Reviewed, UniProtKB/Swiss-Prot P14925 (AMD_RAT)

Names and origin

Protein names

Recommended name:
    Peptidyl-glycine alpha-amidating monooxygenase
      Short name=PAM
Including the following 2 domains:
    1- Recommended name:
            Peptidylglycine alpha-hydroxylating monooxygenase
                Short name=PHM
              EC=1.14.17.3
    2- Recommended name:
            Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
              EC=4.3.2.5
        Alternative name(s):
            Peptidylamidoglycolate lyase
              Short name=PAL

Gene names

Name:

Pam

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	976 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. Binds 2 copper ions per subunit; For the monoxygenase reaction.
Subunit structure	Monomer. Interacts with RASSF9. Ref.8
Subcellular location	Cytoplasmic vesicle › secretory vesicle membrane; Single-pass membrane protein. Note: 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.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane
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	3D-structure Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	central nervous system development Inferred from expression pattern. Source: RGD heart development Inferred from expression pattern. Source: RGD limb development Inferred from expression pattern. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW peptide metabolic process Inferred from electronic annotation. Source: InterPro response to copper ion Inferred from expression pattern. Source: RGD response to drug Inferred from direct assay. Source: RGD response to estradiol stimulus Inferred from expression pattern. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern. Source: RGD response to hypoxia Inferred from expression pattern. Source: RGD response to pH Inferred from direct assay. Source: RGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Inferred from direct assay. Source: RGD perikaryon Inferred from direct assay. Source: RGD secretory granule Inferred from direct assay. Source: RGD
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from direct assay. Source: RGD peptidylamidoglycolate lyase activity Inferred from direct assay. Source: RGD peptidylglycine monooxygenase activity Inferred from direct assay. Source: RGD protein binding Ref.8 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Rassf9	O88869	1	EBI-1395008,EBI-1395057

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform PAM-1 (identifier: P14925-1)

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.

Note: Membrane-bound.

Isoform PAM-2 (identifier: P14925-2)

The sequence of this isoform differs from the canonical sequence as follows:
     393-497: Missing.

Note: Membrane-bound.

Isoform PAM-3 (identifier: P14925-3)

The sequence of this isoform differs from the canonical sequence as follows:
     393-497: Missing.
     832-917: Missing.

Note: Soluble.

Isoform PAM-3A (identifier: P14925-4)

The sequence of this isoform differs from the canonical sequence as follows:
     393-497: Missing.
     832-899: Missing.

Note: Soluble.

Isoform PAM-3B (identifier: P14925-5)

The sequence of this isoform differs from the canonical sequence as follows:
     393-497: Missing.
     900-917: Missing.

Note: Membrane-bound.

Isoform PAM-4 (identifier: P14925-6)

The sequence of this isoform differs from the canonical sequence as follows:
     498-517: DFHVEEELDWPGVYLLPGQV → GASRISFTQKKKCVKHCNPH
     518-917: Missing.

Note: Soluble.

Isoform PAM-5 (identifier: P14925-7)

The sequence of this isoform differs from the canonical sequence as follows:
     308-312: GTSSD → FKDTF
     313-976: Missing.

