ID   ADM2_HUMAN              Reviewed;         148 AA.
AC   Q7Z4H4; Q3LFQ0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   05-OCT-2010, entry version 53.
DE   RecName: Full=ADM2;
DE   AltName: Full=Intermedin;
DE   Contains:
DE     RecName: Full=Adrenomedullin-2;
DE              Short=AM2;
DE     AltName: Full=Intermedin-long;
DE              Short=IMDL;
DE   Contains:
DE     RecName: Full=Intermedin-short;
DE              Short=IMDS;
DE   Flags: Precursor;
GN   Name=ADM2; Synonyms=AM2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=14615490; DOI=10.1074/jbc.M305332200;
RA   Roh J., Chang C.L., Bhalla A., Klein C., Hsu S.Y.T.;
RT   "Intermedin is a calcitonin/calcitonin gene-related peptide family
RT   peptide acting through the calcitonin receptor-like receptor/receptor
RT   activity-modifying protein receptor complexes.";
RL   J. Biol. Chem. 279:7264-7274(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=14706825; DOI=10.1016/S0014-5793(03)01368-1;
RA   Takei Y., Inoue K., Ogoshi M., Kawahara T., Bannai H., Miyano S.;
RT   "Identification of novel adrenomedullin in mammals: a potent
RT   cardiovascular and renal regulator.";
RL   FEBS Lett. 556:53-58(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=16359754; DOI=10.1016/j.peptides.2005.11.004;
RA   Takahashi K., Kikuchi K., Maruyama Y., Urabe T., Nakajima K.,
RA   Sasano H., Imai Y., Murakami O., Totsune K.;
RT   "Immunocytochemical localization of adrenomedullin 2/intermedin-like
RT   immunoreactivity in human hypothalamus, heart and kidney.";
RL   Peptides 27:1383-1389(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA   Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA   Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA   Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA   Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA   Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA   Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA   Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA   Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA   Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA   Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA   Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA   Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA   Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA   Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA   Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA   Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA   Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA   Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA   Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA   Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA   Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA   Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA   Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA   Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA   Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA   Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA   Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA   Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA   Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA   Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA   Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA   O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA   Khan A.S., Lane L., Tilahun Y., Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
CC   -!- FUNCTION: IMDL and IMDS may play a role as physiological
CC       regulators of gastrointestinal, cardiovascular bioactivities
CC       mediated by the CALCRL/RAMPs receptor complexes. Activates the
CC       cAMP-dependent pathway.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in the esophagus, stomach, jejunum,
CC       ileum, ileocecum, ascending colon, transverse colon, descending
CC       colon and rectum. Expressed in myocardial cells of the heart,
CC       renal tubular cells, hypothalamus, and pituitary.
CC   -!- SIMILARITY: Belongs to the adrenomedullin family.
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DR   EMBL; AF529213; AAQ09100.1; -; mRNA.
DR   EMBL; AB121034; BAD07411.1; -; mRNA.
DR   EMBL; AB236970; BAE46395.1; -; mRNA.
DR   EMBL; AL096767; CAO03464.1; -; Genomic_DNA.
DR   IPI; IPI00385109; -.
DR   RefSeq; NP_079142.2; -.
DR   UniGene; Hs.449099; -.
DR   STRING; Q7Z4H4; -.
DR   PRIDE; Q7Z4H4; -.
DR   Ensembl; ENST00000395737; ENSP00000379086; ENSG00000128165.
DR   Ensembl; ENST00000395738; ENSP00000379087; ENSG00000128165.
DR   GeneID; 79924; -.
DR   KEGG; hsa:79924; -.
DR   UCSC; uc003blj.1; human.
DR   CTD; 79924; -.
DR   GeneCards; GC22P050920; -.
DR   H-InvDB; HIX0016613; -.
DR   HGNC; HGNC:28898; ADM2.
DR   MIM; 608682; gene.
DR   PharmGKB; PA134898869; -.
DR   eggNOG; prNOG19492; -.
DR   HOVERGEN; HBG048691; -.
DR   OMA; QLLRVGC; -.
DR   OrthoDB; EOG9KM1NS; -.
DR   Reactome; REACT_14797; Signaling by GPCR.
DR   NextBio; 69834; -.
DR   ArrayExpress; Q7Z4H4; -.
DR   Bgee; Q7Z4H4; -.
DR   CleanEx; HS_ADM2; -.
DR   Genevestigator; Q7Z4H4; -.
DR   GermOnline; ENSG00000128165; Homo sapiens.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR021116; Procalcitonin/adrenomedullin.
DR   Pfam; PF00214; Calc_CGRP_IAPP; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Complete proteome;
KW   Disulfide bond; Hormone; Secreted; Signal.
FT   SIGNAL        1     24       Potential.
FT   PROPEP       25     98       By similarity.
FT                                /FTId=PRO_0000000977.
FT   PEPTIDE     101    147       Adrenomedullin-2 (By similarity).
FT                                /FTId=PRO_0000000978.
FT   PEPTIDE     108    147       Intermedin-short (Potential).
FT                                /FTId=PRO_0000000979.
FT   MOD_RES     147    147       Tyrosine amide (Probable).
FT   DISULFID    110    115       By similarity.
SQ   SEQUENCE   148 AA;  15865 MW;  6E0E3098CFCE5BF2 CRC64;
     MARIPTAALG CISLLCLQLP GSLSRSLGGD PRPVKPREPP ARSPSSSLQP RHPAPRPVVW
     KLHRALQAQR GAGLAPVMGQ PLRDGGRQHS GPRRHSGPRR TQAQLLRVGC VLGTCQVQNL
     SHRLWQLMGP AGRQDSAPVD PSSPHSYG
//