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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

Protein has several cofactor binding sites:
  • Zn2+Note: Zn(2+) is required for the lyase reaction.
  • Cu2+Note: 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. calcium ion binding Source: RGD
  2. copper ion binding Source: RGD
  3. L-ascorbic acid binding Source: UniProtKB-KW
  4. peptidylamidoglycolate lyase activity Source: RGD
  5. peptidylglycine monooxygenase activity Source: RGD
  6. protein kinase binding Source: RGD
  7. 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 – 866831IntragranularSequence AnalysisAdd
BLAST
Transmembranei867 – 89024HelicalSequence AnalysisAdd
BLAST
Topological domaini891 – 97686CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: RGD
  2. extracellular space Source: RGD
  3. integral component of membrane Source: UniProtKB-KW
  4. neuronal cell body Source: RGD
  5. neuron projection 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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Propeptidei26 – 3510PRO_0000006365
Chaini36 – 976941Peptidyl-glycine alpha-amidating monooxygenasePRO_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 – 9321PhosphoserineBy similarity
Modified residuei945 – 9451PhosphoserineBy similarity
Modified residuei946 – 9461PhosphothreonineBy similarity
Modified residuei949 – 9491Phosphoserine; by UHMK1By similarity
Modified residuei965 – 9651SulfotyrosineBy 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

ExpressionAtlasiP14925. baseline and differential.
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

1
976
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi49 – 513Combined sources
Beta strandi53 – 564Combined sources
Beta strandi58 – 6710Combined sources
Beta strandi69 – 713Combined sources
Beta strandi75 – 8511Combined sources
Beta strandi92 – 1009Combined sources
Turni103 – 1053Combined sources
Beta strandi106 – 11813Combined sources
Beta strandi121 – 1255Combined sources
Helixi126 – 1283Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi136 – 1427Combined sources
Beta strandi154 – 1596Combined sources
Turni160 – 1623Combined sources
Beta strandi166 – 1738Combined sources
Helixi178 – 1814Combined sources
Beta strandi188 – 1969Combined sources
Beta strandi199 – 20911Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi219 – 22810Combined sources
Beta strandi234 – 24512Combined sources
Beta strandi247 – 25610Combined sources
Beta strandi259 – 2668Combined sources
Beta strandi275 – 2839Combined sources
Beta strandi288 – 2969Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi315 – 32410Combined sources
Helixi325 – 3273Combined sources
Beta strandi330 – 3345Combined sources
Beta strandi336 – 3383Combined sources
Helixi340 – 3456Combined sources
Helixi348 – 3514Combined sources
Beta strandi498 – 5036Combined sources
Helixi508 – 5114Combined sources
Beta strandi517 – 5226Combined sources
Beta strandi528 – 5325Combined sources
Helixi552 – 5543Combined sources
Beta strandi562 – 5654Combined sources
Turni567 – 5693Combined sources
Beta strandi572 – 5765Combined sources
Turni578 – 5803Combined sources
Beta strandi582 – 5898Combined sources
Beta strandi595 – 5995Combined sources
Turni600 – 6034Combined sources
Beta strandi604 – 6085Combined sources
Beta strandi617 – 6226Combined sources
Beta strandi634 – 6418Combined sources
Turni643 – 6453Combined sources
Beta strandi648 – 6525Combined sources
Beta strandi658 – 6625Combined sources
Beta strandi668 – 6725Combined sources
Beta strandi678 – 6803Combined sources
Beta strandi685 – 6873Combined sources
Beta strandi689 – 6957Combined sources
Turni696 – 6994Combined sources
Beta strandi700 – 7056Combined sources
Turni706 – 7094Combined sources
Beta strandi710 – 7156Combined sources
Turni716 – 7183Combined sources
Beta strandi721 – 7255Combined sources
Turni728 – 7325Combined sources
Beta strandi734 – 7407Combined sources
Beta strandi743 – 7486Combined sources
Beta strandi761 – 7655Combined sources
Turni766 – 7683Combined sources
Beta strandi771 – 7755Combined sources
Beta strandi778 – 7803Combined sources
Beta strandi783 – 7908Combined sources
Beta strandi794 – 80310Combined sources
Beta strandi806 – 8138Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14925.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 497497Peptidylglycine alpha-hydroxylating monooxygenaseAdd
BLAST
Regioni498 – 820323Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseAdd
BLAST
Regioni928 – 94518Interaction with RASSF9Add
BLAST

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

eggNOGiCOG3391.
GeneTreeiENSGT00730000111058.
HOGENOMiHOG000293368.
HOVERGENiHBG004218.
InParanoidiP14925.
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

        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 AAA42068.1 differs from that shown. Reason: Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti959 – 9591T → S no nucleotide entry (PubMed:2337358)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei308 – 3125GTSSD → FKDTF in isoform PAM-5. CuratedVSP_001230
Alternative sequencei313 – 976664Missing in isoform PAM-5. CuratedVSP_001231Add
BLAST
Alternative sequencei393 – 497105Missing in isoform PAM-2, isoform PAM-3, isoform PAM-3A and isoform PAM-3B. CuratedVSP_001232Add
BLAST
Alternative sequencei498 – 51720DFHVE…LPGQV → GASRISFTQKKKCVKHCNPH in isoform PAM-4. CuratedVSP_001236Add
BLAST
Alternative sequencei518 – 917400Missing in isoform PAM-4. CuratedVSP_001237Add
BLAST
Alternative sequencei832 – 91786Missing in isoform PAM-3. CuratedVSP_001234Add
BLAST
Alternative sequencei832 – 89968Missing in isoform PAM-3A. CuratedVSP_001233Add
BLAST
Alternative sequencei900 – 91718Missing in isoform PAM-3B. CuratedVSP_001235Add
BLAST

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_006245598.2. [P14925-2]
XP_006245661.1. XM_006245599.2. [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:
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 .
PIRi A32193. URRTAP.
RefSeqi NP_037132.2. NM_013000.2. [P14925-1 ]
XP_006245660.1. XM_006245598.2. [P14925-2 ]
XP_006245661.1. XM_006245599.2. [P14925-5 ]
UniGenei Rn.1121.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P14925.
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

ExpressionAtlasi P14925. baseline and differential.
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: November 26, 2014
This is version 149 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