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Q7Z4H4 (ADM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ADM2
Alternative name(s):
Intermedin

Cleaved into the following 2 chains:

  1. Adrenomedullin-2
    Short name=AM2
    Alternative name(s):
    Intermedin-long
    Short name=IMDL
  2. Intermedin-short
    Short name=IMDS
Gene names
Name:ADM2
Synonyms:AM2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.1

Subcellular location

Secreted.

Tissue specificity

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. Ref.1 Ref.3

Sequence similarities

Belongs to the adrenomedullin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 9874 By similarity
PRO_0000000977
Peptide101 – 14747Adrenomedullin-2 By similarity
PRO_0000000978
Peptide108 – 14740Intermedin-short Potential
PRO_0000000979

Amino acid modifications

Modified residue1471Tyrosine amide Probable
Disulfide bond110 ↔ 115 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7Z4H4 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 6E0E3098CFCE5BF2

FASTA14815,865
        10         20         30         40         50         60 
MARIPTAALG CISLLCLQLP GSLSRSLGGD PRPVKPREPP ARSPSSSLQP RHPAPRPVVW 

        70         80         90        100        110        120 
KLHRALQAQR GAGLAPVMGQ PLRDGGRQHS GPRRHSGPRR TQAQLLRVGC VLGTCQVQNL 

       130        140 
SHRLWQLMGP AGRQDSAPVD PSSPHSYG 

« Hide

References

« Hide 'large scale' references
[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: 14615490] [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: 14706825] [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: 16359754] [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. expand/collapse author list , 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: 10591208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF529213 mRNA. Translation: AAQ09100.1.
AB121034 mRNA. Translation: BAD07411.1.
AB236970 mRNA. Translation: BAE46395.1.
AL096767 Genomic DNA. Translation: CAO03464.1.
IPIIPI00385109.
RefSeqNP_079142.2. NM_024866.4.
UniGeneHs.449099.

3D structure databases

ProteinModelPortalQ7Z4H4.
SMRQ7Z4H4. Positions 95-147.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7Z4H4.

PTM databases

PhosphoSiteQ7Z4H4.

Polymorphism databases

DMDM47115749.

Proteomic databases

PRIDEQ7Z4H4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395737; ENSP00000379086; ENSG00000128165.
ENST00000395738; ENSP00000379087; ENSG00000128165.
GeneID79924.
KEGGhsa:79924.
UCSCuc003blj.1. human.

Organism-specific databases

CTD79924.
GeneCardsGC22P050920.
H-InvDBHIX0016613.
HGNCHGNC:28898. ADM2.
HPAHPA039691.
MIM608682. gene.
neXtProtNX_Q7Z4H4.
PharmGKBPA134898869.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG19492.
GeneTreeENSGT00500000045332.
HOVERGENHBG048691.
OMALLRVGCV.
OrthoDBEOG4QFWFT.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ7Z4H4.
BgeeQ7Z4H4.
CleanExHS_ADM2.
GenevestigatorQ7Z4H4.
GermOnlineENSG00000128165. Homo sapiens.

Family and domain databases

InterProIPR021116. Procalcitonin/adrenomedullin.
[Graphical view]
PfamPF00214. Calc_CGRP_IAPP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio69834.
SOURCESearch...

Entry information

Entry nameADM2_HUMAN
AccessionPrimary (citable) accession number: Q7Z4H4
Secondary accession number(s): Q3LFQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families