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Protein

ADM

Gene

ADM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels.

GO - Molecular functioni

  • receptor binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

BioCyciZFISH:ENSG00000148926-MONOMER.
ReactomeiR-HSA-418555. G alpha (s) signalling events.
R-HSA-419812. Calcitonin-like ligand receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
ADM
Cleaved into the following 2 chains:
Adrenomedullin
Short name:
AM
Alternative name(s):
ProAM N-terminal 20 peptide
Short name:
PAMP
Short name:
ProAM-N20
Gene namesi
Name:ADM
Synonyms:AM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:259. ADM.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi133.
OpenTargetsiENSG00000148926.
PharmGKBiPA24580.

Chemistry databases

ChEMBLiCHEMBL2062356.

Polymorphism and mutation databases

BioMutaiADM.
DMDMi461474.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21By similarityAdd BLAST21
PeptideiPRO_000000096122 – 41Proadrenomedullin N-20 terminal peptideBy similarityAdd BLAST20
PropeptideiPRO_000000096245 – 92By similarityAdd BLAST48
PeptideiPRO_000000096395 – 146Adrenomedullin1 PublicationAdd BLAST52
PropeptideiPRO_0000000964148 – 185PreproAM C-terminal fragmentAdd BLAST38

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei41Arginine amide1 Publication1
Disulfide bondi110 ↔ 1151 Publication
Modified residuei146Tyrosine amide1 Publication1

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

EPDiP35318.
PaxDbiP35318.
PeptideAtlasiP35318.
PRIDEiP35318.

PTM databases

iPTMnetiP35318.
PhosphoSitePlusiP35318.

Miscellaneous databases

PMAP-CutDBP35318.

Expressioni

Tissue specificityi

Highest levels found in pheochromocytoma and adrenal medulla. Also found in lung, ventricle and kidney tissues.

Gene expression databases

BgeeiENSG00000148926.
CleanExiHS_ADM.
ExpressionAtlasiP35318. baseline and differential.
GenevisibleiP35318. HS.

Organism-specific databases

HPAiCAB016075.

Interactioni

GO - Molecular functioni

  • receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi106645. 1 interactor.
IntActiP35318. 1 interactor.
STRINGi9606.ENSP00000278175.

Structurei

Secondary structure

1185
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 40Combined sources17
Beta strandi102 – 107Combined sources6
Beta strandi111 – 116Combined sources6
Helixi117 – 124Combined sources8
Beta strandi132 – 135Combined sources4
Helixi138 – 141Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FLYNMR-A22-41[»]
2L7SNMR-A95-146[»]
4RWFX-ray1.76B119-146[»]
ProteinModelPortaliP35318.
SMRiP35318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35318.

Family & Domainsi

Sequence similaritiesi

Belongs to the adrenomedullin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IK4C. Eukaryota.
ENOG41120TV. LUCA.
GeneTreeiENSGT00390000000451.
HOGENOMiHOG000033821.
HOVERGENiHBG004181.
InParanoidiP35318.
KOiK12333.
OMAiVAPRNKI.
OrthoDBiEOG091G0QFI.
PhylomeDBiP35318.
TreeFamiTF333447.

Family and domain databases

InterProiIPR001710. Adrenomedullin.
IPR021116. Calcitonin/adrenomedullin.
[Graphical view]
PfamiPF00214. Calc_CGRP_IAPP. 1 hit.
[Graphical view]
PRINTSiPR00801. ADRENOMEDULN.

Sequencei

Sequence statusi: Complete.

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

P35318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLVSVALMY LGSLAFLGAD TARLDVASEF RKKWNKWALS RGKRELRMSS
60 70 80 90 100
SYPTGLADVK AGPAQTLIRP QDMKGASRSP EDSSPDAARI RVKRYRQSMN
110 120 130 140 150
NFQGLRSFGC RFGTCTVQKL AHQIYQFTDK DKDNVAPRSK ISPQGYGRRR
160 170 180
RRSLPEAGPG RTLVSSKPQA HGAPAPPSGS APHFL
Length:185
Mass (Da):20,420
Last modified:February 1, 1994 - v1
Checksum:i64C7D2A0B4654DFE
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01486150S → R.1 PublicationCorresponds to variant rs5005dbSNPEnsembl.1
Natural variantiVAR_04820585P → R.Corresponds to variant rs2228573dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14874 mRNA. Translation: BAA03589.1.
S73906 Genomic DNA. Translation: AAC60642.1.
D43639 Genomic DNA. Translation: BAA07756.1. Sequence problems.
CR541995 mRNA. Translation: CAG46792.1.
BT006902 mRNA. Translation: AAP35548.1.
AK312893 mRNA. Translation: BAG35740.1.
DQ143945 Genomic DNA. Translation: AAZ38717.1.
CH471064 Genomic DNA. Translation: EAW68571.1.
CH471064 Genomic DNA. Translation: EAW68572.1.
BC015961 mRNA. Translation: AAH15961.1.
CCDSiCCDS7801.1.
PIRiJC2351. JN0684.
RefSeqiNP_001115.1. NM_001124.2.
UniGeneiHs.441047.

