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Protein

Peptidyl-glycine alpha-amidating monooxygenase

Gene

Pam

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O.
Peptidylamidoglycolate = peptidyl amide + glyoxylate.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+Note: Zn2+ is required for the lyase reaction.
  • Cu2+Note: Binds 2 copper ions per subunit for the monooxygenase reaction.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi107Copper A1
Metal bindingi108Copper A1
Metal bindingi172Copper A1
Metal bindingi242Copper B1
Metal bindingi244Copper B1
Metal bindingi314Copper B1

GO - Molecular functioni

  • calcium ion binding Source: RGD
  • copper ion binding Source: RGD
  • L-ascorbic acid binding Source: UniProtKB-KW
  • peptidylamidoglycolate lyase activity Source: RGD
  • peptidylglycine monooxygenase activity Source: RGD
  • protein kinase binding Source: RGD
  • zinc ion binding Source: RGD

GO - Biological processi

  • central nervous system development Source: RGD
  • heart development Source: RGD
  • lactation Source: RGD
  • limb development Source: RGD
  • long-chain fatty acid metabolic process Source: RGD
  • maternal process involved in female pregnancy Source: RGD
  • odontogenesis Source: RGD
  • ovulation cycle process Source: RGD
  • peptide amidation Source: RGD
  • peptide metabolic process Source: RGD
  • protein amidation Source: RGD
  • protein homooligomerization Source: RGD
  • protein metabolic process Source: RGD
  • regulation of actin cytoskeleton organization Source: RGD
  • regulation of protein secretion Source: RGD
  • regulation of transcription from RNA polymerase II promoter Source: RGD
  • response to copper ion Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to glucocorticoid Source: RGD
  • response to hypoxia Source: RGD
  • response to pH Source: RGD
  • toxin metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Vitamin C, Zinc

Enzyme and pathway databases

BRENDAi1.14.17.3. 5301.
4.3.2.5. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-glycine alpha-amidating monooxygenase
Short name:
PAM
Including the following 2 domains:
Peptidylglycine alpha-hydroxylating monooxygenase (EC:1.14.17.3)
Short name:
PHM
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC:4.3.2.5)
Alternative name(s):
Peptidylamidoglycolate lyase
Short name:
PAL
Gene namesi
Name:Pam
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi3252. Pam.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini36 – 866IntragranularSequence analysisAdd BLAST831
Transmembranei867 – 890HelicalSequence analysisAdd BLAST24
Topological domaini891 – 976CytoplasmicSequence analysisAdd BLAST86

GO - Cellular componenti

  • cell surface Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • perikaryon Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • secretory granule Source: RGD
  • secretory granule membrane Source: RGD
  • trans-Golgi network Source: RGD
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4963.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
PropeptideiPRO_000000636526 – 3510
ChainiPRO_000000636636 – 976Peptidyl-glycine alpha-amidating monooxygenaseAdd BLAST941

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi47 ↔ 1861 Publication
Disulfide bondi81 ↔ 1261 Publication
Disulfide bondi114 ↔ 1311 Publication
Disulfide bondi227 ↔ 3341 Publication
Disulfide bondi293 ↔ 3151 Publication
Disulfide bondi634 ↔ 6551 Publication
Disulfide bondi702 ↔ 7131 Publication
Glycosylationi765N-linked (GlcNAc...)1 Publication1
Modified residuei921PhosphoserineBy similarity1
Modified residuei932PhosphoserineBy similarity1
Modified residuei945PhosphoserineCombined sources1
Modified residuei946PhosphothreonineBy similarity1
Modified residuei949PhosphoserineCombined sources1
Modified residuei959PhosphothreonineCombined sources1
Modified residuei961PhosphoserineCombined sources1
Modified residuei965SulfotyrosineBy similarity1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

PaxDbiP14925.
PRIDEiP14925.

PTM databases

iPTMnetiP14925.
PhosphoSitePlusiP14925.

Expressioni

Gene expression databases

BgeeiENSRNOG00000033280.
ExpressionAtlasiP14925. baseline and differential.
GenevisibleiP14925. RN.

Interactioni

Subunit structurei

Monomer. Interacts with RASSF9.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Rassf9O888693EBI-1395008,EBI-1395057

GO - Molecular functioni

  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi247540. 2 interactors.
IntActiP14925. 3 interactors.
STRINGi10116.ENSRNOP00000046774.

Chemistry databases

BindingDBiP14925.

