ID   ADML_HUMAN              Reviewed;         185 AA.
AC   P35318; B2R793; D3DQV3; Q6FGW2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 211.
DE   RecName: Full=Pro-adrenomedullin;
DE   Contains:
DE     RecName: Full=Adrenomedullin {ECO:0000303|PubMed:7688224};
DE              Short=AM;
DE   Contains:
DE     RecName: Full=Proadrenomedullin N-20 terminal peptide {ECO:0000250|UniProtKB:P53366};
DE     AltName: Full=ProAM N-terminal 20 peptide {ECO:0000303|PubMed:16315141};
DE              Short=PAMP {ECO:0000303|PubMed:16315141};
DE              Short=ProAM-N20;
DE   Contains:
DE     RecName: Full=Proadrenomedullin 9-20 terminal peptide {ECO:0000303|PubMed:15823563};
DE              Short=PAMP-12 {ECO:0000303|PubMed:15823563};
DE   Flags: Precursor;
GN   Name=ADM {ECO:0000312|HGNC:HGNC:259}; Synonyms=AM;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pheochromocytoma;
RX   PubMed=7688224; DOI=10.1006/bbrc.1993.1881;
RA   Kitamura K., Sakata J., Kangawa K., Kojima M., Matsuo H., Eto T.;
RT   "Cloning and characterization of cDNA encoding a precursor for human
RT   adrenomedullin.";
RL   Biochem. Biophys. Res. Commun. 194:720-725(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=8074714; DOI=10.1006/bbrc.1994.2229;
RA   Ishimitsu T., Kojima M., Kangawa K., Hino J., Matsuoka H., Kitamura K.,
RA   Eto T., Matsuo H.;
RT   "Genomic structure of human adrenomedullin gene.";
RL   Biochem. Biophys. Res. Commun. 203:631-639(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-50.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   PROTEIN SEQUENCE OF 95-146, AMIDATION AT TYR-146, DISULFIDE BOND, FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Pheochromocytoma;
RX   PubMed=8387282; DOI=10.1006/bbrc.1993.1451;
RA   Kitamura K., Kangawa K., Kawamoto M., Ichiki Y., Nakamura S., Matsuo H.,
RA   Eto T.;
RT   "Adrenomedullin: a novel hypotensive peptide isolated from human
RT   pheochromocytoma.";
RL   Biochem. Biophys. Res. Commun. 192:553-560(1993).
RN   [10]
RP   FUNCTION.
RC   TISSUE=Neuroblastoma;
RX   PubMed=9620797; DOI=10.1038/30666;
RA   McLatchie L.M., Fraser N.J., Main M.J., Wise A., Brown J., Thompson N.,
RA   Solari R., Lee M.G., Foord S.M.;
RT   "RAMPs regulate the transport and ligand specificity of the calcitonin-
RT   receptor-like receptor.";
RL   Nature 393:333-339(1998).
RN   [11]
RP   REVIEW.
RX   PubMed=9578982; DOI=10.1006/frne.1998.0164;
RA   Samson W.K.;
RT   "Proadrenomedullin-derived peptides.";
RL   Front. Neuroendocrinol. 19:100-127(1998).
RN   [12]
RP   REVIEW.
RX   PubMed=10588445; DOI=10.1016/s0167-0115(99)00025-7;
RA   Champion H.C., Nussdorfer G.G., Kadowitz P.J.;
RT   "Structure-activity relationships of adrenomedullin in the circulation and
RT   adrenal gland.";
RL   Regul. Pept. 85:1-8(1999).
RN   [13]
RP   FUNCTION (PROADRENOMEDULLIN 9-20 TERMINAL PEPTIDE).
RX   PubMed=15823563; DOI=10.1016/j.bbrc.2005.03.088;
RA   Kamohara M., Matsuo A., Takasaki J., Kohda M., Matsumoto M., Matsumoto S.,
RA   Soga T., Hiyama H., Kobori M., Katou M.;
RT   "Identification of MrgX2 as a human G-protein-coupled receptor for
RT   proadrenomedullin N-terminal peptides.";
RL   Biochem. Biophys. Res. Commun. 330:1146-1152(2005).
RN   [14]
RP   STRUCTURE BY NMR OF 22-41, AND AMIDATION AT ARG-41.
RX   PubMed=16315141; DOI=10.1002/bip.20418;
RA   Lucyk S., Taha H., Yamamoto H., Miskolzie M., Kotovych G.;
RT   "NMR conformational analysis of proadrenomedullin N-terminal 20 peptide, a
RT   proangiogenic factor involved in tumor growth.";
RL   Biopolymers 81:295-308(2006).
