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Protein

ADM

Gene

ADM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • adrenomedullin receptor binding Source: UniProtKB
  • hormone activity Source: UniProtKB-KW
  • receptor binding Source: ProtInc

GO - Biological processi

  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • adrenomedullin receptor signaling pathway Source: UniProtKB
  • aging Source: Ensembl
  • amylin receptor signaling pathway Source: ARUK-UCL
  • androgen metabolic process Source: Ensembl
  • animal organ regeneration Source: Ensembl
  • antibacterial humoral response Source: UniProtKB
  • antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
  • blood circulation Source: ProtInc
  • branching involved in labyrinthine layer morphogenesis Source: Ensembl
  • cAMP biosynthetic process Source: ProtInc
  • cell-cell signaling Source: ProtInc
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • developmental growth Source: Ensembl
  • female pregnancy Source: ProtInc
  • G-protein coupled receptor internalization Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: Reactome
  • heart development Source: Ensembl
  • hormone secretion Source: Ensembl
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of vascular permeability Source: Ensembl
  • negative regulation of vasoconstriction Source: BHF-UCL
  • neural tube closure Source: Ensembl
  • neuron projection regeneration Source: Ensembl
  • odontogenesis of dentin-containing tooth Source: Ensembl
  • positive regulation of angiogenesis Source: Ensembl
  • positive regulation of apoptotic process Source: Ensembl
  • positive regulation of cAMP metabolic process Source: ARUK-UCL
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of cytosolic calcium ion concentration Source: Ensembl
  • positive regulation of heart rate Source: UniProtKB
  • positive regulation of vasculogenesis Source: Ensembl
  • progesterone biosynthetic process Source: ProtInc
  • receptor internalization Source: UniProtKB
  • regulation of systemic arterial blood pressure Source: UniProtKB
  • regulation of the force of heart contraction Source: Ensembl
  • regulation of urine volume Source: UniProtKB
  • response to cold Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to insulin Source: Ensembl
  • response to lipopolysaccharide Source: Ensembl
  • response to starvation Source: Ensembl
  • response to wounding Source: ProtInc
  • signal transduction Source: ProtInc
  • spongiotrophoblast layer development Source: Ensembl
  • vascular smooth muscle cell development Source: Ensembl
  • vasculogenesis Source: UniProtKB

Keywordsi

Molecular functionHormone

Enzyme and pathway databases

ReactomeiR-HSA-418555 G alpha (s) signalling events
R-HSA-419812 Calcitonin-like ligand receptors
SIGNORiP35318

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

EuPathDBiHostDB:ENSG00000148926.9
HGNCiHGNC:259 ADM
MIMi103275 gene
neXtProtiNX_P35318

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

PaxDbiP35318
PeptideAtlasiP35318
PRIDEiP35318

PTM databases

iPTMnetiP35318
PhosphoSitePlusiP35318

Miscellaneous databases

PMAP-CutDBiP35318

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

  • adrenomedullin receptor binding Source: UniProtKB
  • hormone activity Source: UniProtKB-KW
  • 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[»]
5V6YX-ray2.80E/F/G/H131-146[»]
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
OMAiRNKISPQ
OrthoDBiEOG091G0QFI
PhylomeDBiP35318
TreeFamiTF333447

Family and domain databases

InterProiView protein in InterPro
IPR001710 Adrenomedullin
IPR021116 Calcitonin/adrenomedullin
PfamiView protein in Pfam
PF00214 Calc_CGRP_IAPP, 1 hit
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 → R1 PublicationCorresponds to variant dbSNP:rs5005Ensembl.1
Natural variantiVAR_04820585P → R. Corresponds to variant dbSNP:rs2228573Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiADML_HUMAN
AccessioniPrimary (citable) accession number: P35318
Secondary accession number(s): B2R793, D3DQV3, Q6FGW2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 28, 2018
This is version 165 of the entry and version 1 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health