Structurei

Secondary structure

1976
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi49 – 51Combined sources3
Beta strandi53 – 56Combined sources4
Beta strandi58 – 67Combined sources10
Beta strandi69 – 71Combined sources3
Beta strandi75 – 85Combined sources11
Beta strandi92 – 100Combined sources9
Turni103 – 105Combined sources3
Beta strandi106 – 118Combined sources13
Beta strandi121 – 125Combined sources5
Helixi126 – 128Combined sources3
Beta strandi130 – 133Combined sources4
Beta strandi136 – 142Combined sources7
Beta strandi154 – 159Combined sources6
Turni160 – 162Combined sources3
Beta strandi166 – 173Combined sources8
Helixi178 – 181Combined sources4
Beta strandi188 – 196Combined sources9
Beta strandi199 – 209Combined sources11
Beta strandi211 – 214Combined sources4
Beta strandi219 – 228Combined sources10
Beta strandi234 – 245Combined sources12
Beta strandi247 – 256Combined sources10
Beta strandi259 – 266Combined sources8
Beta strandi275 – 283Combined sources9
Beta strandi288 – 296Combined sources9
Beta strandi304 – 306Combined sources3
Beta strandi315 – 324Combined sources10
Helixi325 – 327Combined sources3
Beta strandi330 – 334Combined sources5
Beta strandi336 – 338Combined sources3
Helixi340 – 345Combined sources6
Helixi348 – 351Combined sources4
Beta strandi498 – 503Combined sources6
Helixi508 – 511Combined sources4
Beta strandi517 – 522Combined sources6
Beta strandi528 – 532Combined sources5
Helixi552 – 554Combined sources3
Beta strandi562 – 565Combined sources4
Turni567 – 569Combined sources3
Beta strandi572 – 576Combined sources5
Turni578 – 580Combined sources3
Beta strandi582 – 589Combined sources8
Beta strandi595 – 599Combined sources5
Turni600 – 603Combined sources4
Beta strandi604 – 608Combined sources5
Beta strandi617 – 622Combined sources6
Beta strandi634 – 641Combined sources8
Turni643 – 645Combined sources3
Beta strandi648 – 652Combined sources5
Beta strandi658 – 662Combined sources5
Beta strandi668 – 672Combined sources5
Beta strandi678 – 680Combined sources3
Beta strandi685 – 687Combined sources3
Beta strandi689 – 695Combined sources7
Turni696 – 699Combined sources4
Beta strandi700 – 705Combined sources6
Turni706 – 709Combined sources4
Beta strandi710 – 715Combined sources6
Turni716 – 718Combined sources3
Beta strandi721 – 725Combined sources5
Turni728 – 732Combined sources5
Beta strandi734 – 740Combined sources7
Beta strandi743 – 748Combined sources6
Beta strandi761 – 765Combined sources5
Turni766 – 768Combined sources3
Beta strandi771 – 775Combined sources5
Beta strandi778 – 780Combined sources3
Beta strandi783 – 790Combined sources8
Beta strandi794 – 803Combined sources10
Beta strandi806 – 813Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OPMX-ray2.10A45-354[»]
1PHMX-ray1.90A45-354[»]
1SDWX-ray1.85A43-356[»]
1YI9X-ray1.70A47-355[»]
1YIPX-ray2.20A45-355[»]
1YJKX-ray2.00A50-355[»]
1YJLX-ray2.40A50-355[»]
3FVZX-ray2.35A498-820[»]
3FW0X-ray2.52A498-820[»]
3MIBX-ray2.35A43-356[»]
3MICX-ray2.42A43-356[»]
3MIDX-ray3.06A43-356[»]
3MIEX-ray3.26A43-356[»]
3MIFX-ray2.00A43-356[»]
3MIGX-ray2.70A43-356[»]
3MIHX-ray2.74A43-356[»]
3MLJX-ray2.15A43-356[»]
3MLKX-ray3.10A43-356[»]
3MLLX-ray3.25A43-356[»]
3PHMX-ray2.10A45-354[»]
4E4ZX-ray1.98A45-356[»]
ProteinModelPortaliP14925.
SMRiP14925.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14925.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati501 – 544NHL 1Add BLAST44
Repeati570 – 611NHL 2Add BLAST42
Repeati620 – 665NHL 3Add BLAST46
Repeati673 – 717NHL 4Add BLAST45
Repeati769 – 812NHL 5Add BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 497Peptidylglycine alpha-hydroxylating monooxygenaseAdd BLAST497
Regioni498 – 820Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseAdd BLAST323
Regioni928 – 945Interaction with RASSF91 PublicationAdd BLAST18

