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Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (Multisynthase complex auxiliary component p43) [Cleaved into: Endothelial monocyte-activating polypeptide 2 (EMAP-2) (Endothelial monocyte-activating polypeptide II) (EMAP-II) (Small inducible cytokine subfamily E member 1)]

 AIMP1_MOUSE             Reviewed;         310 AA.
P31230; Q60659;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
28-MAR-2018, entry version 133.
RecName: Full=Aminoacyl tRNA synthase complex-interacting multifunctional protein 1;
AltName: Full=Multisynthase complex auxiliary component p43;
Contains:
RecName: Full=Endothelial monocyte-activating polypeptide 2;
Short=EMAP-2;
AltName: Full=Endothelial monocyte-activating polypeptide II {ECO:0000303|PubMed:7929199};
Short=EMAP-II;
AltName: Full=Small inducible cytokine subfamily E member 1;
Name=Aimp1; Synonyms=Emap2, Scye1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7929199;
Kao J., Houck K., Fan Y., Haehnel I., Libutti S.K., Kayton M.L.,
Grikscheit T., Chabot J., Nowygrod R., Greenberg S., Kuang W.J.,
Leung D.W., Hayward J.R., Kisiel W., Heath M., Brett J., Stern D.M.;
"Characterization of a novel tumor-derived cytokine. Endothelial-
monocyte activating polypeptide II.";
J. Biol. Chem. 269:25106-25119(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 145-164, AND FUNCTION.
PubMed=1400342;
Kao J., Ryan J., Brett G., Chen J., Shen H., Fan Y.-G., Godman G.,
Familletti P.C., Wang F., Pan Y.-C.E., Stern D., Clauss M.;
"Endothelial monocyte-activating polypeptide II. A novel tumor-derived
polypeptide that activates host-response mechanisms.";
J. Biol. Chem. 267:20239-20247(1992).
[4]
FUNCTION.
PubMed=7545917;
Kao J., Fan Y., Haehnel I., Brett J., Greenberg S., Clauss M.,
Kayton M., Houck K., Kisiel W., Seljelid R., Burnier J., Stern D.;
"A peptide derived from the amino terminus of endothelial-monocyte-
activating polypeptide II modulates mononuclear and polymorphonuclear
leukocyte functions, defines an apparently novel cellular interaction
site, and induces an acute inflammatory response.";
J. Biol. Chem. 269:9774-9782(1994).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9770485; DOI=10.1073/pnas.95.21.12322;
Knies U.E., Behrensdorf H.A., Mitchell C.A., Deutsch U., Risau W.,
Drexler H.C.A., Clauss M.;
"Regulation of endothelial monocyte-activating polypeptide II release
by apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 95:12322-12327(1998).
[6]
CLEAVAGE.
PubMed=11306575; DOI=10.1074/jbc.M100489200;
Shalak V., Kaminska M., Mitnacht-Kraus R., Vandenabeele P., Clauss M.,
Mirande M.;
"The EMAPII cytokine is released from the mammalian multisynthetase
complex after cleavage of its p43/proEMAPII component.";
J. Biol. Chem. 276:23769-23776(2001).
[7]
SUBUNIT, AND FUNCTION.
PubMed=12060739; DOI=10.1073/pnas.122110199;
Kim J.Y., Kang Y.-S., Lee J.-W., Kim H.J., Ahn Y.H., Park H.,
Ko Y.-G., Kim S.;
"p38 is essential for the assembly and stability of macromolecular
tRNA synthetase complex: implications for its physiological
significance.";
Proc. Natl. Acad. Sci. U.S.A. 99:7912-7916(2002).
[8]
FUNCTION.
PubMed=15681823; DOI=10.1016/S0002-9440(10)62262-6;
Park S.G., Shin H., Shin Y.K., Lee Y., Choi E.-C., Park B.-J., Kim S.;
"The novel cytokine p43 stimulates dermal fibroblast proliferation and
wound repair.";
Am. J. Pathol. 166:387-398(2005).
[9]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=17001013; DOI=10.1073/pnas.0602045103;
Park S.G., Kang Y.S., Kim J.Y., Lee C.S., Ko Y.G., Lee W.J.,
Lee K.-U., Yeom Y.I., Kim S.;
"Hormonal activity of AIMP1/p43 for glucose homeostasis.";
Proc. Natl. Acad. Sci. U.S.A. 103:14913-14918(2006).
