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ADML_MOUSE
ID   ADML_MOUSE              Reviewed;         184 AA.
AC   P97297; P97453; Q6GTK2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   03-AUG-2022, entry version 150.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=8938454; DOI=10.1006/geno.1996.0576;
RA   Okazaki T., Ogawa Y., Tamura N., Mori Y., Isse N., Aoki T., Rochelle J.M.,
RA   Taketo M.M., Seldin M.F., Nakao K.;
RT   "Genomic organization, expression, and chromosomal mapping of the mouse
RT   adrenomedullin gene.";
RL   Genomics 37:395-399(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=9808778; DOI=10.1006/dbio.1998.9073;
RA   Yotsumoto S., Shimada T., Cui C.Y., Nakashima H., Fujiwara H., Ko M.S.H.;
RT   "Expression of adrenomedullin, a hypotensive peptide, in the trophoblast
RT   giant cells at the embryo implantation site in mouse.";
RL   Dev. Biol. 203:264-275(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Kidney, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg;
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).
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; D78349; BAA11367.1; -; Genomic_DNA.
DR   EMBL; U77630; AAB36535.1; -; mRNA.
DR   EMBL; AK144181; BAE25751.1; -; mRNA.
DR   EMBL; AK144600; BAE25959.1; -; mRNA.
DR   EMBL; AK144649; BAE25989.1; -; mRNA.
DR   EMBL; AK171066; BAE42225.1; -; mRNA.
DR   EMBL; CH466531; EDL16987.1; -; Genomic_DNA.
DR   EMBL; BC052665; AAH52665.1; -; mRNA.
DR   CCDS; CCDS21745.1; -.
DR   RefSeq; NP_033757.1; NM_009627.1.
DR   AlphaFoldDB; P97297; -.
DR   BioGRID; 197989; 1.
DR   STRING; 10090.ENSMUSP00000140890; -.
DR   iPTMnet; P97297; -.
DR   PhosphoSitePlus; P97297; -.
DR   MaxQB; P97297; -.
DR   PaxDb; P97297; -.
DR   PeptideAtlas; P97297; -.
DR   PRIDE; P97297; -.
DR   Antibodypedia; 4233; 630 antibodies from 34 providers.
DR   DNASU; 11535; -.
DR   Ensembl; ENSMUST00000033054; ENSMUSP00000033054; ENSMUSG00000030790.
DR   GeneID; 11535; -.
DR   KEGG; mmu:11535; -.
DR   UCSC; uc009jfj.1; mouse.
DR   CTD; 133; -.
DR   MGI; MGI:108058; Adm.
DR   VEuPathDB; HostDB:ENSMUSG00000030790; -.
DR   eggNOG; ENOG502S4SF; Eukaryota.
DR   GeneTree; ENSGT00940000154380; -.
DR   HOGENOM; CLU_099291_1_0_1; -.
DR   InParanoid; P97297; -.
DR   OMA; QSFLYCC; -.
DR   OrthoDB; 1555764at2759; -.
DR   TreeFam; TF333447; -.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-419812; Calcitonin-like ligand receptors.
DR   BioGRID-ORCS; 11535; 0 hits in 74 CRISPR screens.
DR   PRO; PR:P97297; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P97297; protein.
DR   Bgee; ENSMUSG00000030790; Expressed in ectoplacental cone and 184 other tissues.
DR   Genevisible; P97297; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0031700; F:adrenomedullin receptor binding; ISO:MGI.
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:MGI.
DR   GO; GO:1990410; P:adrenomedullin receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0097647; P:amylin receptor signaling pathway; ISO:MGI.
DR   GO; GO:0008209; P:androgen metabolic process; ISO:MGI.
DR   GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR   GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR   GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
DR   GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IEA:Ensembl.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0002031; P:G protein-coupled receptor internalization; ISO:MGI.
DR   GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR   GO; GO:0046879; P:hormone secretion; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0043116; P:negative regulation of vascular permeability; IMP:UniProtKB.
DR   GO; GO:0045906; P:negative regulation of vasoconstriction; ISO:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0031102; P:neuron projection regeneration; ISO:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:0010460; P:positive regulation of heart rate; ISO:MGI.
DR   GO; GO:2001214; P:positive regulation of vasculogenesis; IMP:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:MGI.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; ISO:MGI.
DR   GO; GO:0035809; P:regulation of urine volume; ISO:MGI.
DR   GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR   GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR   GO; GO:0009611; P:response to wounding; ISO:MGI.
DR   GO; GO:0060712; P:spongiotrophoblast layer development; IMP:MGI.
DR   GO; GO:0097084; P:vascular associated smooth muscle cell development; IMP:UniProtKB.
DR   GO; GO:0001570; P:vasculogenesis; ISO:MGI.
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_0000000965"
FT   PROPEP          45..92
FT                   /evidence="ECO:0000250|UniProtKB:P43145"
FT                   /id="PRO_0000000966"
FT   PEPTIDE         95..144
FT                   /note="Adrenomedullin"
FT                   /evidence="ECO:0000250|UniProtKB:P35318"
FT                   /id="PRO_0000000967"
FT   PROPEP          151..184
FT                   /note="PreproAM C-terminal fragment"
FT                   /evidence="ECO:0000250|UniProtKB:P43145"
FT                   /id="PRO_0000000968"
FT   REGION          130..149
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         144
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P35318"
FT   DISULFID        108..113
FT                   /evidence="ECO:0000250|UniProtKB:P35318"
FT   CONFLICT        173
FT                   /note="G -> A (in Ref. 1; BAA11367)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   184 AA;  20750 MW;  C88C9903C479C898 CRC64;
     MKLVSITLML LGSLAFLGAD TAGPDTPSQF RKKWNKWALS RGKRELQASS SYPTGLADET
     TVPTQTLDPF LDEQNTTGPL QASNQSEAHI RVKRYRQSMN QGSRSNGCRF GTCTFQKLAH
     QIYQLTDKDK DGMAPRNKIS PQGYGRRRRR SLLEVLRSRT VESSQEQTHT APGPWAHISR
     LFRI
 
 
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