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Protein

ADM

Gene

Adm

Organism
Rattus norvegicus (Rat)
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.

GO - Molecular functioni

  • adrenomedullin receptor binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • androgen metabolic process Source: RGD
  • antibacterial humoral response Source: Ensembl
  • branching involved in labyrinthine layer morphogenesis Source: Ensembl
  • calcium ion homeostasis Source: RGD
  • cAMP biosynthetic process Source: Ensembl
  • cAMP-mediated signaling Source: RGD
  • defense response to Gram-negative bacterium Source: Ensembl
  • defense response to Gram-positive bacterium Source: Ensembl
  • developmental growth Source: Ensembl
  • female pregnancy Source: RGD
  • G-protein coupled receptor internalization Source: Ensembl
  • heart development Source: Ensembl
  • hormone secretion Source: RGD
  • negative regulation of cell proliferation Source: RGD
  • negative regulation of vascular permeability Source: Ensembl
  • negative regulation of vasoconstriction Source: Ensembl
  • neural tube closure Source: Ensembl
  • neuron projection regeneration Source: RGD
  • odontogenesis of dentin-containing tooth Source: RGD
  • organ regeneration Source: RGD
  • positive regulation of angiogenesis Source: Ensembl
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of cAMP biosynthetic process Source: Ensembl
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of cytosolic calcium ion concentration Source: RGD
  • positive regulation of heart rate Source: RGD
  • positive regulation of vasculogenesis Source: Ensembl
  • positive regulation of vasodilation Source: RGD
  • regulation of the force of heart contraction Source: RGD
  • response to cold Source: RGD
  • response to glucocorticoid Source: RGD
  • response to hypoxia Source: RGD
  • response to insulin Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to organic substance Source: RGD
  • response to starvation Source: RGD
  • response to wounding Source: RGD
  • spongiotrophoblast layer development Source: Ensembl
  • vascular smooth muscle cell development Source: Ensembl
  • vasculogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiR-RNO-418555. G alpha (s) signalling events.
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2047. Adm.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121By similarityAdd
BLAST
Peptidei22 – 4120Proadrenomedullin N-20 terminal peptide1 PublicationPRO_0000000973Add
BLAST
Propeptidei45 – 91471 PublicationPRO_0000000974Add
BLAST
Peptidei94 – 14350Adrenomedullin1 PublicationPRO_0000000975Add
BLAST
Propeptidei150 – 18536PreproAM C-terminal fragment1 PublicationPRO_0000000976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Arginine amide1 Publication
Disulfide bondi107 ↔ 112By similarity
Modified residuei143 – 1431Tyrosine amide1 Publication

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiP43145.

PTM databases

iPTMnetiP43145.
PhosphoSiteiP43145.

Expressioni

Tissue specificityi

Expressed in adrenal glands, lung, kidney, heart, spleen, duodenum and submandibular glands.

Gene expression databases

GenevisibleiP43145. RN.

Interactioni

GO - Molecular functioni

  • adrenomedullin receptor binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000035811.

Family & Domainsi

Sequence similaritiesi

Belongs to the adrenomedullin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IK4C. Eukaryota.
ENOG41120TV. LUCA.
GeneTreeiENSGT00390000000451.
HOGENOMiHOG000033821.
HOVERGENiHBG004181.
InParanoidiP43145.
KOiK12333.
OMAiVAPRNKI.
OrthoDBiEOG7DC266.
PhylomeDBiP43145.
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.

P43145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLVSIALML LGSLAVLGAD TARLDTSSQF RKKWNKWALS RGKRELQASS
60 70 80 90 100
SYPTGLVDEK TVPTQTLGLQ DKQSTSSTPQ ASTQSTAHIR VKRYRQSMNQ
110 120 130 140 150
GSRSTGCRFG TCTMQKLAHQ IYQFTDKDKD GMAPRNKISP QGYGRRRRRS
160 170 180
LPEVLRARTV ESSQEQTHSA PASPAHQDIS RVSRL
Length:185
Mass (Da):20,636
Last modified:November 1, 1995 - v1
Checksum:i35CAD9A9DD19AE35
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D15069 mRNA. Translation: BAA03665.1.
U15419 mRNA. Translation: AAB60519.1.
BC061775 mRNA. Translation: AAH61775.1.
PIRiJN0766.
RefSeqiNP_036847.1. NM_012715.1.
XP_008757909.1. XM_008759687.1.
UniGeneiRn.10232.

Genome annotation databases

EnsembliENSRNOT00000036718; ENSRNOP00000035811; ENSRNOG00000027030.
GeneIDi25026.
KEGGirno:25026.
UCSCiRGD:2047. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D15069 mRNA. Translation: BAA03665.1.
U15419 mRNA. Translation: AAB60519.1.
BC061775 mRNA. Translation: AAH61775.1.
PIRiJN0766.
RefSeqiNP_036847.1. NM_012715.1.
XP_008757909.1. XM_008759687.1.
UniGeneiRn.10232.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000035811.

PTM databases

iPTMnetiP43145.
PhosphoSiteiP43145.

Proteomic databases

PaxDbiP43145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000036718; ENSRNOP00000035811; ENSRNOG00000027030.
GeneIDi25026.
KEGGirno:25026.
UCSCiRGD:2047. rat.

Organism-specific databases

CTDi133.
RGDi2047. Adm.

Phylogenomic databases

eggNOGiENOG410IK4C. Eukaryota.
ENOG41120TV. LUCA.
GeneTreeiENSGT00390000000451.
HOGENOMiHOG000033821.
HOVERGENiHBG004181.
InParanoidiP43145.
KOiK12333.
OMAiVAPRNKI.
OrthoDBiEOG7DC266.
PhylomeDBiP43145.
TreeFamiTF333447.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP43145.

Gene expression databases

GenevisibleiP43145. RN.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and biological activities of rat adrenomedullin, a hypotensive peptide."
    Sakata J., Shimokuba T., Kitamura K., Nakamura S., Kangawa K., Matsuo H., Eto T.
    Biochem. Biophys. Res. Commun. 195:921-927(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Adrenal gland.
  2. "Discovery of adrenomedullin in rat ischemic cortex and evidence for its role in exacerbating focal brain ischemic damage."
    Wang X., Yue T.L., Barone F.C., White R.F., Clark R.K., Willette R.N., Sulpizio A.C., Aiyar N.V., Ruffolo R.R. Jr., Feuerstein G.Z.
    Proc. Natl. Acad. Sci. U.S.A. 92:11480-11484(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  4. Cited for: PROTEOLYTIC PROCESSING, AMIDATION AT ARG-41 AND TYR-143, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiADML_RAT
AccessioniPrimary (citable) accession number: P43145
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. 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.