位置:首页 > 蛋白库 > ADM2_RAT
ADM2_RAT
ID   ADM2_RAT                Reviewed;         146 AA.
AC   P61312; Q6L5N4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein 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   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   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 cardiovascular
RT   and renal regulator.";
RL   FEBS Lett. 556:53-58(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Inoue K., Takei Y.;
RT   "cDNA for the precursor of rat adrenomedullin 2.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Chang C.L., Roh J., Hsu S.Y.;
RT   "Rat IMD sequence.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   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 peptide
RT   acting through the calcitonin receptor-like receptor/receptor activity-
RT   modifying protein receptor complexes.";
RL   J. Biol. Chem. 279:7264-7274(2004).
RN   [5]
RP   CLEAVAGE OF SIGNAL PEPTIDE AFTER SER-25, AND IDENTIFICATION BY MASS
RP   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: [Adrenomedullin-2]: May play a role as physiological
CC       regulators of gastrointestinal, cardiovascular bioactivities mediated
CC       by the CALCRL/RAMPs receptor complexes. Activates the cAMP-dependent
CC       pathway. {ECO:0000269|PubMed:14615490}.
CC   -!- FUNCTION: [Intermedin-short]: May play a role as physiological
CC       regulators of gastrointestinal, cardiovascular bioactivities mediated
CC       by the CALCRL/RAMPs receptor complexes. Activates the cAMP-dependent
CC       pathway. {ECO:0000269|PubMed:14615490}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expression was restricted to the intermediate and
CC       anterior lobes of the pituitary. {ECO:0000269|PubMed:14615490}.
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; AB121036; BAD07413.1; -; mRNA.
DR   EMBL; AB181297; BAD22678.1; -; mRNA.
DR   EMBL; AY590103; AAT01302.1; -; mRNA.
DR   RefSeq; NP_958829.1; NM_201426.1.
DR   AlphaFoldDB; P61312; -.
DR   SMR; P61312; -.
DR   STRING; 10116.ENSRNOP00000051266; -.
DR   PaxDb; P61312; -.
DR   Ensembl; ENSRNOT00000044854; ENSRNOP00000051266; ENSRNOG00000029830.
DR   GeneID; 399475; -.
DR   KEGG; rno:399475; -.
DR   CTD; 79924; -.
DR   RGD; 1302971; Adm2.
DR   eggNOG; ENOG502S7F2; Eukaryota.
DR   GeneTree; ENSGT00940000154380; -.
DR   HOGENOM; CLU_134508_0_0_1; -.
DR   InParanoid; P61312; -.
DR   OMA; RLWQLVR; -.
DR   OrthoDB; 1381783at2759; -.
DR   Reactome; R-RNO-419812; Calcitonin-like ligand receptors.
DR   PRO; PR:P61312; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000029830; Expressed in adult mammalian kidney and 12 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; TAS:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR   GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR   GO; GO:0007586; P:digestion; IMP:RGD.
DR   GO; GO:0007631; P:feeding behavior; IMP:RGD.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0010460; P:positive regulation of heart rate; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
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..25
FT                   /evidence="ECO:0000269|PubMed:26479776"
FT   PROPEP          26..96
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000983"
FT   PEPTIDE         99..145
FT                   /note="Adrenomedullin-2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000984"
FT   PEPTIDE         106..145
FT                   /note="Intermedin-short"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000000985"
FT   REGION          29..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..55
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         145
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P35318"
FT   DISULFID        108..113
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   146 AA;  15572 MW;  C87043237AD29DDC CRC64;
     MAQLLMVTVT FGCISLLYLL PGTLSGSLGK GLRPREPPAK IPSSGPQPGH PSLRPVVWKP
     PHALQPQGRG NPALATVHLP QGGGSRHPGP QRHVGSRRPH AQLLRVGCVL GTCQVQNLSH
     RLWQLVRPSG RRDSAPVDPS SPHSYG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024