVKKA GIEVQEIKDS EHKLETSSGR 850 860 870 880 890 900 VLGRFRGKGS GGLNLGNFFA SRKGYSRKGF DRLSTEGSDQ EKEDDGSESE EEYSAPLPAL APSSS
	Isoform 4 [UniParc]. Checksum: 5F3E355C256FF35C	FASTA	887	98,762
	10 20 30 40 50 60 MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV PIDSSDFALD 70 80 90 100 110 120 IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT VHHMLLFGCN MPSSTGSYWF 130 140 150 160 170 180 CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNNKD 190 200 210 220 230 240 CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH 250 260 270 280 290 300 LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 310 320 330 340 350 360 IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP VKSDMVMMHE 370 380 390 400 410 420 HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES 430 440 450 460 470 480 DLVAEIANVV QKKDLGRSDA REGAEHERGN AILVRDRIHK FHRLVSTLRP PESRVFSLQQ 490 500 510 520 530 540 PPPGEGTWEP EHTGDFHMEE ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF 550 560 570 580 590 600 DSKFVYQQIG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 610 620 630 640 650 660 QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG YCNSRIVQFS 670 680 690 700 710 720 PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV ADRENGRIQC FKTDTKEFVR 730 740 750 760 770 780 EIKHSSFGRN VFAISYIPGL LFAVNGKPHF GDQEPVQGFV MNFSNGEIID IFKPVRKHFD 790 800 810 820 830 840 MPHDIVASED GTVYIGDAHT NTVWKFTLTE KLEHRSVKKA GIEVQEIKGK GSGGLNLGNF 850 860 870 880 FASRKGYSRK GFDRLSTEGS DQEKEDDGSE SEEEYSAPLP ALAPSSS
	Isoform 5 [UniParc]. Checksum: F6D51C73F6E264A3	FASTA	974	108,403
	10 20 30 40 50 60 MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV PIDSSDFALD 70 80 90 100 110 120 IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT VHHMLLFGCN MPSSTGSYWF 130 140 150 160 170 180 CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNNKD 190 200 210 220 230 240 CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH 250 260 270 280 290 300 LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 310 320 330 340 350 360 IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP VKSDMVMMHE 370 380 390 400 410 420 HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES 430 440 450 460 470 480 DLVAEIANVV QKKDLGRSDA REGAEHERGN AILVRDRIHK FHRLVSTLRP PESRVFSLQQ 490 500 510 520 530 540 PPPGEGTWEP EHTGDFHMEE ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF 550 560 570 580 590 600 DSKFVYQQIG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 610 620 630 640 650 660 QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG YCNSRIVQFS 670 680 690 700 710 720 PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV ADRENGRIQC FKTDTKEFVR 730 740 750 760 770 780 EIKHSSFGRN VFAISYIPGL LFAVNGKPHF GDQEPVQGFV MNFSNGEIID IFKPVRKHFD 790 800 810 820 830 840 MPHDIVASED GTVYIGDAHT NTVWKFTLTE KLEHRSVKKA GIEVQEIKEA EAVVETKMEN 850 860 870 880 890 900 KPTSSELQKM QEKQKLIKEP GSGVPVVLIT TLLVIPVVVL LAIAIFIRWK KSRAFGADSE 910 920 930 940 950 960 HKLETSSGRV LGRFRGKGSG GLNLGNFFAS RKGYSRKGFD RLSTEGSDQE KEDDGSESEE 970 EYSAPLPALA PSSS
	Isoform 6 [UniParc]. Checksum: EE05609B9A7F1772	FASTA	955	106,276
	10 20 30 40 50 60 MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV PIDSSDFALD 70 80 90 100 110 120 IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT VHHMLLFGCN MPSSTGSYWF 130 140 150 160 170 180 CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNNKD 190 200 210 220 230 240 CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH 250 260 270 280 290 300 LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 310 320 330 340 350 360 IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP VKSDMVMMHE 370 380 390 400 410 420 HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES 430 440 450 460 470 480 DLVAEIANVV QKKDLGRSDA REGAEHERGN AILVRDRIHK FHRLVSTLRP PESRVFSLQQ 490 500 510 520 530 540 PPPGEGTWEP EHTGDFHMEE ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF 550 560 570 580 590 600 DSKFVYQQIG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 610 620 630 640 650 660 QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG YCNSRIVQFS 670 680 690 700 710 720 PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV ADRENGRIQC FKTDTKEFVR 730 740 750 760 770 780 EIKHSSFGRN VFAISYIPGL LFAVNGKPHF GDQEPVQGFV MNFSNGEIID IFKPVRKHFD 790 800 810 820 830 840 MPHDIVASED GTVYIGDAHT NTVWKFTLTE KLEHRSVKKA GIEVQEIKEA EAVVETKMEN 850 860 870 880 890 900 KPTSSELQKM QEKQKLIKEP GSGVPVVLIT TLLVIPVVVL LAIAIFIRWK KSRAFGGKGS 910 920 930 940 950 GGLNLGNFFA SRKGYSRKGF DRLSTEGSDQ EKEDDGSESE EEYSAPLPAL APSSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells." Glauder J., Ragg H., Rauch J., Engels J.W. Biochem. Biophys. Res. Commun. 169:551-558(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Tissue: Thyroid carcinoma.