[10]
FUNCTION, INTERACTION WITH HSP90B1, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
PubMed=17525271; DOI=10.2353/ajpath.2007.061266;
Han J.M., Park S.G., Liu B., Park B.-J., Kim J.Y., Jin C.H.,
Song Y.W., Li Z., Kim S.;
"Aminoacyl-tRNA synthetase-interacting multifunctional protein 1/p43
controls endoplasmic reticulum retention of heat shock protein gp96:
its pathological implications in lupus-like autoimmune diseases.";
Am. J. Pathol. 170:2042-2054(2007).
[11]
FUNCTION, INTERACTION WITH SMURF2, AND INDUCTION.
PubMed=18448069; DOI=10.1016/j.bbrc.2008.04.099;
Lee Y.S., Han J.M., Son S.H., Choi J.W., Jeon E.J., Bae S.-C.,
Park Y.I., Kim S.;
"AIMP1/p43 downregulates TGF-beta signaling via stabilization of
smurf2.";
Biochem. Biophys. Res. Commun. 371:395-400(2008).
[12]
FUNCTION.
PubMed=18292511; DOI=10.4049/jimmunol.180.5.2894;
Kim E., Kim S.H., Kim S., Cho D., Kim T.S.;
"AIMP1/p43 protein induces the maturation of bone marrow-derived
dendritic cells with T helper type 1-polarizing ability.";
J. Immunol. 180:2894-2902(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Non-catalytic component of the multisynthase complex
(PubMed:12060739). Stimulates the catalytic activity of
cytoplasmic arginyl-tRNA synthase (By similarity). Binds tRNA.
Possesses inflammatory cytokine activity (PubMed:1400342,
PubMed:7545917). Negatively regulates TGF-beta signaling through
stabilization of SMURF2 by binding to SMURF2 and inhibiting its
SMAD7-mediated degradation (PubMed:18448069). Involved in glucose
homeostasis through induction of glucagon secretion at low glucose
levels (PubMed:17001013). Promotes dermal fibroblast proliferation
and wound repair (PubMed:15681823). Regulates KDELR1-mediated
retention of HSP90B1/gp96 in the endoplasmic reticulum
(PubMed:17525271). Plays a role in angiogenesis by inducing
endothelial cell migration at low concentrations and endothelian
cell apoptosis at high concentrations (By similarity). Induces
maturation of dendritic cells and monocyte cell adhesion
(PubMed:18292511). Modulates endothelial cell responses by
degrading HIF-1A through interaction with PSMA7 (By similarity).
{ECO:0000250|UniProtKB:Q12904, ECO:0000269|PubMed:12060739,
ECO:0000269|PubMed:1400342, ECO:0000269|PubMed:15681823,
ECO:0000269|PubMed:17001013, ECO:0000269|PubMed:17525271,
ECO:0000269|PubMed:18292511, ECO:0000269|PubMed:18448069,
ECO:0000269|PubMed:7545917}.
-!- SUBUNIT: Homodimer. Part of a multisubunit complex that groups
tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS),
Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu
and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and
EEF1E1/p18 (PubMed:12060739). Interacts (via N-terminus) with RARS
(via N-terminus). Part of a complex composed of RARS, QARS and
AIMP1. Interacts (via C-terminus) with SMURF2 (PubMed:18448069).
Interacts (via N-terminus) with HSP90B1/gp96 (via C-terminus)
(PubMed:17525271). Interacts with PSMA7 (By similarity).
{ECO:0000250|UniProtKB:Q12904, ECO:0000269|PubMed:12060739,
ECO:0000269|PubMed:17525271, ECO:0000269|PubMed:18448069}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12904}.
Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q12904}. Secreted
{ECO:0000269|PubMed:17001013, ECO:0000269|PubMed:9770485}.
Endoplasmic reticulum {ECO:0000269|PubMed:17525271}. Golgi
apparatus {ECO:0000269|PubMed:17525271}. Note=Enriched in
secretory vesicles of pancreatic alpha cells and secreted from the
pancreas in response to low glucose levels (PubMed:17001013).
Secreted in response to hypoxia (By similarity). Also secreted in
response to both apoptotic and necrotic cell death.
{ECO:0000250|UniProtKB:Q12904, ECO:0000269|PubMed:17001013}.
