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Protein

ADM2

Gene

ADM2

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

Functioni

IMDL and IMDS may play a role as physiological regulators of gastrointestinal, cardiovascular bioactivities mediated by the CALCRL/RAMPs receptor complexes. Activates the cAMP-dependent pathway.1 Publication

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

GO - Biological processi

  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: Ensembl
  • angiogenesis Source: UniProtKB
  • digestion Source: Ensembl
  • feeding behavior Source: Ensembl
  • negative regulation of blood pressure Source: Ensembl
  • positive regulation of angiogenesis Source: MGI
  • positive regulation of gene expression Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
ADM2
Alternative name(s):
Intermedin
Cleaved into the following 2 chains:
Adrenomedullin-2
Short name:
AM2
Alternative name(s):
Intermedin-long
Short name:
IMDL
Intermedin-short
Short name:
IMDS
Gene namesi
Name:ADM2
Synonyms:AM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:28898. ADM2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134898869.

Chemistry

ChEMBLiCHEMBL5267.

Polymorphism and mutation databases

BioMutaiADM2.
DMDMi47115749.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424By similarityAdd
BLAST
Propeptidei25 – 9874By similarityPRO_0000000977Add
BLAST
Peptidei101 – 14747Adrenomedullin-2By similarityPRO_0000000978Add
BLAST
Peptidei108 – 14740Intermedin-shortSequence analysisPRO_0000000979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi110 ↔ 115By similarity
Modified residuei147 – 1471Tyrosine amideCurated

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiQ7Z4H4.
PRIDEiQ7Z4H4.

PTM databases

PhosphoSiteiQ7Z4H4.

Expressioni

Tissue specificityi

Expressed in the esophagus, stomach, jejunum, ileum, ileocecum, ascending colon, transverse colon, descending colon and rectum. Expressed in myocardial cells of the heart, renal tubular cells, hypothalamus, and pituitary.2 Publications

Gene expression databases

BgeeiQ7Z4H4.
CleanExiHS_ADM2.
GenevisibleiQ7Z4H4. HS.

Organism-specific databases

HPAiHPA039691.

Interactioni

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

STRINGi9606.ENSP00000379086.

Chemistry

BindingDBiQ7Z4H4.

Structurei

3D structure databases

ProteinModelPortaliQ7Z4H4.
SMRiQ7Z4H4. Positions 103-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the adrenomedullin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J3UK. Eukaryota.
ENOG410Z5UT. LUCA.
GeneTreeiENSGT00530000064523.
HOGENOMiHOG000033820.
HOVERGENiHBG048691.
InParanoidiQ7Z4H4.
OMAiPAMGHPL.
OrthoDBiEOG74N5JJ.
PhylomeDBiQ7Z4H4.
TreeFamiTF338591.

Family and domain databases

InterProiIPR021116. Calcitonin/adrenomedullin.
[Graphical view]
PfamiPF00214. Calc_CGRP_IAPP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q7Z4H4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARIPTAALG CISLLCLQLP GSLSRSLGGD PRPVKPREPP ARSPSSSLQP
60 70 80 90 100
RHPAPRPVVW KLHRALQAQR GAGLAPVMGQ PLRDGGRQHS GPRRHSGPRR
110 120 130 140
TQAQLLRVGC VLGTCQVQNL SHRLWQLMGP AGRQDSAPVD PSSPHSYG
Length:148
Mass (Da):15,865
Last modified:October 1, 2003 - v1
Checksum:i6E0E3098CFCE5BF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF529213 mRNA. Translation: AAQ09100.1.
AB121034 mRNA. Translation: BAD07411.1.
AB236970 mRNA. Translation: BAE46395.1.
AL096767 Genomic DNA. Translation: CAO03464.1.
CCDSiCCDS33682.1.
RefSeqiNP_001240774.1. NM_001253845.1.
UniGeneiHs.449099.
Hs.743540.

Genome annotation databases

EnsembliENST00000395737; ENSP00000379086; ENSG00000128165.
ENST00000395738; ENSP00000379087; ENSG00000128165.
GeneIDi79924.
KEGGihsa:79924.
UCSCiuc003blj.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF529213 mRNA. Translation: AAQ09100.1.
AB121034 mRNA. Translation: BAD07411.1.
AB236970 mRNA. Translation: BAE46395.1.
AL096767 Genomic DNA. Translation: CAO03464.1.
CCDSiCCDS33682.1.
RefSeqiNP_001240774.1. NM_001253845.1.
UniGeneiHs.449099.
Hs.743540.

3D structure databases

ProteinModelPortaliQ7Z4H4.
SMRiQ7Z4H4. Positions 103-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000379086.

Chemistry

BindingDBiQ7Z4H4.
ChEMBLiCHEMBL5267.

PTM databases

PhosphoSiteiQ7Z4H4.

Polymorphism and mutation databases

BioMutaiADM2.
DMDMi47115749.

Proteomic databases

PaxDbiQ7Z4H4.
PRIDEiQ7Z4H4.

Protocols and materials databases

DNASUi79924.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395737; ENSP00000379086; ENSG00000128165.
ENST00000395738; ENSP00000379087; ENSG00000128165.
GeneIDi79924.
KEGGihsa:79924.
UCSCiuc003blj.4. human.

Organism-specific databases

CTDi79924.
GeneCardsiADM2.
HGNCiHGNC:28898. ADM2.
HPAiHPA039691.
MIMi608682. gene.
neXtProtiNX_Q7Z4H4.
PharmGKBiPA134898869.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J3UK. Eukaryota.
ENOG410Z5UT. LUCA.
GeneTreeiENSGT00530000064523.
HOGENOMiHOG000033820.
HOVERGENiHBG048691.
InParanoidiQ7Z4H4.
OMAiPAMGHPL.
OrthoDBiEOG74N5JJ.
PhylomeDBiQ7Z4H4.
TreeFamiTF338591.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikiiADM2.
GenomeRNAii79924.
PROiQ7Z4H4.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z4H4.
CleanExiHS_ADM2.
GenevisibleiQ7Z4H4. HS.

Family and domain databases

InterProiIPR021116. Calcitonin/adrenomedullin.
[Graphical view]
PfamiPF00214. Calc_CGRP_IAPP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Intermedin is a calcitonin/calcitonin gene-related peptide family peptide acting through the calcitonin receptor-like receptor/receptor activity-modifying protein receptor complexes."
    Roh J., Chang C.L., Bhalla A., Klein C., Hsu S.Y.T.
    J. Biol. Chem. 279:7264-7274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  2. "Identification of novel adrenomedullin in mammals: a potent cardiovascular and renal regulator."
    Takei Y., Inoue K., Ogoshi M., Kawahara T., Bannai H., Miyano S.
    FEBS Lett. 556:53-58(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  3. "Immunocytochemical localization of adrenomedullin 2/intermedin-like immunoreactivity in human hypothalamus, heart and kidney."
    Takahashi K., Kikuchi K., Maruyama Y., Urabe T., Nakajima K., Sasano H., Imai Y., Murakami O., Totsune K.
    Peptides 27:1383-1389(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiADM2_HUMAN
AccessioniPrimary (citable) accession number: Q7Z4H4
Secondary accession number(s): Q3LFQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: June 8, 2016
This is version 97 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.