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P35318

- ADML_HUMAN

UniProt

P35318 - ADML_HUMAN

Protein

ADM

Gene

ADM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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. protein binding Source: UniProtKB
    2. 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

    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

    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

    ArrayExpressiP35318.
    BgeeiP35318.
    CleanExiHS_ADM.
    GenevestigatoriP35318.

    Organism-specific databases

    HPAiCAB016075.
    HPA031806.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000278175.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MKLVSVALMY LGSLAFLGAD TARLDVASEF RKKWNKWALS RGKRELRMSS    50
    SYPTGLADVK AGPAQTLIRP QDMKGASRSP EDSSPDAARI RVKRYRQSMN 100
    NFQGLRSFGC RFGTCTVQKL AHQIYQFTDK DKDNVAPRSK ISPQGYGRRR 150
    RRSLPEAGPG RTLVSSKPQA HGAPAPPSGS APHFL 185
    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:
    EMBL
    GenBank
    DDBJ
    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_001124.1.
    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:
    EMBL
    GenBank
    DDBJ
    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_001124.1.
    UniGenei Hs.441047.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    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.
    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

    ArrayExpressi P35318.
    Bgeei P35318.
    CleanExi HS_ADM.
    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

    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: October 1, 2014
    This is version 136 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