RN   [15] {ECO:0007744|PDB:6UUN, ECO:0007744|PDB:6UUS}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.40 ANGSTROMS) OF 95-146 IN COMPLEX WITH
RP   CALCRL; RAMP2; RAMP3 AND G PROTEINS.
RX   PubMed=32296767; DOI=10.1021/acsptsci.9b00080;
RA   Liang Y.L., Belousoff M.J., Fletcher M.M., Zhang X., Khoshouei M.,
RA   Deganutti G., Koole C., Furness S.G.B., Miller L.J., Hay D.L.,
RA   Christopoulos A., Reynolds C.A., Danev R., Wootten D., Sexton P.M.;
RT   "Structure and Dynamics of Adrenomedullin Receptors AM1 and AM2 Reveal Key
RT   Mechanisms in the Control of Receptor Phenotype by Receptor Activity-
RT   Modifying Proteins.";
RL   ACS Pharmacol. Transl. Sci. 3:263-284(2020).
RN   [16] {ECO:0007744|PDB:7VV0}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 30-41 IN COMPLEX WITH
RP   MRGPRX2, AND FUNCTION (PROADRENOMEDULLIN 9-20 TERMINAL PEPTIDE).
RX   PubMed=34789875; DOI=10.1038/s41586-021-04077-y;
RA   Yang F., Guo L., Li Y., Wang G., Wang J., Zhang C., Fang G.X., Chen X.,
RA   Liu L., Yan X., Liu Q., Qu C., Xu Y., Xiao P., Zhu Z., Li Z., Zhou J.,
RA   Yu X., Gao N., Sun J.P.;
RT   "Structure, function and pharmacology of human itch receptor complexes.";
RL   Nature 600:164-169(2021).
CC   -!- FUNCTION: Adrenomedullin/ADM and proadrenomedullin N-20 terminal
CC       peptide/PAMP are peptide hormones that act as potent hypotensive and
CC       vasodilatator agents (PubMed:8387282, PubMed:9620797). Numerous actions
CC       have been reported most related to the physiologic control of fluid and
CC       electrolyte homeostasis. In the kidney, ADM is diuretic and
CC       natriuretic, and both ADM and PAMP inhibit aldosterone secretion by
CC       direct adrenal actions. In pituitary gland, both peptides at
CC       physiologically relevant doses inhibit basal ACTH secretion. Both
CC       peptides appear to act in brain and pituitary gland to facilitate the
CC       loss of plasma volume, actions which complement their hypotensive
CC       effects in blood vessels. {ECO:0000269|PubMed:8387282,
CC       ECO:0000269|PubMed:9620797}.
CC   -!- FUNCTION: [Adrenomedullin]: Peptide hormone that act as potent
CC       hypotensive and vasodilatator agents (PubMed:8387282). ADM function is
CC       mediated by the CALCRL-RAMP2 and CALCRL-RAMP3 receptor complexes with
CC       ADM showing the highest potency for the CALCRL-RAMP2 complex
CC       (PubMed:32296767, PubMed:9620797). {ECO:0000269|PubMed:32296767,
CC       ECO:0000269|PubMed:8387282, ECO:0000269|PubMed:9620797}.
CC   -!- FUNCTION: [Proadrenomedullin N-20 terminal peptide]: Peptide hormone
CC       that act as potent hypotensive and vasodilatator agents by inhibiting
CC       catecholamine secretion from sympathetic nerve endings and adrenal
CC       chromaffin cells (PubMed:10588445, PubMed:9578982). Acts as a ligand
CC       for MRGPRX2 receptor in mast cells (PubMed:15823563).
CC       {ECO:0000269|PubMed:15823563, ECO:0000303|PubMed:10588445,
CC       ECO:0000303|PubMed:9578982}.
CC   -!- FUNCTION: [Proadrenomedullin 9-20 terminal peptide]: Peptide hormone
CC       that act as potent hypotensive and vasodilatator agents by inhibiting
CC       catecholamine secretion from sympathetic nerve endings and adrenal
CC       chromaffin cells (PubMed:10588445, PubMed:9578982). Acts as a ligand
CC       for MRGPRX2 receptor in mast cells (PubMed:15823563, PubMed:34789875).
CC       {ECO:0000269|PubMed:15823563, ECO:0000269|PubMed:34789875,
CC       ECO:0000303|PubMed:10588445, ECO:0000303|PubMed:9578982}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8387282}.
CC   -!- TISSUE SPECIFICITY: Highest levels found in pheochromocytoma and
CC       adrenal medulla. Also found in lung, ventricle and kidney tissues.
CC       {ECO:0000269|PubMed:8387282}.
CC   -!- SIMILARITY: Belongs to the adrenomedullin family. {ECO:0000305}.
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DR   EMBL; D14874; BAA03589.1; -; mRNA.
DR   EMBL; S73906; AAC60642.1; -; Genomic_DNA.