Sequence similaritiesi

In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.Curated
In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.Curated
Contains 5 NHL repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3567. Eukaryota.
ENOG410XS0X. LUCA.
GeneTreeiENSGT00730000111058.
HOGENOMiHOG000293368.
HOVERGENiHBG004218.
InParanoidiP14925.
KOiK00504.
K18200.
OMAiMDTVHHM.
PhylomeDBiP14925.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR011042. 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.
IPR024548. Cu2_monoox_C.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000720. PHM/PAL.
IPR008977. PHM/PNGase_F_dom.
[Graphical view]
PfamiPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 3 hits.
[Graphical view]
PRINTSiPR00790. PAMONOXGNASE.
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform PAM-1 (identifier: P14925-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT
60 70 80 90 100
IGPVTPLDAS DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR
110 120 130 140 150
ASMDTVHHML LFGCNMPSST GSYWFCDEGT CTDKANILYA WARNAPPTRL
160 170 180 190 200
PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR DNHKDCSGVS VHLTRVPQPL
210 220 230 240 250
IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR VHTHHLGKVV
260 270 280 290 300
SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR
310 320 330 340 350
TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA
360 370 380 390 400
NIPIPVKPDM VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQGDFYSLLS
410 420 430 440 450
KLLGEREDVH VHKYNPTEKT ESGSDLVAEI ANVVQKKDLG RSDAREGAEH
460 470 480 490 500
EEWGNAILVR DRIHRFHQLE STLRPAESRA FSFQQPGEGP WEPEPSGDFH
510 520 530 540 550
VEEELDWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG NSFDSKFVYQ
560 570 580 590 600
QRGLGPIEED TILVIDPNNA EILQSSGKNL FYLPHGLSID TDGNYWVTDV
610 620 630 640 650
ALHQVFKLDP HSKEGPLLIL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV
660 670 680 690 700
SDGYCNSRIV QFSPSGKFVT QWGEESSGSS PRPGQFSVPH SLALVPHLDQ
710 720 730 740 750
LCVADRENGR IQCFKTDTKE FVREIKHASF GRNVFAISYI PGFLFAVNGK
760 770 780 790 800
PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK HFDMPHDIVA SEDGTVYIGD
810 820 830 840 850
AHTNTVWKFT LTEKMEHRSV KKAGIEVQEI KEAEAVVEPK VENKPTSSEL
860 870 880 890 900
QKMQEKQKLS TEPGSGVSVV LITTLLVIPV LVLLAIVMFI RWKKSRAFGD
910 920 930 940 950
HDRKLESSSG RVLGRFRGKG SGGLNLGNFF ASRKGYSRKG FDRVSTEGSD
960 970
QEKDEDDGTE SEEEYSAPLP KPAPSS
Note: Membrane-bound.
Length:976
Mass (Da):108,675
Last modified:April 1, 1990 - v1
Checksum:i7233021BEBEFD9B9
GO
Isoform PAM-2 (identifier: P14925-2) [UniParc]FASTAAdd to basket

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

Note: Membrane-bound.
Show »
Length:871
Mass (Da):96,825
Checksum:iBA1F40E92F7B8C02
GO
Isoform PAM-3 (identifier: P14925-3) [UniParc]FASTAAdd to basket

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

Note: Soluble.
Show »
Length:785
Mass (Da):87,253
Checksum:iD49246033AEA388B
GO
Isoform PAM-3A (identifier: P14925-4) [UniParc]FASTAAdd to basket

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

Note: Soluble.
Show »
Length:803
Mass (Da):89,350
Checksum:iA9C822E643E870D0
GO
Isoform PAM-3B (identifier: P14925-5) [UniParc]FASTAAdd to basket

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

Note: Membrane-bound.
Show »
Length:853
Mass (Da):94,728
Checksum:iD4620879E16C381F
GO
Isoform PAM-4 (identifier: P14925-6) [UniParc]FASTAAdd to basket

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

Note: Soluble.
Show »
Length:576
Mass (Da):64,102
Checksum:iDA702AEAC95B0F49
GO
Isoform PAM-5 (identifier: P14925-7) [UniParc]FASTAAdd to basket

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

Note: Soluble.
Show »
Length:312
Mass (Da):34,676
Checksum:i0150C054899C8326
GO

Sequence cautioni

The sequence AAA42068 differs from that shown.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti959T → S no nucleotide entry (PubMed:2337358).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001230308 – 312GTSSD → FKDTF in isoform PAM-5. Curated5
Alternative sequenceiVSP_001231313 – 976Missing in isoform PAM-5. CuratedAdd BLAST664
Alternative sequenceiVSP_001232393 – 497Missing in isoform PAM-2, isoform PAM-3, isoform PAM-3A and isoform PAM-3B. CuratedAdd BLAST105
Alternative sequenceiVSP_001236498 – 517DFHVE…LPGQV → GASRISFTQKKKCVKHCNPH in isoform PAM-4. CuratedAdd BLAST20
Alternative sequenceiVSP_001237518 – 917Missing in isoform PAM-4. CuratedAdd BLAST400
Alternative sequenceiVSP_001234832 – 917Missing in isoform PAM-3. CuratedAdd BLAST86
Alternative sequenceiVSP_001233832 – 899Missing in isoform PAM-3A. CuratedAdd BLAST68
Alternative sequenceiVSP_001235900 – 917Missing in isoform PAM-3B. CuratedAdd BLAST18

