ADML_CANLF
ID ADML_CANLF Reviewed; 188 AA.
AC O77559; Q9TVC9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 25-MAY-2022, entry version 93.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Imoto I., Jougasaki M.;
RT "Cloning of cDNA encoding canine adrenomedullin.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9788655; DOI=10.1097/00024382-199810000-00003;
RA Ono Y., Kojima M., Okada K., Kangawa K.;
RT "cDNA cloning of canine adrenomedullin and its gene expression in the heart
RT and blood vessels in endotoxin shock.";
RL Shock 10:243-247(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sasaki Y., Asano K.;
RT "Canis familiaris adrenomedullin mRNA, complete cds.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: AM and PAMP are potent hypotensive and vasodilatator agents.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the adrenomedullin family. {ECO:0000305}.
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DR EMBL; AF045773; AAD05423.1; -; mRNA.
DR EMBL; U96127; AAD09957.1; -; mRNA.
DR EMBL; AB191461; BAD52304.1; -; mRNA.
DR RefSeq; NP_001003183.1; NM_001003183.1.
DR AlphaFoldDB; O77559; -.
DR SMR; O77559; -.
DR STRING; 9615.ENSCAFP00000011183; -.
DR PaxDb; O77559; -.
DR GeneID; 403817; -.
DR KEGG; cfa:403817; -.
DR CTD; 133; -.
DR eggNOG; ENOG502S4SF; Eukaryota.
DR InParanoid; O77559; -.
DR OrthoDB; 1555764at2759; -.
DR TreeFam; TF333447; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR InterPro; IPR021116; Calcitonin/adrenomedullin.
DR InterPro; IPR001710; Pro-ADM.
DR Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR PRINTS; PR00801; ADRENOMEDULN.
PE 2: Evidence at transcript 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:0000250|UniProtKB:P43145"
FT /id="PRO_0000000957"
FT PROPEP 45..92
FT /evidence="ECO:0000250|UniProtKB:P43145"
FT /id="PRO_0000000958"
FT PEPTIDE 95..146
FT /note="Adrenomedullin"
FT /evidence="ECO:0000250|UniProtKB:P35318"
FT /id="PRO_0000000959"
FT PROPEP 153..188
FT /note="PreproAM C-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:P43145"
FT /id="PRO_0000000960"
FT REGION 131..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Arginine amide"
FT /evidence="ECO:0000250|UniProtKB:P35318"
FT MOD_RES 146
FT /note="Tyrosine amide"
FT /evidence="ECO:0000250|UniProtKB:P35318"
FT DISULFID 110..115
FT /evidence="ECO:0000250|UniProtKB:P35318"
FT CONFLICT 130
FT /note="N -> K (in Ref. 2; AAD09957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 20929 MW; 809D6A64F98F5578 CRC64;
MKLVPVALLY LGSLAFLGAD TARLDVASEF RKKWNKWAVS RGKRELRVSS SYPTGLAEVK
AGPAQTLIRT QDVKGASRNP QTSGPDAARI RVKRYRQSMN NFQGPRSFGC RFGTCTVQKL
AHQIYQFTDN DKDGVAPRSK ISPQGYGRRR RRSLPEPGLR RTLLFPEPRP GGAPAPRAHQ
VLANLLKM
