Reviewed, UniProtKB/Swiss-Prot Q7Z4H4 (ADM2_HUMAN)

Names and origin

Protein names

Recommended name:
    ADM2
Alternative name(s):
    Intermedin
Cleaved into the following 2 chains:
    1- Recommended name:
            Adrenomedullin-2
        Alternative name(s):
            Intermedin-long
              Short name=IMDL
    2- Recommended name:
            Intermedin-short
                Short name=IMDS

Gene names

Name:	ADM2
Synonyms:	AM2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hormone
PTM	Amidation Cleavage on pair of basic residues Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	G-protein coupled receptor protein signaling pathway Inferred from Experiment. Source: Reactome
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Propeptide	25 – 98	74	By similarity		PRO_0000000977
	Peptide	101 – 147	47	Adrenomedullin-2 By similarity		PRO_0000000978
	Peptide	108 – 147	40	Intermedin-short Potential		PRO_0000000979
Amino acid modifications
	Modified residue	147	1	Tyrosine amide Probable
	Disulfide bond	110 ↔ 115		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7Z4H4-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 6E0E3098CFCE5BF2	FASTA	148	15,865
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBLGenBankDDBJ	AF529213 mRNA. Translation: AAQ09100.1. AB121034 mRNA. Translation: BAD07411.1. AB236970 mRNA. Translation: BAE46395.1. AL096767 Genomic DNA. Translation: CAO03464.1.
IPI	IPI00385109.
RefSeq	NP_079142.2.
UniGene	Hs.449099
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q7Z4H4.
Proteomic databases
PRIDE	Q7Z4H4.
Genome annotation databases
Ensembl	ENST00000395737; ENSP00000379086; ENSG00000128165; Homo sapiens. [Genome view] ENST00000395738; ENSP00000379087; ENSG00000128165; Homo sapiens. [Genome view]
GeneID	79924.
KEGG	hsa:79924.
UCSC	uc003blj.1. human.
Organism-specific databases
CTD	79924.
GeneCards	GC22P049267.
H-InvDB	HIX0016613.
HGNC	HGNC:28898. ADM2.
MIM	608682. gene.
PharmGKB	PA134898869.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q7Z4H4.
HOVERGEN	Q7Z4H4.
OMA	QLLRVGC
OrthoDB	EOG9KM1NS
Enzyme and pathway databases
Reactome	REACT_14797. Signaling by GPCR.
Gene expression databases
ArrayExpress	Q7Z4H4.
Bgee	Q7Z4H4.
CleanEx	HS_ADM2.
Genevestigator	Q7Z4H4.
GermOnline	ENSG00000128165. Homo sapiens.
Family and domain databases
InterPro	IPR018014. Adrenomedullin/Adrenomedullin2. [Graphical view]
Pfam	PF02039. Adrenomedullin. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	69834.
SOURCE	Search...

Entry information

Entry name

ADM2_HUMAN

Accession

Primary (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:	November 24, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.