Genome annotation databases

EnsembliENST00000278175; ENSP00000278175; ENSG00000148926.
ENST00000525063; ENSP00000435124; ENSG00000148926.
ENST00000528655; ENSP00000436607; ENSG00000148926.
GeneIDi133.
KEGGihsa:133.
UCSCiuc001mil.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14874 mRNA. Translation: BAA03589.1.
S73906 Genomic DNA. Translation: AAC60642.1.
D43639 Genomic DNA. Translation: BAA07756.1. Sequence problems.
CR541995 mRNA. Translation: CAG46792.1.
BT006902 mRNA. Translation: AAP35548.1.
AK312893 mRNA. Translation: BAG35740.1.
DQ143945 Genomic DNA. Translation: AAZ38717.1.
CH471064 Genomic DNA. Translation: EAW68571.1.
CH471064 Genomic DNA. Translation: EAW68572.1.
BC015961 mRNA. Translation: AAH15961.1.
CCDSiCCDS7801.1.
PIRiJC2351. JN0684.
RefSeqiNP_001115.1. NM_001124.2.
UniGeneiHs.441047.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FLYNMR-A22-41[»]
2L7SNMR-A95-146[»]
4RWFX-ray1.76B119-146[»]
ProteinModelPortaliP35318.
SMRiP35318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106645. 1 interactor.
IntActiP35318. 1 interactor.
STRINGi9606.ENSP00000278175.

Chemistry databases

ChEMBLiCHEMBL2062356.

PTM databases

iPTMnetiP35318.
PhosphoSitePlusiP35318.

Polymorphism and mutation databases

BioMutaiADM.
DMDMi461474.

Proteomic databases

EPDiP35318.
PaxDbiP35318.
PeptideAtlasiP35318.
PRIDEiP35318.

Protocols and materials databases

DNASUi133.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278175; ENSP00000278175; ENSG00000148926.
ENST00000525063; ENSP00000435124; ENSG00000148926.
ENST00000528655; ENSP00000436607; ENSG00000148926.
GeneIDi133.
KEGGihsa:133.
UCSCiuc001mil.2. human.

Organism-specific databases

CTDi133.
DisGeNETi133.
GeneCardsiADM.
HGNCiHGNC:259. ADM.
HPAiCAB016075.
MIMi103275. gene.
neXtProtiNX_P35318.
OpenTargetsiENSG00000148926.
PharmGKBiPA24580.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IK4C. Eukaryota.
ENOG41120TV. LUCA.
GeneTreeiENSGT00390000000451.
HOGENOMiHOG000033821.
HOVERGENiHBG004181.
InParanoidiP35318.
KOiK12333.
OMAiVAPRNKI.
OrthoDBiEOG091G0QFI.
PhylomeDBiP35318.
TreeFamiTF333447.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000148926-MONOMER.
ReactomeiR-HSA-418555. G alpha (s) signalling events.
R-HSA-419812. Calcitonin-like ligand receptors.

Miscellaneous databases

ChiTaRSiADM. human.
EvolutionaryTraceiP35318.
GeneWikiiAdrenomedullin.
GenomeRNAii133.
PMAP-CutDBP35318.
PROiP35318.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000148926.
CleanExiHS_ADM.
ExpressionAtlasiP35318. baseline and differential.
GenevisibleiP35318. HS.

Family and domain databases

InterProiIPR001710. Adrenomedullin.
IPR021116. Calcitonin/adrenomedullin.
[Graphical view]
PfamiPF00214. Calc_CGRP_IAPP. 1 hit.
[Graphical view]
PRINTSiPR00801. ADRENOMEDULN.
ProtoNetiSearch...

Entry informationi

Entry nameiADML_HUMAN
AccessioniPrimary (citable) accession number: P35318
Secondary accession number(s): B2R793, D3DQV3, Q6FGW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 2, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.