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P14925

- AMD_RAT

UniProt

P14925 - AMD_RAT

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Protein
Peptidyl-glycine alpha-amidating monooxygenase
Gene
Pam
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

Zinc; for the lyase reaction.
Binds 2 copper ions per subunit; For the monoxygenase reaction.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi107 – 1071Copper A
Metal bindingi108 – 1081Copper A
Metal bindingi172 – 1721Copper A
Metal bindingi242 – 2421Copper B
Metal bindingi244 – 2441Copper B
Metal bindingi314 – 3141Copper B

GO - Molecular functioni

  1. L-ascorbic acid binding Source: UniProtKB-KW
  2. calcium ion binding Source: RGD
  3. copper ion binding Source: RGD
  4. peptidylamidoglycolate lyase activity Source: RGD
  5. peptidylglycine monooxygenase activity Source: RGD
  6. protein binding Source: UniProtKB
  7. protein kinase binding Source: RGD
  8. zinc ion binding Source: RGD

GO - Biological processi

  1. central nervous system development Source: RGD
  2. heart development Source: RGD
  3. lactation Source: RGD
  4. limb development Source: RGD
  5. long-chain fatty acid metabolic process Source: RGD
  6. maternal process involved in female pregnancy Source: RGD
  7. odontogenesis Source: RGD
  8. ovulation cycle process Source: RGD
  9. peptide amidation Source: RGD
  10. peptide metabolic process Source: RGD
  11. protein amidation Source: RGD
  12. protein homooligomerization Source: RGD
  13. protein metabolic process Source: RGD
  14. regulation of actin cytoskeleton organization Source: RGD
  15. regulation of protein secretion Source: RGD
  16. regulation of transcription from RNA polymerase II promoter Source: RGD
  17. response to copper ion Source: RGD
  18. response to drug Source: RGD
  19. response to estradiol Source: RGD
  20. response to glucocorticoid Source: RGD
  21. response to hypoxia Source: RGD
  22. response to pH Source: RGD
  23. 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

BRENDAi4.3.2.5. 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
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi3252. Pam.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 866831Intragranular Reviewed prediction
Add
BLAST
Transmembranei867 – 89024Helical; Reviewed prediction
Add
BLAST
Topological domaini891 – 97686Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: RGD
  2. extracellular space Source: RGD
  3. integral component of membrane Source: UniProtKB-KW
  4. neuron projection Source: RGD
  5. neuronal cell body Source: RGD
  6. perikaryon Source: RGD
  7. perinuclear region of cytoplasm Source: RGD
  8. plasma membrane Source: RGD
  9. secretory granule Source: RGD
  10. secretory granule membrane Source: RGD
  11. trans-Golgi network Source: RGD
  12. transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 Publication
Add
BLAST
Propeptidei26 – 3510
PRO_0000006365
Chaini36 – 976941Peptidyl-glycine alpha-amidating monooxygenase
PRO_0000006366Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi765 – 7651N-linked (GlcNAc...)1 Publication
Modified residuei932 – 9321Phosphoserine By similarity
Modified residuei945 – 9451Phosphoserine By similarity
Modified residuei946 – 9461Phosphothreonine By similarity
Modified residuei949 – 9491Phosphoserine; by UHMK1 By similarity
Modified residuei965 – 9651Sulfotyrosine By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP14925.
PRIDEiP14925.

PTM databases

PhosphoSiteiP14925.

Expressioni

Gene expression databases

GenevestigatoriP14925.