Note: Soluble.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.6

Propeptide

26 – 35

10

PRO_0000006365

Chain

36 – 976

941

Peptidyl-glycine alpha-amidating monooxygenase

PRO_0000006366

Regions

Topological domain

36 – 866

831

Intragranular Potential

Transmembrane

867 – 890

24

Potential

Topological domain

891 – 976

86

Cytoplasmic Potential

Repeat

501 – 544

44

NHL 1

Repeat

570 – 611

42

NHL 2

Repeat

620 – 665

46

NHL 3

Repeat

673 – 717

45

NHL 4

Repeat

769 – 812

44

NHL 5

Region

1 – 497

497

Peptidylglycine alpha-hydroxylating monooxygenase

Region

498 – 820

323

Peptidyl-alpha-hydroxyglycine alpha-amidating lyase

Region

928 – 945

18

Interaction with RASSF9

Sites

Metal binding

107

1

Copper A

Metal binding

108

1

Copper A

Metal binding

172

1

Copper A

Metal binding

242

1

Copper B

Metal binding

244

1

Copper B

Metal binding

314

1

Copper B

Amino acid modifications

Modified residue

921

1

Phosphoserine By similarity

Modified residue

932

1

Phosphoserine By similarity

Modified residue

945

1

Phosphoserine By similarity

Modified residue

949

1

Phosphoserine By similarity

Modified residue

961

1

Phosphoserine By similarity

Modified residue

965

1

Sulfotyrosine By similarity

Glycosylation

765

1

N-linked (GlcNAc...) Ref.6

Disulfide bond

47 ↔ 186

Ref.9

Disulfide bond

81 ↔ 126

Ref.9

Disulfide bond

114 ↔ 131

Ref.9

Disulfide bond

227 ↔ 334

Ref.9

Disulfide bond

293 ↔ 315

Ref.9

Disulfide bond

634 ↔ 655

Ref.9

Disulfide bond

702 ↔ 713

Ref.9

Natural variations

Alternative sequence

308 – 312

5

GTSSD → FKDTF in isoform PAM-5.

VSP_001230

Alternative sequence

313 – 976

664

Missing in isoform PAM-5.

VSP_001231

Alternative sequence

393 – 497

105

Missing in isoform PAM-2, isoform PAM-3, isoform PAM-3A and isoform PAM-3B.

VSP_001232

Alternative sequence

498 – 517

20

DFHVE…LPGQV → GASRISFTQKKKCVKHCNPH in isoform PAM-4.

VSP_001236

Alternative sequence

518 – 917

400

Missing in isoform PAM-4.

VSP_001237

Alternative sequence

832 – 917

86

Missing in isoform PAM-3.

VSP_001234

Alternative sequence

832 – 899

68

Missing in isoform PAM-3A.

VSP_001233

Alternative sequence

900 – 917

18

Missing in isoform PAM-3B.

VSP_001235

Experimental info

Sequence conflict

959

1

T → S Ref.3

Secondary structure

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976

Helix Strand Turn

Details...

