ADM5_PIG
ID ADM5_PIG Reviewed; 108 AA.
AC A5LHG2;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=ADM5;
DE Contains:
DE RecName: Full=Adrenomedullin-5;
DE Short=AM5;
DE Flags: Precursor;
GN Name=ADM5;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-57, AMIDATION AT TYR-77, DISULFIDE
RP BOND, SYNTHESIS OF 26-77, TISSUE SPECIFICITY, AND FUNCTION.
RC TISSUE=Spleen;
RX PubMed=18434369; DOI=10.1677/joe-07-0541;
RA Takei Y., Hashimoto H., Inoue K., Osaki T., Yoshizawa-Kumagaye K.,
RA Tsunemi M., Watanabe T.X., Ogoshi M., Minamino N., Ueta Y.;
RT "Central and peripheral cardiovascular actions of adrenomedullin 5, a novel
RT member of the calcitonin gene-related peptide family, in mammals.";
RL J. Endocrinol. 197:391-400(2008).
CC -!- FUNCTION: Seems to have a peripheral vasodepressor effect and a central
CC vasopressor effect. {ECO:0000269|PubMed:18434369}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the spleen and thymus. Also
CC expressed in adrenal and pituitary. Not expressed in brain, heart,
CC kidney, liver and stomach. {ECO:0000269|PubMed:18434369}.
CC -!- SIMILARITY: Belongs to the adrenomedullin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB287333; BAF64272.1; -; mRNA.
DR RefSeq; NP_001093409.1; NM_001099939.1.
DR AlphaFoldDB; A5LHG2; -.
DR STRING; 9823.ENSSSCP00000003462; -.
DR PaxDb; A5LHG2; -.
DR Ensembl; ENSSSCT00015098633; ENSSSCP00015040666; ENSSSCG00015073286.
DR Ensembl; ENSSSCT00025106980; ENSSSCP00025048146; ENSSSCG00025077072.
DR Ensembl; ENSSSCT00045028688; ENSSSCP00045019842; ENSSSCG00045016785.
DR Ensembl; ENSSSCT00050069970; ENSSSCP00050030086; ENSSSCG00050051378.
DR Ensembl; ENSSSCT00060108669; ENSSSCP00060048468; ENSSSCG00060078620.
DR GeneID; 100101476; -.
DR KEGG; ssc:100101476; -.
DR CTD; 199800; -.
DR eggNOG; ENOG502TD4C; Eukaryota.
DR HOGENOM; CLU_2209104_0_0_1; -.
DR InParanoid; A5LHG2; -.
DR OrthoDB; 1532005at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; A5LHG2; SS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0010460; P:positive regulation of heart rate; 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 InterPro; IPR021116; Calcitonin/adrenomedullin.
DR Pfam; PF00214; Calc_CGRP_IAPP; 1.
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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..25
FT /id="PRO_0000392552"
FT PEPTIDE 26..77
FT /note="Adrenomedullin-5"
FT /id="PRO_0000392553"
FT PROPEP 89..108
FT /evidence="ECO:0000250"
FT /id="PRO_0000392554"
FT REGION 61..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..91
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:18434369"
FT DISULFID 38..43
FT /evidence="ECO:0000269|PubMed:18434369"
FT VARIANT 57
FT /note="S -> F"
FT /evidence="ECO:0000269|PubMed:18434369"
SQ SEQUENCE 108 AA; 12507 MW; C8887F6FECF95D5F CRC64;
MTAHILLLWL FASSILGDPD SAGRLTRHQV SLKSGRLCSL GTCQTHRLPE IIYWLRSAST
KELSGKAGRK PQDPYSYGRR RRRRRRRREA RLLRRLQDPS LRRAQLAG