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P14925 (AMD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length976 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 vesiclesecretory 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.

Sequence caution

The sequence AAA42068.1 differs from that shown. Reason:

Ontologies

Keywords
   Cellular componentCytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCopper
Metal-binding
Vitamin C
Zinc
   Molecular functionLyase
Monooxygenase
Oxidoreductase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Sulfation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processcentral nervous system development

Inferred from expression pattern PubMed 9441675. Source: RGD

heart development

Inferred from expression pattern PubMed 9441675. Source: RGD

lactation

Inferred from expression pattern PubMed 16448835. Source: RGD

limb development

Inferred from expression pattern PubMed 9441675. Source: RGD

long-chain fatty acid metabolic process

Inferred from direct assay PubMed 8660675. Source: RGD

maternal process involved in female pregnancy

Inferred from expression pattern PubMed 9441675. Source: RGD

odontogenesis

Inferred from expression pattern PubMed 9441675. Source: RGD

ovulation cycle process

Inferred from expression pattern PubMed 9618561. Source: RGD

peptide amidation

Inferred from direct assay PubMed 2999151. Source: RGD

peptide metabolic process

Inferred from direct assay PubMed 18818385. Source: RGD

protein amidation

Inferred from direct assay PubMed 12075461. Source: RGD

protein homooligomerization

Inferred from direct assay PubMed 11395514. Source: RGD

protein metabolic process

Inferred from direct assay PubMed 16098968. Source: RGD

regulation of actin cytoskeleton organization

Inferred from mutant phenotype PubMed 11251076. Source: RGD

regulation of protein secretion

Inferred from mutant phenotype PubMed 11251076. Source: RGD

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20573687. Source: RGD

response to copper ion

Inferred from expression pattern PubMed 15629125. Source: RGD

response to drug

Inferred from direct assay PubMed 10347250. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 9618561. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 10347250. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 18818385. Source: RGD

response to pH

Inferred from direct assay PubMed 11395514. Source: RGD

toxin metabolic process

Inferred from direct assay PubMed 12721493. Source: RGD

   Cellular_componentcell surface

Inferred from direct assay PubMed 15905171. Source: RGD

extracellular space

Inferred from direct assay PubMed 16448835. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from direct assay PubMed 20202202. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 20202202. Source: RGD

perikaryon

Inferred from direct assay PubMed 8910496. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 8663411. Source: RGD

plasma membrane

Inferred from direct assay PubMed 8663411. Source: RGD

secretory granule

Inferred from direct assay PubMed 15539631. Source: RGD

secretory granule membrane

Inferred from direct assay PubMed 15158736. Source: RGD

trans-Golgi network

Inferred from direct assay PubMed 20573687. Source: RGD

transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-ascorbic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from direct assay PubMed 19604476. Source: RGD

copper ion binding

Inferred from direct assay PubMed 16931045. Source: RGD

peptidylamidoglycolate lyase activity

Inferred from direct assay PubMed 16405966. Source: RGD

peptidylglycine monooxygenase activity

Inferred from direct assay PubMed 16405966. Source: RGD

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 8910496. Source: RGD

zinc ion binding

Inferred from direct assay PubMed 19604476. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rassf9O888693EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.6
Propeptide26 – 3510
PRO_0000006365
Chain36 – 976941Peptidyl-glycine alpha-amidating monooxygenase
PRO_0000006366

Regions

Topological domain36 – 866831Intragranular Potential
Transmembrane867 – 89024Helical; Potential
Topological domain891 – 97686Cytoplasmic Potential
Repeat501 – 54444NHL 1
Repeat570 – 61142NHL 2
Repeat620 – 66546NHL 3
Repeat673 – 71745NHL 4
Repeat769 – 81244NHL 5
Region1 – 497497Peptidylglycine alpha-hydroxylating monooxygenase
Region498 – 820323Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
Region928 – 94518Interaction with RASSF9

Sites

Metal binding1071Copper A
Metal binding1081Copper A
Metal binding1721Copper A
Metal binding2421Copper B
Metal binding2441Copper B
Metal binding3141Copper B

Amino acid modifications

Modified residue9321Phosphoserine By similarity
Modified residue9451Phosphoserine By similarity
Modified residue9461Phosphothreonine By similarity
Modified residue9491Phosphoserine; by UHMK1 By similarity
Modified residue9651Sulfotyrosine By similarity
Glycosylation7651N-linked (GlcNAc...) Ref.6
Disulfide bond47 ↔ 186 Ref.9
Disulfide bond81 ↔ 126 Ref.9
Disulfide bond114 ↔ 131 Ref.9
Disulfide bond227 ↔ 334 Ref.9
Disulfide bond293 ↔ 315 Ref.9
Disulfide bond634 ↔ 655 Ref.9
Disulfide bond702 ↔ 713 Ref.9