Interactioni

Subunit structurei

Monomer. Interacts with RASSF9.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi247540. 2 interactions.
IntActiP14925. 3 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi49 – 513
Beta strandi53 – 564
Beta strandi58 – 6710
Beta strandi69 – 713
Beta strandi75 – 8511
Beta strandi92 – 1009
Turni103 – 1053
Beta strandi106 – 11813
Beta strandi121 – 1255
Helixi126 – 1283
Beta strandi130 – 1334
Beta strandi136 – 1427
Beta strandi154 – 1596
Turni160 – 1623
Beta strandi166 – 1738
Helixi178 – 1814
Beta strandi188 – 1969
Beta strandi199 – 20911
Beta strandi211 – 2144
Beta strandi219 – 22810
Beta strandi234 – 24512
Beta strandi247 – 25610
Beta strandi259 – 2668
Beta strandi275 – 2839
Beta strandi288 – 2969
Beta strandi304 – 3063
Beta strandi315 – 32410
Helixi325 – 3273
Beta strandi330 – 3345
Beta strandi336 – 3383
Helixi340 – 3456
Helixi348 – 3514
Beta strandi498 – 5036
Helixi508 – 5114
Beta strandi517 – 5226
Beta strandi528 – 5325
Helixi552 – 5543
Beta strandi562 – 5654
Turni567 – 5693
Beta strandi572 – 5765
Turni578 – 5803
Beta strandi582 – 5898
Beta strandi595 – 5995
Turni600 – 6034
Beta strandi604 – 6085
Beta strandi617 – 6226
Beta strandi634 – 6418
Turni643 – 6453
Beta strandi648 – 6525
Beta strandi658 – 6625
Beta strandi668 – 6725
Beta strandi678 – 6803
Beta strandi685 – 6873
Beta strandi689 – 6957
Turni696 – 6994
Beta strandi700 – 7056
Turni706 – 7094
Beta strandi710 – 7156
Turni716 – 7183
Beta strandi721 – 7255
Turni728 – 7325
Beta strandi734 – 7407
Beta strandi743 – 7486
Beta strandi761 – 7655
Turni766 – 7683
Beta strandi771 – 7755
Beta strandi778 – 7803
Beta strandi783 – 7908
Beta strandi794 – 80310
Beta strandi806 – 8138

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 45-356.

Miscellaneous databases

EvolutionaryTraceiP14925.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati501 – 54444NHL 1
Add
BLAST
Repeati570 – 61142NHL 2
Add
BLAST
Repeati620 – 66546NHL 3
Add
BLAST
Repeati673 – 71745NHL 4
Add
BLAST
Repeati769 – 81244NHL 5
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 497497Peptidylglycine alpha-hydroxylating monooxygenase
Add
BLAST
Regioni498 – 820323Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
Add
BLAST
Regioni928 – 94518Interaction with RASSF9
Add
BLAST

Sequence similaritiesi

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.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3391.
GeneTreeiENSGT00730000111058.
HOGENOMiHOG000293368.
HOVERGENiHBG004218.
KOiK00504.
K18200.
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.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000720. Pep_amidat_mOase.
IPR008977. PHM/PNGase_F_dom.
[Graphical view]
PfamiPF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 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. Align

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

MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT    50
IGPVTPLDAS DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR 100
ASMDTVHHML LFGCNMPSST GSYWFCDEGT CTDKANILYA WARNAPPTRL 150
PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR DNHKDCSGVS VHLTRVPQPL 200
IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR VHTHHLGKVV 250
SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR 300
TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA 350
NIPIPVKPDM VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQGDFYSLLS 400
KLLGEREDVH VHKYNPTEKT ESGSDLVAEI ANVVQKKDLG RSDAREGAEH 450
EEWGNAILVR DRIHRFHQLE STLRPAESRA FSFQQPGEGP WEPEPSGDFH 500
VEEELDWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG NSFDSKFVYQ 550
QRGLGPIEED TILVIDPNNA EILQSSGKNL FYLPHGLSID TDGNYWVTDV 600
ALHQVFKLDP HSKEGPLLIL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV 650
SDGYCNSRIV QFSPSGKFVT QWGEESSGSS PRPGQFSVPH SLALVPHLDQ 700
LCVADRENGR IQCFKTDTKE FVREIKHASF GRNVFAISYI PGFLFAVNGK 750
PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK HFDMPHDIVA SEDGTVYIGD 800
AHTNTVWKFT LTEKMEHRSV KKAGIEVQEI KEAEAVVEPK VENKPTSSEL 850
QKMQEKQKLS TEPGSGVSVV LITTLLVIPV LVLLAIVMFI RWKKSRAFGD 900
HDRKLESSSG RVLGRFRGKG SGGLNLGNFF ASRKGYSRKG FDRVSTEGSD 950
QEKDEDDGTE SEEEYSAPLP KPAPSS 976

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 AAA42068.1 differs from that shown. Reason:

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei308 – 3125GTSSD → FKDTF in isoform PAM-5.
VSP_001230
Alternative sequencei313 – 976664Missing in isoform PAM-5.
VSP_001231Add
BLAST
Alternative sequencei393 – 497105Missing in isoform PAM-2, isoform PAM-3, isoform PAM-3A and isoform PAM-3B.
VSP_001232Add
BLAST
Alternative sequencei498 – 51720DFHVE…LPGQV → GASRISFTQKKKCVKHCNPH in isoform PAM-4.
VSP_001236Add
BLAST
Alternative sequencei518 – 917400Missing in isoform PAM-4.
VSP_001237Add
BLAST
Alternative sequencei832 – 91786Missing in isoform PAM-3.
VSP_001234Add
BLAST
Alternative sequencei832 – 89968Missing in isoform PAM-3A.
VSP_001233Add
BLAST
Alternative sequencei900 – 91718Missing in isoform PAM-3B.
VSP_001235Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti959 – 9591T → S no nucleotide entry 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006245598.1. [P14925-2]
XP_006245661.1. XM_006245599.1. [P14925-5]
UniGeneiRn.1121.

Genome annotation databases

EnsembliENSRNOT00000041418; ENSRNOP00000050784; ENSRNOG00000033280. [P14925-7]
ENSRNOT00000049205; ENSRNOP00000043018; ENSRNOG00000033280. [P14925-3]
ENSRNOT00000049286; ENSRNOP00000041777; ENSRNOG00000033280. [P14925-4]
ENSRNOT00000056457; ENSRNOP00000053295; ENSRNOG00000033280. [P14925-5]
GeneIDi25508.
KEGGirno:25508.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A32193. URRTAP.
RefSeqi NP_037132.2. NM_013000.2. [P14925-1 ]
XP_006245660.1. XM_006245598.1. [P14925-2 ]
XP_006245661.1. XM_006245599.1. [P14925-5 ]
UniGenei Rn.1121.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3MIB X-ray 2.35 A 43-356 [» ]
3MIC X-ray 2.42 A 43-356 [» ]
3MID X-ray 3.06 A 43-356 [» ]
3MIE X-ray 3.26 A 43-356 [» ]
3MIF X-ray 2.00 A 43-356 [» ]
3MIG X-ray 2.70 A 43-356 [» ]
3MIH X-ray 2.74 A 43-356 [» ]
3MLJ X-ray 2.15 A 43-356 [» ]
3MLK X-ray 3.10 A 43-356 [» ]
3MLL X-ray 3.25 A 43-356 [» ]
3PHM X-ray 2.10 A 45-354 [» ]
4E4Z X-ray 1.98 A 45-356 [» ]
ProteinModelPortali P14925.
SMRi P14925. Positions 45-356.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247540. 2 interactions.
IntActi P14925. 3 interactions.

Chemistry

BindingDBi P14925.
ChEMBLi CHEMBL4963.

PTM databases

PhosphoSitei P14925.

Proteomic databases

PaxDbi P14925.
PRIDEi P14925.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000041418 ; ENSRNOP00000050784 ; ENSRNOG00000033280 . [P14925-7 ]
ENSRNOT00000049205 ; ENSRNOP00000043018 ; ENSRNOG00000033280 . [P14925-3 ]
ENSRNOT00000049286 ; ENSRNOP00000041777 ; ENSRNOG00000033280 . [P14925-4 ]
ENSRNOT00000056457 ; ENSRNOP00000053295 ; ENSRNOG00000033280 . [P14925-5 ]
GeneIDi 25508.
KEGGi rno:25508.

Organism-specific databases

CTDi 5066.
RGDi 3252. Pam.

Phylogenomic databases

eggNOGi COG3391.
GeneTreei ENSGT00730000111058.
HOGENOMi HOG000293368.
HOVERGENi HBG004218.
KOi K00504.
K18200.
PhylomeDBi P14925.

Enzyme and pathway databases

BRENDAi 4.3.2.5. 5301.

Miscellaneous databases

EvolutionaryTracei P14925.
NextBioi 606933.
PROi P14925.

Gene expression databases

Genevestigatori P14925.

Family and domain databases

Gene3Di 2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProi 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 ]
Pfami PF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 hits.
[Graphical view ]
PRINTSi PR00790. PAMONOXGNASE.
SUPFAMi SSF49742. SSF49742. 2 hits.
PROSITEi PS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: June 11, 2014
This is version 146 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

External Data

Dasty 3

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