Helix

49 – 51

3

Beta strand

53 – 58

6

Beta strand

61 – 67

7

Beta strand

69 – 71

3

Beta strand

75 – 85

11

Beta strand

92 – 100

9

Turn

103 – 105

3

Beta strand

106 – 118

13

Beta strand

121 – 125

5

Helix

126 – 128

3

Beta strand

130 – 133

4

Beta strand

136 – 142

7

Beta strand

154 – 159

6

Turn

160 – 162

3

Beta strand

165 – 173

9

Helix

177 – 179

3

Beta strand

188 – 196

9

Beta strand

199 – 208

10

Beta strand

221 – 228

8

Beta strand

234 – 242

9

Beta strand

247 – 256

10

Beta strand

259 – 266

8

Beta strand

275 – 283

9

Beta strand

288 – 295

8

Beta strand

304 – 306

3

Beta strand

316 – 324

9

Turn

325 – 327

3

Beta strand

330 – 334

5

Helix

340 – 345

6

Helix

348 – 351

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform PAM-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 7233021BEBEFD9B9	FASTA	976	108,675
	10 20 30 40 50 60 MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT IGPVTPLDAS 70 80 90 100 110 120 DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR ASMDTVHHML LFGCNMPSST 130 140 150 160 170 180 GSYWFCDEGT CTDKANILYA WARNAPPTRL PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR 190 200 210 220 230 240 DNHKDCSGVS VHLTRVPQPL IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR 250 260 270 280 290 300 VHTHHLGKVV SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR 310 320 330 340 350 360 TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA NIPIPVKPDM 370 380 390 400 410 420 VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQGDFYSLLS KLLGEREDVH VHKYNPTEKT 430 440 450 460 470 480 ESGSDLVAEI ANVVQKKDLG RSDAREGAEH EEWGNAILVR DRIHRFHQLE STLRPAESRA 490 500 510 520 530 540 FSFQQPGEGP WEPEPSGDFH VEEELDWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG 550 560 570 580 590 600 NSFDSKFVYQ QRGLGPIEED TILVIDPNNA EILQSSGKNL FYLPHGLSID TDGNYWVTDV 610 620 630 640 650 660 ALHQVFKLDP HSKEGPLLIL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV SDGYCNSRIV 670 680 690 700 710 720 QFSPSGKFVT QWGEESSGSS PRPGQFSVPH SLALVPHLDQ LCVADRENGR IQCFKTDTKE 730 740 750 760 770 780 FVREIKHASF GRNVFAISYI PGFLFAVNGK PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK 790 800 810 820 830 840 HFDMPHDIVA SEDGTVYIGD AHTNTVWKFT LTEKMEHRSV KKAGIEVQEI KEAEAVVEPK 850 860 870 880 890 900 VENKPTSSEL QKMQEKQKLS TEPGSGVSVV LITTLLVIPV LVLLAIVMFI RWKKSRAFGD 910 920 930 940 950 960 HDRKLESSSG RVLGRFRGKG SGGLNLGNFF ASRKGYSRKG FDRVSTEGSD QEKDEDDGTE 970 SEEEYSAPLP KPAPSS
	Isoform PAM-2. Checksum: BA1F40E92F7B8C02	FASTA	871	96,825
	10 20 30 40 50 60 MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT IGPVTPLDAS 70 80 90 100 110 120 DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR ASMDTVHHML LFGCNMPSST 130 140 150 160 170 180 GSYWFCDEGT CTDKANILYA WARNAPPTRL PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR 190 200 210 220 230 240 DNHKDCSGVS VHLTRVPQPL IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR 250 260 270 280 290 300 VHTHHLGKVV SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR 310 320 330 340 350 360 TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA NIPIPVKPDM 370 380 390 400 410 420 VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQDFHVEEEL DWPGVYLLPG QVSGVALDSK 430 440 450 460 470 480 NNLVIFHRGD HVWDGNSFDS KFVYQQRGLG PIEEDTILVI DPNNAEILQS SGKNLFYLPH 490 500 510 520 530 540 GLSIDTDGNY WVTDVALHQV FKLDPHSKEG PLLILGRSMQ PGSDQNHFCQ PTDVAVEPST 550 560 570 580 590 600 GAVFVSDGYC NSRIVQFSPS GKFVTQWGEE SSGSSPRPGQ FSVPHSLALV PHLDQLCVAD 610 620 630 640 650 660 RENGRIQCFK TDTKEFVREI KHASFGRNVF AISYIPGFLF AVNGKPYFGD QEPVQGFVMN 670 680 690 700 710 720 FSSGEIIDVF KPVRKHFDMP HDIVASEDGT VYIGDAHTNT VWKFTLTEKM EHRSVKKAGI 730 740 750 760 770 780 EVQEIKEAEA VVEPKVENKP TSSELQKMQE KQKLSTEPGS GVSVVLITTL LVIPVLVLLA 790 800 810 820 830 840 IVMFIRWKKS RAFGDHDRKL ESSSGRVLGR FRGKGSGGLN LGNFFASRKG YSRKGFDRVS 850 860 870 TEGSDQEKDE DDGTESEEEY SAPLPKPAPS S
	Isoform PAM-3. Checksum: D49246033AEA388B	FASTA	785	87,253
	10 20 30 40 50 60 MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT IGPVTPLDAS 70 80 90 100 110 120 DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR ASMDTVHHML LFGCNMPSST 130 140 150 160 170 180 GSYWFCDEGT CTDKANILYA WARNAPPTRL PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR 190 200 210 220 230 240 DNHKDCSGVS VHLTRVPQPL IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR 250 260 270 280 290 300 VHTHHLGKVV SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR 310 320 330 340 350 360 TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA NIPIPVKPDM 370 380 390 400 410 420 VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQDFHVEEEL DWPGVYLLPG QVSGVALDSK 430 440 450 460 470 480 NNLVIFHRGD HVWDGNSFDS KFVYQQRGLG PIEEDTILVI DPNNAEILQS SGKNLFYLPH 490 500 510 520 530 540 GLSIDTDGNY WVTDVALHQV FKLDPHSKEG PLLILGRSMQ PGSDQNHFCQ PTDVAVEPST 550 560 570 580 590 600 GAVFVSDGYC NSRIVQFSPS GKFVTQWGEE SSGSSPRPGQ FSVPHSLALV PHLDQLCVAD 610 620 630 640 650 660 RENGRIQCFK TDTKEFVREI KHASFGRNVF AISYIPGFLF AVNGKPYFGD QEPVQGFVMN 670 680 690 700 710 720 FSSGEIIDVF KPVRKHFDMP HDIVASEDGT VYIGDAHTNT VWKFTLTEKM EHRSVKKAGI 730 740 750 760 770 780 EVQEIKGKGS GGLNLGNFFA SRKGYSRKGF DRVSTEGSDQ EKDEDDGTES EEEYSAPLPK PAPSS
	Isoform PAM-3A. Checksum: A9C822E643E870D0	FASTA	803	89,350
	10 20 30 40 50 60 MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT IGPVTPLDAS 70 80 90 100 110 120 DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR ASMDTVHHML LFGCNMPSST 130 140 150 160 170 180 GSYWFCDEGT CTDKANILYA WARNAPPTRL PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR 190 200 210 220 230 240 DNHKDCSGVS VHLTRVPQPL IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR 250 260 270 280 290 300 VHTHHLGKVV SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR 310 320 330 340 350 360 TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA NIPIPVKPDM 370 380 390 400 410 420 VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQDFHVEEEL DWPGVYLLPG QVSGVALDSK 430 440 450 460 470 480 NNLVIFHRGD HVWDGNSFDS KFVYQQRGLG PIEEDTILVI DPNNAEILQS SGKNLFYLPH 490 500 510 520 530 540 GLSIDTDGNY WVTDVALHQV FKLDPHSKEG PLLILGRSMQ PGSDQNHFCQ PTDVAVEPST 550 560 570 580 590 600 GAVFVSDGYC NSRIVQFSPS GKFVTQWGEE SSGSSPRPGQ FSVPHSLALV PHLDQLCVAD 610 620 630 640 650 660 RENGRIQCFK TDTKEFVREI KHASFGRNVF AISYIPGFLF AVNGKPYFGD QEPVQGFVMN 670 680 690 700 710 720 FSSGEIIDVF KPVRKHFDMP HDIVASEDGT VYIGDAHTNT VWKFTLTEKM EHRSVKKAGI 730 740 750 760 770 780 EVQEIKDHDR KLESSSGRVL GRFRGKGSGG LNLGNFFASR KGYSRKGFDR VSTEGSDQEK 790 800 DEDDGTESEE EYSAPLPKPA PSS
