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P35318

- ADML_HUMAN

UniProt

P35318 - ADML_HUMAN

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Protein

ADM

Gene

ADM

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. receptor binding Source: ProtInc

GO - Biological processi

  1. aging Source: Ensembl
  2. androgen metabolic process Source: Ensembl
  3. blood circulation Source: ProtInc
  4. branching involved in labyrinthine layer morphogenesis Source: Ensembl
  5. cAMP biosynthetic process Source: UniProtKB
  6. cAMP-mediated signaling Source: Ensembl
  7. cell-cell signaling Source: ProtInc
  8. developmental growth Source: Ensembl
  9. female pregnancy Source: ProtInc
  10. G-protein coupled receptor internalization Source: UniProtKB
  11. heart development Source: Ensembl
  12. hormone secretion Source: Ensembl
  13. negative regulation of cell proliferation Source: Ensembl
  14. negative regulation of vascular permeability Source: Ensembl
  15. negative regulation of vasoconstriction Source: BHF-UCL
  16. neural tube closure Source: Ensembl
  17. neuron projection regeneration Source: Ensembl
  18. odontogenesis of dentin-containing tooth Source: Ensembl
  19. organ regeneration Source: Ensembl
  20. positive regulation of angiogenesis Source: Ensembl
  21. positive regulation of apoptotic process Source: Ensembl
  22. positive regulation of cAMP biosynthetic process Source: UniProtKB
  23. positive regulation of cell proliferation Source: Ensembl
  24. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  25. positive regulation of heart rate Source: Ensembl
  26. positive regulation of vasculogenesis Source: Ensembl
  27. positive regulation of vasodilation Source: Ensembl
  28. progesterone biosynthetic process Source: ProtInc
  29. receptor internalization Source: UniProtKB
  30. regulation of the force of heart contraction Source: Ensembl
  31. response to cold Source: Ensembl
  32. response to glucocorticoid Source: Ensembl
  33. response to hypoxia Source: Ensembl
  34. response to insulin Source: Ensembl
  35. response to lipopolysaccharide Source: Ensembl
  36. response to starvation Source: Ensembl
  37. response to wounding Source: ProtInc
  38. signal transduction Source: ProtInc
  39. spongiotrophoblast layer development Source: Ensembl
  40. vascular smooth muscle cell development Source: Ensembl
  41. vasculogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_18290. Calcitonin-like ligand receptors.
REACT_19327. G alpha (s) signalling events.

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
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:259. ADM.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. extracellular region Source: Reactome
  3. extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24580.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Peptidei22 – 4120Proadrenomedullin N-20 terminal peptidePRO_0000000961Add
BLAST
Propeptidei45 – 9248PRO_0000000962Add
BLAST
Peptidei95 – 14652AdrenomedullinPRO_0000000963Add
BLAST
Propeptidei148 – 18538PreproAM C-terminal fragmentPRO_0000000964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Arginine amide1 Publication
Disulfide bondi110 ↔ 1151 Publication
Modified residuei146 – 1461Tyrosine amide1 Publication

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiP35318.
PeptideAtlasiP35318.
PRIDEiP35318.

PTM databases

PhosphoSiteiP35318.

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

BgeeiP35318.
CleanExiHS_ADM.
ExpressionAtlasiP35318. baseline and differential.
GenevestigatoriP35318.

Organism-specific databases

HPAiCAB016075.
HPA031806.

Interactioni

Protein-protein interaction databases

BioGridi106645. 1 interaction.
STRINGi9606.ENSP00000278175.

Structurei

Secondary structure

1
185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 4017Combined sources
Beta strandi102 – 1076Combined sources
Beta strandi111 – 1166Combined sources
Helixi117 – 1248Combined sources
Helixi137 – 1404Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FLYNMR-A22-41[»]
2L7SNMR-A95-146[»]
ProteinModelPortaliP35318.
SMRiP35318. Positions 95-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35318.

Family & Domainsi

Sequence similaritiesi

Belongs to the adrenomedullin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG46109.
GeneTreeiENSGT00390000000451.
HOGENOMiHOG000033821.
HOVERGENiHBG004181.
InParanoidiP35318.
KOiK12333.
OMAiVAPRNKI.
OrthoDBiEOG7DC266.
PhylomeDBiP35318.
TreeFamiTF333447.