Natural variations

Alternative sequence308 – 3125GTSSD → FKDTF in isoform PAM-5.
VSP_001230
Alternative sequence313 – 976664Missing in isoform PAM-5.
VSP_001231
Alternative sequence393 – 497105Missing in isoform PAM-2, isoform PAM-3, isoform PAM-3A and isoform PAM-3B.
VSP_001232
Alternative sequence498 – 51720DFHVE…LPGQV → GASRISFTQKKKCVKHCNPH in isoform PAM-4.
VSP_001236
Alternative sequence518 – 917400Missing in isoform PAM-4.
VSP_001237
Alternative sequence832 – 91786Missing in isoform PAM-3.
VSP_001234
Alternative sequence832 – 89968Missing in isoform PAM-3A.
VSP_001233
Alternative sequence900 – 91718Missing in isoform PAM-3B.
VSP_001235

Experimental info

Sequence conflict9591T → S no nucleotide entry Ref.4

Secondary structure

................................................................................................................................. 976
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PAM-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 7233021BEBEFD9B9

FASTA976108,675
        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 

« Hide

Isoform PAM-2 [UniParc].

Checksum: BA1F40E92F7B8C02
Show »

FASTA87196,825
Isoform PAM-3 [UniParc].

Checksum: D49246033AEA388B
Show »

FASTA78587,253
Isoform PAM-3A [UniParc].

Checksum: A9C822E643E870D0
Show »

FASTA80389,350
Isoform PAM-3B [UniParc].

Checksum: D4620879E16C381F
Show »

FASTA85394,728
Isoform PAM-4 [UniParc].

Checksum: DA702AEAC95B0F49
Show »

FASTA57664,102
Isoform PAM-5 [UniParc].

Checksum: 0150C054899C8326
Show »

FASTA31234,676

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 45-354.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52650 expand/collapse EMBL AC list , U52639, U52640, U52641, U52642, U52643, U52644, U52645, U52646, U52647, U52648, U52649 Genomic DNA. Translation: AAC05602.1.
U52653 expand/collapse EMBL AC list , U52639, U52640, U52641, U52642, U52643, U52644, U52645, U52646, U52647, U52648, U52649, U52651, U52652 Genomic DNA. Translation: AAC05603.1.
U52664 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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.
PIRURRTAP. A32193.
RefSeqNP_037132.2. NM_013000.2. [P14925-1]
XP_006245660.1. XM_006245598.1. [P14925-2]
XP_006245661.1. XM_006245599.1. [P14925-5]
UniGeneRn.1121.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP14925.
SMRP14925. Positions 45-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247540. 2 interactions.
IntActP14925. 3 interactions.

Chemistry

BindingDBP14925.
ChEMBLCHEMBL4963.

PTM databases

PhosphoSiteP14925.

Proteomic databases

PaxDbP14925.
PRIDEP14925.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000041418; ENSRNOP00000050784; ENSRNOG00000033280. [P14925-7]
ENSRNOT00000049205; ENSRNOP00000043018; ENSRNOG00000033280. [P14925-3]
ENSRNOT00000049286; ENSRNOP00000041777; ENSRNOG00000033280. [P14925-4]
ENSRNOT00000056457; ENSRNOP00000053295; ENSRNOG00000033280. [P14925-5]
GeneID25508.
KEGGrno:25508.

Organism-specific databases

CTD5066.
RGD3252. Pam.

Phylogenomic databases

eggNOGCOG3391.
GeneTreeENSGT00730000111058.
HOGENOMHOG000293368.
HOVERGENHBG004218.
KOK00504.
K18200.
PhylomeDBP14925.

Enzyme and pathway databases

BRENDA4.3.2.5. 5301.

Gene expression databases

GenevestigatorP14925.

Family and domain databases

Gene3D2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProIPR011042. 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]
PfamPF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 hits.
[Graphical view]
PRINTSPR00790. PAMONOXGNASE.
SUPFAMSSF49742. SSF49742. 2 hits.
PROSITEPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14925.
NextBio606933.
PROP14925.

Entry information

Entry nameAMD_RAT
AccessionPrimary (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: June 11, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references