	Isoform PAM-3B. Checksum: D4620879E16C381F	FASTA	853	94,728
	10 20 30 40 50 60 MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT IGPVTPLDAS 70 80 90 100 110 120 DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR ASMDTVHHML LFGCNMPSST 130 140 150 160 170 180 GSYWFCDEGT CTDKANILYA WARNAPPTRL PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR 190 200 210 220 230 240 DNHKDCSGVS VHLTRVPQPL IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR 250 260 270 280 290 300 VHTHHLGKVV SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR 310 320 330 340 350 360 TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA NIPIPVKPDM 370 380 390 400 410 420 VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQDFHVEEEL DWPGVYLLPG QVSGVALDSK 430 440 450 460 470 480 NNLVIFHRGD HVWDGNSFDS KFVYQQRGLG PIEEDTILVI DPNNAEILQS SGKNLFYLPH 490 500 510 520 530 540 GLSIDTDGNY WVTDVALHQV FKLDPHSKEG PLLILGRSMQ PGSDQNHFCQ PTDVAVEPST 550 560 570 580 590 600 GAVFVSDGYC NSRIVQFSPS GKFVTQWGEE SSGSSPRPGQ FSVPHSLALV PHLDQLCVAD 610 620 630 640 650 660 RENGRIQCFK TDTKEFVREI KHASFGRNVF AISYIPGFLF AVNGKPYFGD QEPVQGFVMN 670 680 690 700 710 720 FSSGEIIDVF KPVRKHFDMP HDIVASEDGT VYIGDAHTNT VWKFTLTEKM EHRSVKKAGI 730 740 750 760 770 780 EVQEIKEAEA VVEPKVENKP TSSELQKMQE KQKLSTEPGS GVSVVLITTL LVIPVLVLLA 790 800 810 820 830 840 IVMFIRWKKS RAFGGKGSGG LNLGNFFASR KGYSRKGFDR VSTEGSDQEK DEDDGTESEE 850 EYSAPLPKPA PSS
	Isoform PAM-4. Checksum: DA702AEAC95B0F49	FASTA	576	64,102
	10 20 30 40 50 60 MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT IGPVTPLDAS 70 80 90 100 110 120 DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR ASMDTVHHML LFGCNMPSST 130 140 150 160 170 180 GSYWFCDEGT CTDKANILYA WARNAPPTRL PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR 190 200 210 220 230 240 DNHKDCSGVS VHLTRVPQPL IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR 250 260 270 280 290 300 VHTHHLGKVV SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR 310 320 330 340 350 360 TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA NIPIPVKPDM 370 380 390 400 410 420 VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQGDFYSLLS KLLGEREDVH VHKYNPTEKT 430 440 450 460 470 480 ESGSDLVAEI ANVVQKKDLG RSDAREGAEH EEWGNAILVR DRIHRFHQLE STLRPAESRA 490 500 510 520 530 540 FSFQQPGEGP WEPEPSGGAS RISFTQKKKC VKHCNPHGKG SGGLNLGNFF ASRKGYSRKG 550 560 570 FDRVSTEGSD QEKDEDDGTE SEEEYSAPLP KPAPSS
	Isoform PAM-5. Checksum: 0150C054899C8326	FASTA	312	34,676
	10 20 30 40 50 60 MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT IGPVTPLDAS 70 80 90 100 110 120 DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR ASMDTVHHML LFGCNMPSST 130 140 150 160 170 180 GSYWFCDEGT CTDKANILYA WARNAPPTRL PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR 190 200 210 220 230 240 DNHKDCSGVS VHLTRVPQPL IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR 250 260 270 280 290 300 VHTHHLGKVV SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR 310 TEATHIGFKD TF