[2]	"Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase." Tateishi K., Arakawa F., Misumi Y., Treston A.M., Vos M., Matsuoka Y. Biochem. Biophys. Res. Commun. 205:282-290(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[3]	"Expression and characterization of human bifunctional peptidylglycine alpha-amidating monooxygenase." Satani M., Takahashi K., Sakamoto H., Harada S., Kaida Y., Noguchi M. Protein Expr. Purif. 28:293-302(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, ENZYME REGULATION. Tissue: Heart.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Thalamus.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung.
[9]	"The alpha-amidating monooxygenase gene of human kidney." Chung B.H., Oh G.H., Choi E.S. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-973 (ISOFORM 4). Tissue: Kidney.
[10]	"Large-scale concatenation cDNA sequencing." Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A. Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 707-973 (ISOFORM 6). Tissue: Brain.
[11]	"Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase." Yun H.Y., Keutmann H.T., Eipper B.A. J. Biol. Chem. 269:10946-10955(1994) [PubMed] [Europe PMC] [Abstract] Cited for: SULFATION AT TYR-961.
[12]	"The novel kinase peptidylglycine alpha-amidating monooxygenase cytosolic interactor protein 2 interacts with the cytosolic routing determinants of the peptide processing enzyme peptidylglycine alpha-amidating monooxygenase." Caldwell B.D., Darlington D.N., Penzes P., Johnson R.C., Eipper B.A., Mains R.E. J. Biol. Chem. 274:34646-34656(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-943 AND SER-946.
[13]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-946, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-929, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-946, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M37721 mRNA. Translation: AAA36414.1. S75037 mRNA. Translation: AAB32775.1. S75038 mRNA. Translation: AAB32776.1. AB095007 mRNA. Translation: BAC22594.1. AK290158 mRNA. Translation: BAF82847.1. BT007419 mRNA. Translation: AAP36087.1. AC008779 Genomic DNA. No translation available. AC010250 Genomic DNA. No translation available. AC113373 Genomic DNA. No translation available. CH471086 Genomic DNA. Translation: EAW49085.1. BC018127 mRNA. Translation: AAH18127.1. AF010472 mRNA. Translation: AAD01439.1. Different initiation. AF035320 mRNA. Translation: AAB88190.1.
IPI	IPI00177543. IPI00219042. IPI00219043. IPI00749176. IPI00878690. IPI00940221.
PIR	URHUAP. A35477.
RefSeq	NP_000910.2. NM_000919.3. NP_001170777.1. NM_001177306.1. NP_620121.1. NM_138766.2. NP_620176.1. NM_138821.2. NP_620177.1. NM_138822.2.
UniGene	Hs.369430.
3D structure databases
ProteinModelPortal	P19021.
ModBase	Search...
Protein-protein interaction databases
IntAct	P19021. 2 interactions.
PTM databases
PhosphoSite	P19021.
Polymorphism databases
DMDM	23503036.
Proteomic databases
PaxDb	P19021.
PRIDE	P19021.
Protocols and materials databases
DNASU	5066.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000304400; ENSP00000306100; ENSG00000145730. ENST00000346918; ENSP00000282992; ENSG00000145730. ENST00000348126; ENSP00000314638; ENSG00000145730. ENST00000438793; ENSP00000396493; ENSG00000145730. ENST00000455264; ENSP00000403461; ENSG00000145730.
GeneID	5066.
KEGG	hsa:5066.
UCSC	uc003kns.3. human. uc003knt.3. human. uc003knu.3. human. uc003knv.3. human. uc003knw.3. human. uc003knz.3. human.
Organism-specific databases
CTD	5066.
GeneCards	GC05P102089.
HGNC	HGNC:8596. PAM.
HPA	CAB026119.
MIM	170270. gene.
neXtProt	NX_P19021.
PharmGKB	PA32926.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3391.
HOVERGEN	HBG004218.
KO	K00504.
OMA	DTVHHML.
OrthoDB	EOG46MBHT.
Enzyme and pathway databases
SignaLink	P19021.
Gene expression databases
ArrayExpress	P19021.
Bgee	P19021.
CleanEx	HS_PAM.
Genevestigator	P19021.
GermOnline	ENSG00000145730. Homo sapiens.
Family and domain databases
Gene3D	2.120.10.30. 2 hits. 2.60.120.230. 1 hit. 2.60.120.310. 1 hit.
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR014784. Cu2_ascorb_mOase-like_C. IPR020611. Cu2_ascorb_mOase_CS-1. IPR014783. Cu2_ascorb_mOase_CS-2. IPR000323. Cu2_ascorb_mOase_N. IPR001258. NHL_repeat. IPR013017. NHL_repeat_subgr. IPR000720. Pep_amidat_mOase. IPR008977. PHM/PNGase_F_dom. [Graphical view]
Pfam	PF01082. Cu2_monooxygen. 1 hit. PF01436. NHL. 4 hits. [Graphical view]
PRINTS	PR00790. PAMONOXGNASE.
SUPFAM	SSF49742. PHM_PNGase_F. 2 hits.
PROSITE	PS00084. CU2_MONOOXYGENASE_1. 1 hit. PS00085. CU2_MONOOXYGENASE_2. 1 hit. PS51125. NHL. 5 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P19021.
ChEMBL	CHEMBL2544.
ChiTaRS	PAM. human.
DrugBank	DB00126. Vitamin C.
GenomeRNAi	5066.
NextBio	19512.
SOURCE	Search...

Entry information

Entry name

AMD_HUMAN

Accession

Primary (citable) accession number: P19021
Secondary accession number(s): A6NMR0 , A8K293, O43211, O95080, Q16252, Q16253, Q54A45, Q86U53, Q8WVC7, Q9UCG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	September 19, 2002
Last modified:	May 29, 2013
This is version 156 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.