Family and domain databases

InterProiIPR001710. Adrenomedullin.
IPR021116. Procalcitonin/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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501S → R.1 Publication
Corresponds to variant rs5005 [ dbSNP | Ensembl ].
VAR_014861
Natural varianti85 – 851P → R.
Corresponds to variant rs2228573 [ dbSNP | Ensembl ].
VAR_048205

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.1. human.

Polymorphism databases

DMDMi461474.

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 .
CCDSi CCDS7801.1.
PIRi JC2351. JN0684.
RefSeqi NP_001115.1. NM_001124.2.
UniGenei Hs.441047.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FLY NMR - A 22-41 [» ]
2L7S NMR - A 95-146 [» ]
ProteinModelPortali P35318.
SMRi P35318. Positions 95-146.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106645. 1 interaction.
STRINGi 9606.ENSP00000278175.

Chemistry

ChEMBLi CHEMBL2062356.

PTM databases

PhosphoSitei P35318.

Polymorphism databases

DMDMi 461474.

Proteomic databases

PaxDbi P35318.
PeptideAtlasi P35318.
PRIDEi P35318.

Protocols and materials databases

DNASUi 133.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000278175 ; ENSP00000278175 ; ENSG00000148926 .
ENST00000525063 ; ENSP00000435124 ; ENSG00000148926 .
ENST00000528655 ; ENSP00000436607 ; ENSG00000148926 .
GeneIDi 133.
KEGGi hsa:133.
UCSCi uc001mil.1. human.

Organism-specific databases

CTDi 133.
GeneCardsi GC11P010326.
HGNCi HGNC:259. ADM.
HPAi CAB016075.
HPA031806.
MIMi 103275. gene.
neXtProti NX_P35318.
PharmGKBi PA24580.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46109.
GeneTreei ENSGT00390000000451.
HOGENOMi HOG000033821.
HOVERGENi HBG004181.
InParanoidi P35318.
KOi K12333.
OMAi VAPRNKI.
OrthoDBi EOG7DC266.
PhylomeDBi P35318.
TreeFami TF333447.

Enzyme and pathway databases

Reactomei REACT_18290. Calcitonin-like ligand receptors.
REACT_19327. G alpha (s) signalling events.

Miscellaneous databases

ChiTaRSi ADM. human.
EvolutionaryTracei P35318.
GeneWikii Adrenomedullin.
GenomeRNAii 133.
NextBioi 533.
PMAP-CutDB P35318.
PROi P35318.
SOURCEi Search...

Gene expression databases

Bgeei P35318.
CleanExi HS_ADM.
ExpressionAtlasi P35318. baseline and differential.
Genevestigatori P35318.

Family and domain databases

InterProi IPR001710. Adrenomedullin.
IPR021116. Procalcitonin/adrenomedullin.
[Graphical view ]
Pfami PF00214. Calc_CGRP_IAPP. 1 hit.
[Graphical view ]
PRINTSi PR00801. ADRENOMEDULN.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of cDNA encoding a precursor for human adrenomedullin."
    Kitamura K., Sakata J., Kangawa K., Kojima M., Matsuo H., Eto T.
    Biochem. Biophys. Res. Commun. 194:720-725(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pheochromocytoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.
  6. NIEHS SNPs program
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-50.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Kidney.
  9. "Adrenomedullin: a novel hypotensive peptide isolated from human pheochromocytoma."
    Kitamura K., Kangawa K., Kawamoto M., Ichiki Y., Nakamura S., Matsuo H., Eto T.
    Biochem. Biophys. Res. Commun. 192:553-560(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 95-146, AMIDATION AT TYR-146, DISULFIDE BOND.
    Tissue: Pheochromocytoma.
  10. Cited for: REVIEW.
  11. "Structure-activity relationships of adrenomedullin in the circulation and adrenal gland."
    Champion H.C., Nussdorfer G.G., Kadowitz P.J.
    Regul. Pept. 85:1-8(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  12. "NMR conformational analysis of proadrenomedullin N-terminal 20 peptide, a proangiogenic factor involved in tumor growth."
    Lucyk S., Taha H., Yamamoto H., Miskolzie M., Kotovych G.
    Biopolymers 81:295-308(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 22-41, AMIDATION AT ARG-41.

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 26, 2014
This is version 138 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

External Data

Dasty 3