References

[1]	"Alternative mRNA splicing generates multiple forms of peptidyl-glycine alpha-amidating monooxygenase in rat atrium." Stoffers D.A., Green C.B.R., Eipper B.A. Proc. Natl. Acad. Sci. U.S.A. 86:735-739(1989) [PubMed: 2911604] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (PAM-1/2). Strain: Sprague-Dawley. Tissue: Heart atrium.
[2]	"Characterization of novel mRNAs encoding enzymes involved in peptide alpha-amidation." Stoffers D.A., Ouafik L., Eipper B.A. J. Biol. Chem. 266:1701-1707(1991) [PubMed: 1988445] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (PAM-3/4). Strain: Sprague-Dawley. Tissue: Heart atrium.
[3]	"Isolation and functional expression of pituitary peptidylglycine alpha-amidating enzyme mRNA. A variant lacking the transmembrane domain." Kato I., Yonekura H., Yamamoto H., Okamoto H. FEBS Lett. 269:319-323(1990) [PubMed: 2401356] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (PAM-1 TO 5). Strain: Wistar. Tissue: Pituitary.
[4]	"Cloning and characterization of two alternatively spliced rat alpha-amidating enzyme cDNAs from rat medullary thyroid carcinoma." Bertelsen A.H., Beaudry G.A., Galella E.A., Jones B.N., Ray M.L., Mehta N.M. Arch. Biochem. Biophys. 279:87-96(1990) [PubMed: 2337358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (PAM-4). Strain: Sprague-Dawley. Tissue: Liver.
[5]	"Alternative splicing and endoproteolytic processing generate tissue-specific forms of pituitary peptidylglycine alpha-amidating monooxygenase (PAM)." Eipper B.A., Green C.B., Campbell T.A., Stoffers D.A., Keutmann H.T., Mains R.E., Ouafik L. J. Biol. Chem. 267:4008-4015(1992) [PubMed: 1740449] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[6]	"Purification and characterization of functional recombinant alpha-amidating enzyme secreted from mammalian cells." Beaudry G.A., Mehta N.M., Ray M.L., Bertelsen A.H. J. Biol. Chem. 265:17694-17699(1990) [PubMed: 2211657] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-42, GLYCOSYLATION AT ASN-765.
[7]	"The multifunctional peptidylglycine alpha-amidating monooxygenase gene: exon/intron organization of catalytic, processing, and routing domains." Ouafik L.H., Stoffers D.A., Campbell T.A., Johnson R.C., Bloomquist B.T., Mains R.E., Eipper B.A. Mol. Endocrinol. 6:1571-1584(1992) [PubMed: 1448112] [Abstract] Cited for: ALTERNATIVE SPLICING.
[8]	"P-CIP1, a novel protein that interacts with the cytosolic domain of peptidylglycine alpha-amidating monooxygenase, is associated with endosomes." Chen L., Johnson R.C., Milgram S.L. J. Biol. Chem. 273:33524-33532(1998) [PubMed: 9837933] [Abstract] Cited for: INTERACTION WITH RASSF9.
[9]	"Essential features of the catalytic core of peptidyl-alpha-hydroxyglycine alpha-amidating lyase." Kolhekar A.S., Bell J., Shiozaki E.N., Jin L., Keutmann H.T., Hand T.A., Mains R.E., Eipper B.A. Biochemistry 41:12384-12394(2002) [PubMed: 12369828] [Abstract] Cited for: DISULFIDE BONDS IN CATALYTIC DOMAIN.
[10]	"Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase." Prigge S.T., Kolhekar A.S., Eipper B.A., Mains R.E., Amzel L.M. Science 278:1300-1305(1997) [PubMed: 9360928] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 45-354.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U52650 , U52639, U52640, U52641, U52642, U52643, U52644, U52645, U52646, U52647, U52648, U52649 Genomic DNA. Translation: AAC05602.1.
U52653 , U52639, U52640, U52641, U52642, U52643, U52644, U52645, U52646, U52647, U52648, U52649, U52651, U52652 Genomic DNA. Translation: AAC05603.1.
U52664 , U52639, U52640, U52641, U52642, U52643, U52644, U52645, U52646, U52647, U52648, U52649, U52651, U52652, U52653, U52654, U52655, U52656, U52657, U52658, U52659, U52660, U52661, U52662, U52663 Genomic DNA. Translation: AAC05607.1.
U52664 , U52639, U52640, U52641, U52642, U52643, U52644, U52645, U52646, U52647, U52648, U52649, U52651, U52652, U52654, U52655, U52656, U52657, U52658, U52659, U52660, U52661, U52662, U52663 Genomic DNA. Translation: AAC05605.1.
U52664 , U52639, U52640, U52641, U52642, U52643, U52644, U52645, U52646, U52647, U52648, U52649, U52651, U52652, U52654, U52655, U52656, U52657, U52658, U52659, U52660, U52661, U52662 Genomic DNA. Translation: AAC05604.1.
U52664 , U52639, U52640, U52641, U52642, U52643, U52644, U52645, U52646, U52647, U52648, U52649, U52651, U52652, U52654, U52655, U52656, U52657, U52658, U52659, U52660, U52661 Genomic DNA. Translation: AAC05608.1.
U52664 , U52639, U52640, U52641, U52642, U52643, U52644, U52645, U52646, U52647, U52648, U52649, U52651, U52652, U52654, U52655, U52656, U52657, U52658, U52659, U52660, U52661, U52663 Genomic DNA. Translation: AAC05606.1.
M25732 mRNA. Translation: AAA41803.1.
M25719 mRNA. Translation: AAA41804.1.
M63662 mRNA. Translation: AAA42068.1. Sequence problems.
X59685 mRNA. Translation: CAA42206.1. Sequence problems.
X59686 mRNA. Translation: CAA42207.1.
X59687 mRNA. Translation: CAA42208.1.
X59688 mRNA. Translation: CAA42209.1.
X59689 mRNA. Translation: CAA42210.1.
M82845 mRNA. Translation: AAB00162.1.