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
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.
PIRiA32193. URRTAP.
RefSeqiNP_037132.2. NM_013000.2. [P14925-1]
XP_006245660.1. XM_006245598.3. [P14925-2]
XP_006245661.1. XM_006245599.3. [P14925-5]
UniGeneiRn.1121.

Genome annotation databases

EnsembliENSRNOT00000041418; ENSRNOP00000050784; ENSRNOG00000033280. [P14925-7]
ENSRNOT00000043451; ENSRNOP00000046774; ENSRNOG00000033280. [P14925-1]
ENSRNOT00000056457; ENSRNOP00000053295; ENSRNOG00000033280. [P14925-5]
GeneIDi25508.
KEGGirno:25508.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
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.
PIRiA32193. URRTAP.
RefSeqiNP_037132.2. NM_013000.2. [P14925-1]
XP_006245660.1. XM_006245598.3. [P14925-2]
XP_006245661.1. XM_006245599.3. [P14925-5]
UniGeneiRn.1121.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OPMX-ray2.10A45-354[»]
1PHMX-ray1.90A45-354[»]
1SDWX-ray1.85A43-356[»]
1YI9X-ray1.70A47-355[»]
1YIPX-ray2.20A45-355[»]
1YJKX-ray2.00A50-355[»]
1YJLX-ray2.40A50-355[»]
3FVZX-ray2.35A498-820[»]
3FW0X-ray2.52A498-820[»]
3MIBX-ray2.35A43-356[»]
3MICX-ray2.42A43-356[»]
3MIDX-ray3.06A43-356[»]
3MIEX-ray3.26A43-356[»]
3MIFX-ray2.00A43-356[»]
3MIGX-ray2.70A43-356[»]
3MIHX-ray2.74A43-356[»]
3MLJX-ray2.15A43-356[»]
3MLKX-ray3.10A43-356[»]
3MLLX-ray3.25A43-356[»]
3PHMX-ray2.10A45-354[»]
4E4ZX-ray1.98A45-356[»]
ProteinModelPortaliP14925.
SMRiP14925.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247540. 2 interactors.
IntActiP14925. 3 interactors.
STRINGi10116.ENSRNOP00000046774.

Chemistry databases

BindingDBiP14925.
ChEMBLiCHEMBL4963.

PTM databases

iPTMnetiP14925.
PhosphoSitePlusiP14925.

Proteomic databases

PaxDbiP14925.
PRIDEiP14925.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000041418; ENSRNOP00000050784; ENSRNOG00000033280. [P14925-7]
ENSRNOT00000043451; ENSRNOP00000046774; ENSRNOG00000033280. [P14925-1]
ENSRNOT00000056457; ENSRNOP00000053295; ENSRNOG00000033280. [P14925-5]
GeneIDi25508.
KEGGirno:25508.

Organism-specific databases

CTDi5066.
RGDi3252. Pam.

Phylogenomic databases

eggNOGiKOG3567. Eukaryota.
ENOG410XS0X. LUCA.
GeneTreeiENSGT00730000111058.
HOGENOMiHOG000293368.
HOVERGENiHBG004218.
InParanoidiP14925.
KOiK00504.
K18200.
OMAiMDTVHHM.
PhylomeDBiP14925.

Enzyme and pathway databases

BRENDAi1.14.17.3. 5301.
4.3.2.5. 5301.

Miscellaneous databases

EvolutionaryTraceiP14925.
PROiP14925.

Gene expression databases

BgeeiENSRNOG00000033280.
ExpressionAtlasiP14925. baseline and differential.
GenevisibleiP14925. RN.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR011042. 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.
IPR024548. Cu2_monoox_C.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000720. PHM/PAL.
IPR008977. PHM/PNGase_F_dom.
[Graphical view]
PfamiPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 3 hits.
[Graphical view]
PRINTSiPR00790. PAMONOXGNASE.
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMD_RAT
AccessioniPrimary (citable) accession number: P14925
Secondary accession number(s): P70710, Q64616, Q64668
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.