DR   EMBL; D43639; BAA07756.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CR541995; CAG46792.1; -; mRNA.
DR   EMBL; BT006902; AAP35548.1; -; mRNA.
DR   EMBL; AK312893; BAG35740.1; -; mRNA.
DR   EMBL; DQ143945; AAZ38717.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68571.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68572.1; -; Genomic_DNA.
DR   EMBL; BC015961; AAH15961.1; -; mRNA.
DR   CCDS; CCDS7801.1; -.
DR   PIR; JC2351; JN0684.
DR   RefSeq; NP_001115.1; NM_001124.3.
DR   PDB; 2FLY; NMR; -; A=22-41.
DR   PDB; 2L7S; NMR; -; A=95-146.
DR   PDB; 4RWF; X-ray; 1.76 A; B=119-146.
DR   PDB; 5V6Y; X-ray; 2.80 A; E/F/G/H=131-146.
DR   PDB; 6UUN; EM; 3.00 A; P=95-146.
DR   PDB; 6UUS; EM; 2.40 A; P=95-146.
DR   PDB; 6V2E; X-ray; 1.83 A; B=131-146.
DR   PDB; 7VV0; EM; 3.50 A; L=30-41.
DR   AlphaFoldDB; P35318; -.
DR   EMDB; EMD-20883; -.
DR   EMDB; EMD-20901; -.
DR   EMDB; EMD-32133; -.
DR   SMR; P35318; -.
DR   BioGRID; 106645; 10.
DR   FunCoup; P35318; 631.
DR   IntAct; P35318; 2.
DR   NDEx; IQUERY-CP-ADM; 4 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000436607; -.
DR   ChEMBL; CHEMBL2062356; -.
DR   GlyGen; P35318; 13 sites, 2 O-linked glycans (12 sites).
DR   iPTMnet; P35318; -.
DR   PhosphoSitePlus; P35318; -.
DR   BioMuta; ADM; -.
DR   DMDM; 461474; -.
DR   MassIVE; P35318; -.
DR   PaxDb; 9606-ENSP00000436607; -.
DR   PeptideAtlas; P35318; -.
DR   ProteomicsDB; 55021; -.
DR   Antibodypedia; 4233; 633 antibodies from 37 providers.
DR   DNASU; 133; -.
DR   Ensembl; ENST00000278175.10; ENSP00000278175.5; ENSG00000148926.11.
DR   Ensembl; ENST00000525063.2; ENSP00000435124.1; ENSG00000148926.11.
DR   Ensembl; ENST00000528655.5; ENSP00000436607.1; ENSG00000148926.11.
DR   Ensembl; ENST00000879128.1; ENSP00000549187.1; ENSG00000148926.11.
DR   Ensembl; ENST00000912087.1; ENSP00000582146.1; ENSG00000148926.11.
DR   Ensembl; ENST00000963835.1; ENSP00000633894.1; ENSG00000148926.11.
DR   GeneID; 133; -.
DR   KEGG; hsa:133; -.
DR   MANE-Select; ENST00000278175.10; ENSP00000278175.5; NM_001124.3; NP_001115.1.
DR   UCSC; uc001mil.2; human.
DR   AGR; HGNC:259; -.
DR   ClinPGx; PA24580; -.
DR   CTD; 133; -.
DR   DisGeNET; 133; -.
DR   GeneCards; ADM; -.
DR   HGNC; HGNC:259; ADM.
DR   HPA; ENSG00000148926; Tissue enhanced (adipose).
DR   MIM; 103275; gene.
DR   OpenTargets; ENSG00000148926; -.
DR   VEuPathDB; HostDB:ENSG00000148926; -.
DR   eggNOG; ENOG502S4SF; Eukaryota.
DR   GeneTree; ENSGT00940000154380; -.
DR   HOGENOM; CLU_099291_1_0_1; -.
DR   InParanoid; P35318; -.
DR   OMA; QSFLYCC; -.
DR   OrthoDB; 8771893at2759; -.
DR   PAN-GO; P35318; 8 GO annotations based on evolutionary models.
DR   PhylomeDB; P35318; -.
DR   PathwayCommons; P35318; -.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-419812; Calcitonin-like ligand receptors.
DR   Reactome; R-HSA-9856530; High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells.
DR   SignaLink; P35318; -.
DR   SIGNOR; P35318; -.
DR   Agora; ENSG00000148926; -.
DR   BioGRID-ORCS; 133; 16 hits in 1152 CRISPR screens.
DR   ChiTaRS; ADM; human.
DR   EvolutionaryTrace; P35318; -.
DR   GeneWiki; Adrenomedullin; -.
DR   GenomeRNAi; 133; -.
DR   Pharos; P35318; Tbio.