IPI

IPI00210470.
IPI00231904.
IPI00231905.
IPI00231906.
IPI00231907.
IPI00231908.
IPI00780724.

PIR

URRTAP. A32193.

RefSeq

NP_037132.2.

UniGene

Rn.1121

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OPM	X-ray	2.10	A	45-354	[»]
1PHM	X-ray	1.90	A	45-354	[»]
1SDW	X-ray	1.85	A	43-356	[»]
1YI9	X-ray	1.70	A	47-355	[»]
1YIP	X-ray	2.20	A	45-355	[»]
1YJK	X-ray	2.00	A	50-355	[»]
1YJL	X-ray	2.40	A	50-355	[»]
3FVZ	X-ray	2.35	A	498-820	[»]
3FW0	X-ray	2.52	A	498-820	[»]
3PHM	X-ray	2.10	A	45-354	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P14925. 3 interactions.

STRING

P14925.

PTM databases

PhosphoSite

P14925.

Genome annotation databases

Ensembl

ENSRNOT00000041418; ENSRNOP00000050784; ENSRNOG00000033280; Rattus norvegicus. [Genome view]
ENSRNOT00000043451; ENSRNOP00000046774; ENSRNOG00000033280; Rattus norvegicus. [Genome view]
ENSRNOT00000044154; ENSRNOP00000040968; ENSRNOG00000033280; Rattus norvegicus. [Genome view]
ENSRNOT00000046546; ENSRNOP00000045177; ENSRNOG00000033280; Rattus norvegicus. [Genome view]
ENSRNOT00000049205; ENSRNOP00000043018; ENSRNOG00000033280; Rattus norvegicus. [Genome view]
ENSRNOT00000049286; ENSRNOP00000041777; ENSRNOG00000033280; Rattus norvegicus. [Genome view]
ENSRNOT00000052255; ENSRNOP00000041857; ENSRNOG00000033280; Rattus norvegicus. [Genome view]
ENSRNOT00000056457; ENSRNOP00000053295; ENSRNOG00000033280; Rattus norvegicus. [Genome view]

GeneID

25508.

KEGG

rno:25508.

Organism-specific databases

CTD

25508.

RGD

3252. Pam.

Phylogenomic databases

HOVERGEN

P14925.

Enzyme and pathway databases

BRENDA

1.14.17.3. 248.
4.3.2.5. 248.

Gene expression databases

ArrayExpress

P14925.

Genevestigator

P14925.

GermOnline

ENSRNOG00000033280. Rattus norvegicus.

Family and domain databases

InterPro

IPR011042. 6-blade_b-propeller_TolB-like.
IPR014784. Cu2_ascorb_mOase-like_C.
IPR014783. Cu2_ascorb_mOase_C.
IPR000323. Cu2_ascorb_mOase_N.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000720. Pep_amidat_mOase.
[Graphical view]

Gene3D

G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.
G3DSA:2.60.120.230. Cu2_ascorb_mOase_core. 1 hit.
G3DSA:2.60.120.310. Cu2_ascorb_mOase_core. 1 hit.

Pfam

PF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 hits.
[Graphical view]

PRINTS

PR00790. PAMONOXGNASE.

PROSITE

PS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

606933.

Entry information

Entry name

AMD_RAT

Accession

Primary (citable) accession number: P14925
Secondary accession number(s): P70710, Q64616, Q64668

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	November 3, 2009
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)