ADML_RAT
ID ADML_RAT Reviewed; 185 AA.
AC P43145;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Pro-adrenomedullin;
DE Contains:
DE RecName: Full=Adrenomedullin;
DE Short=AM;
DE Contains:
DE RecName: Full=Proadrenomedullin N-20 terminal peptide;
DE AltName: Full=ProAM N-terminal 20 peptide;
DE Short=PAMP;
DE Short=ProAM-N20;
DE Flags: Precursor;
GN Name=Adm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Adrenal gland;
RX PubMed=7690563; DOI=10.1006/bbrc.1993.2132;
RA Sakata J., Shimokuba T., Kitamura K., Nakamura S., Kangawa K., Matsuo H.,
RA Eto T.;
RT "Molecular cloning and biological activities of rat adrenomedullin, a
RT hypotensive peptide.";
RL Biochem. Biophys. Res. Commun. 195:921-927(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8524787; DOI=10.1073/pnas.92.25.11480;
RA Wang X., Yue T.L., Barone F.C., White R.F., Clark R.K., Willette R.N.,
RA Sulpizio A.C., Aiyar N.V., Ruffolo R.R. Jr., Feuerstein G.Z.;
RT "Discovery of adrenomedullin in rat ischemic cortex and evidence for its
RT role in exacerbating focal brain ischemic damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11480-11484(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [4]
RP PROTEOLYTIC PROCESSING, AMIDATION AT ARG-41 AND TYR-143, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
CC -!- FUNCTION: AM and PAMP are potent hypotensive and vasodilatator agents.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in adrenal glands, lung, kidney, heart,
CC spleen, duodenum and submandibular glands.
CC -!- SIMILARITY: Belongs to the adrenomedullin family. {ECO:0000305}.
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DR EMBL; D15069; BAA03665.1; -; mRNA.
DR EMBL; U15419; AAB60519.1; -; mRNA.
DR EMBL; BC061775; AAH61775.1; -; mRNA.
DR PIR; JN0766; JN0766.
DR RefSeq; NP_036847.1; NM_012715.1.
DR RefSeq; XP_008757909.1; XM_008759687.2.
DR AlphaFoldDB; P43145; -.
DR SMR; P43145; -.
DR BioGRID; 247106; 2.
DR STRING; 10116.ENSRNOP00000035811; -.
DR iPTMnet; P43145; -.
DR PhosphoSitePlus; P43145; -.
DR PaxDb; P43145; -.
DR PRIDE; P43145; -.
DR Ensembl; ENSRNOT00000036718; ENSRNOP00000035811; ENSRNOG00000027030.
DR GeneID; 25026; -.
DR KEGG; rno:25026; -.
DR UCSC; RGD:2047; rat.
DR CTD; 133; -.
DR RGD; 2047; Adm.
DR eggNOG; ENOG502S4SF; Eukaryota.
DR GeneTree; ENSGT00940000154380; -.
DR HOGENOM; CLU_099291_1_0_1; -.
DR InParanoid; P43145; -.
DR OMA; QSFLYCC; -.
DR OrthoDB; 1555764at2759; -.
DR PhylomeDB; P43145; -.
DR TreeFam; TF333447; -.
DR Reactome; R-RNO-419812; Calcitonin-like ligand receptors.
DR PRO; PR:P43145; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000027030; Expressed in heart and 19 other tissues.
DR Genevisible; P43145; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0031700; F:adrenomedullin receptor binding; IDA:RGD.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:1990410; P:adrenomedullin receptor signaling pathway; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0097647; P:amylin receptor signaling pathway; ISO:RGD.
DR GO; GO:0008209; P:androgen metabolic process; IDA:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; ISO:RGD.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:RGD.
DR GO; GO:0019933; P:cAMP-mediated signaling; IEP:RGD.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0046879; P:hormone secretion; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0043116; P:negative regulation of vascular permeability; ISO:RGD.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0031102; P:neuron projection regeneration; IMP:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0010460; P:positive regulation of heart rate; IDA:RGD.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; ISO:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IDA:RGD.
DR GO; GO:0035809; P:regulation of urine volume; ISO:RGD.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IDA:RGD.
DR GO; GO:0060712; P:spongiotrophoblast layer development; ISO:RGD.
DR GO; GO:0097084; P:vascular associated smooth muscle cell development; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR InterPro; IPR021116; Calcitonin/adrenomedullin.
DR InterPro; IPR001710; Pro-ADM.
DR Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR PRINTS; PR00801; ADRENOMEDULN.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW 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:0000269|PubMed:26479776"
FT /id="PRO_0000000973"
FT PROPEP 45..91
FT /evidence="ECO:0000269|PubMed:26479776"
FT /id="PRO_0000000974"
FT PEPTIDE 94..143
FT /note="Adrenomedullin"
FT /evidence="ECO:0000269|PubMed:26479776"
FT /id="PRO_0000000975"
FT PROPEP 150..185
FT /note="PreproAM C-terminal fragment"
FT /evidence="ECO:0000269|PubMed:26479776"
FT /id="PRO_0000000976"
FT REGION 68..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:26479776"
FT MOD_RES 143
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:26479776"
FT DISULFID 107..112
FT /evidence="ECO:0000250|UniProtKB:P35318"
SQ SEQUENCE 185 AA; 20636 MW; 35CAD9A9DD19AE35 CRC64;
MKLVSIALML LGSLAVLGAD TARLDTSSQF RKKWNKWALS RGKRELQASS SYPTGLVDEK
TVPTQTLGLQ DKQSTSSTPQ ASTQSTAHIR VKRYRQSMNQ GSRSTGCRFG TCTMQKLAHQ
IYQFTDKDKD GMAPRNKISP QGYGRRRRRS LPEVLRARTV ESSQEQTHSA PASPAHQDIS
RVSRL