DR   PRO; PR:P35318; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P35318; protein.
DR   Bgee; ENSG00000148926; Expressed in vena cava and 195 other cell types or tissues.
DR   ExpressionAtlas; P35318; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0031700; F:adrenomedullin receptor binding; IDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IDA:UniProt.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:1990410; P:adrenomedullin receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0002031; P:G protein-coupled receptor internalization; IDA:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; TAS:GO_Central.
DR   GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
DR   GO; GO:0045906; P:negative regulation of vasoconstriction; IDA:BHF-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0010460; P:positive regulation of heart rate; IDA:UniProtKB.
DR   GO; GO:2000184; P:positive regulation of progesterone biosynthetic process; TAS:GO_Central.
DR   GO; GO:2001214; P:positive regulation of vasculogenesis; IEA:Ensembl.
DR   GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; IDA:UniProtKB.
DR   GO; GO:0035809; P:regulation of urine volume; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0097084; P:vascular associated smooth muscle cell development; IEA:Ensembl.
DR   GO; GO:0001570; P:vasculogenesis; IDA:UniProtKB.
DR   InterPro; IPR051665; Adrenomedullin-reg_peptide.
DR   InterPro; IPR021116; Calcitonin/adrenomedullin.
DR   InterPro; IPR001710; Pro-ADM.
DR   PANTHER; PTHR23414; ADRENOMEDULLIN, ADM; 1.
DR   PANTHER; PTHR23414:SF3; PRO-ADRENOMEDULLIN; 1.
DR   Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR   PRINTS; PR00801; ADRENOMEDULN.
DR   PDBsum; 2FLY; -.
DR   PDBsum; 2L7S; -.
DR   PDBsum; 4RWF; -.
DR   PDBsum; 5V6Y; -.
DR   PDBsum; 6UUN; -.
DR   PDBsum; 6UUS; -.
DR   PDBsum; 6V2E; -.
DR   PDBsum; 7VV0; -.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Hormone;
KW   Proteomics identification; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250|UniProtKB:P53366"
FT   PEPTIDE         22..41
FT                   /note="Proadrenomedullin N-20 terminal peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P43145"
FT                   /id="PRO_0000000961"
FT   PEPTIDE         30..41
FT                   /note="Proadrenomedullin 9-20 terminal peptide"
FT                   /evidence="ECO:0000269|PubMed:34789875"
FT                   /id="PRO_0000463039"
FT   PROPEP          45..92
FT                   /evidence="ECO:0000250|UniProtKB:P43145"
FT                   /id="PRO_0000000962"
FT   PEPTIDE         95..146
FT                   /note="Adrenomedullin"
FT                   /evidence="ECO:0000269|PubMed:8387282"
FT                   /id="PRO_0000000963"
FT   PROPEP          148..185
FT                   /note="PreproAM C-terminal fragment"
FT                   /id="PRO_0000000964"
FT   REGION          60..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            116
FT                   /note="Required for CALCRL receptor interaction"
FT                   /evidence="ECO:0000269|PubMed:32296767"
FT   SITE            125
FT                   /note="Required for CALCRL receptor interaction"
FT                   /evidence="ECO:0000269|PubMed:32296767"
FT   MOD_RES         41
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:16315141"
FT   MOD_RES         146
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000269|PubMed:8387282"
FT   DISULFID        110..115
FT                   /evidence="ECO:0000269|PubMed:32296767,
FT                   ECO:0000269|PubMed:8387282"
FT   VARIANT         50
FT                   /note="S -> R (in dbSNP:rs5005)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_014861"
FT   VARIANT         85
FT                   /note="P -> R (in dbSNP:rs2228573)"
FT                   /id="VAR_048205"
FT   HELIX           24..40
FT                   /evidence="ECO:0007829|PDB:2FLY"
FT   STRAND          102..107
FT                   /evidence="ECO:0007829|PDB:2L7S"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:6UUN"
FT   HELIX           116..126
FT                   /evidence="ECO:0007829|PDB:6UUS"
FT   STRAND          132..135
FT                   /evidence="ECO:0007829|PDB:4RWF"
FT   HELIX           138..141
FT                   /evidence="ECO:0007829|PDB:4RWF"
SQ   SEQUENCE   185 AA;  20420 MW;  64C7D2A0B4654DFE CRC64;
     MKLVSVALMY LGSLAFLGAD TARLDVASEF RKKWNKWALS RGKRELRMSS SYPTGLADVK
     AGPAQTLIRP QDMKGASRSP EDSSPDAARI RVKRYRQSMN NFQGLRSFGC RFGTCTVQKL
     AHQIYQFTDK DKDNVAPRSK ISPQGYGRRR RRSLPEAGPG RTLVSSKPQA HGAPAPPSGS
     APHFL
//