-!- TISSUE SPECIFICITY: Highly expressed in salivary glands and
pancreatic alpha cells in the adult (at protein level)
(PubMed:17001013). In the embryo, expressed primarily at sites of
tissue remodeling such as ganglia, developing bones and teeth
(PubMed:9770485). {ECO:0000269|PubMed:17001013,
ECO:0000269|PubMed:9770485}.
-!- INDUCTION: By wounding. {ECO:0000269|PubMed:18448069}.
-!- PTM: Cleaved by caspase-7 in response to apoptosis to produce
EMAP-II. {ECO:0000269|PubMed:11306575}.
-!- DISRUPTION PHENOTYPE: Increased Hsp90b1 surface expression,
dendritic cell hyperactivation and development of lupus-like
autoimmune phenotypes (PubMed:17525271). Retarded growth after
birth, reduced food intake, reduced plasma levels of glucose, free
fatty acid, glucagon and insulin, increased glycogen content in
the liver, and rapid decrease in blood glucose concentration upon
fasting (PubMed:17001013). {ECO:0000269|PubMed:17001013,
ECO:0000269|PubMed:17525271}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U10118; AAA62203.1; -; mRNA.
EMBL; BC002054; AAH02054.1; -; mRNA.
PIR; A55053; A55053.
UniGene; Mm.235137; -.
ProteinModelPortal; P31230; -.
SMR; P31230; -.
IntAct; P31230; 3.
MINT; P31230; -.
STRING; 10090.ENSMUSP00000029663; -.
MoonProt; P31230; -.
iPTMnet; P31230; -.
PhosphoSitePlus; P31230; -.
SwissPalm; P31230; -.
EPD; P31230; -.
MaxQB; P31230; -.
PaxDb; P31230; -.
PeptideAtlas; P31230; -.
PRIDE; P31230; -.
MGI; MGI:102774; Aimp1.
eggNOG; KOG2241; Eukaryota.
eggNOG; COG0073; LUCA.
InParanoid; P31230; -.
PhylomeDB; P31230; -.
ChiTaRS; Aimp1; mouse.
PRO; PR:P31230; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_SCYE1; -.
GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:CAFA.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005125; F:cytokine activity; IDA:HGNC.
GO; GO:0051020; F:GTPase binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC.
GO; GO:0000049; F:tRNA binding; ISS:HGNC.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0050900; P:leukocyte migration; IDA:HGNC.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:HGNC.
GO; GO:0070094; P:positive regulation of glucagon secretion; IDA:UniProtKB.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; IBA:GO_Central.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR002547; tRNA-bd_dom.
Pfam; PF01588; tRNA_bind; 1.
SUPFAM; SSF50249; SSF50249; 1.
PROSITE; PS50886; TRBD; 1.
1: Evidence at protein level;
Acetylation; Angiogenesis; Apoptosis; Cell adhesion;
Complete proteome; Cytokine; Cytoplasm; Direct protein sequencing;
Endoplasmic reticulum; Golgi apparatus; Inflammatory response;
Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome;
RNA-binding; Secreted; tRNA-binding.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q12904}.
CHAIN 2 310 Aminoacyl tRNA synthase complex-
interacting multifunctional protein 1.
/FTId=PRO_0000223395.
CHAIN 145 310 Endothelial monocyte-activating
polypeptide 2.
/FTId=PRO_0000019244.
DOMAIN 149 250 tRNA-binding. {ECO:0000255|PROSITE-
ProRule:PRU00209}.
REGION 6 46 Required for fibroblast proliferation.
{ECO:0000250}.
REGION 54 192 Interaction with HSP90B1.
{ECO:0000269|PubMed:17525271}.
REGION 101 115 Required for endothelial cell death.
{ECO:0000250}.
REGION 115 190 Required for endothelial cell migration.
{ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q12904}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000250|UniProtKB:Q12904}.
MOD_RES 267 267 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
SEQUENCE 310 AA; 33997 MW; A2F8FF52A33D03A0 CRC64;
MATNDAVLKR LEQKGAEADQ IIEYLKQQVA LLKEKAILQA TMREEKKLRV ENAKLKKEIE
ELKQELILAE IHNGVEQVRV RLSTPLQTNC TASESVVQSP SVATTASPAT KEQIKAGEEK
KVKEKTEKKG EKKEKQQSAA ASTDSKPIDA SRLDLRIGCI VTAKKHPDAD SLYVEEVDVG
EAAPRTVVSG LVNHVPLEQM QNRMVVLLCN LKPAKMRGVL SQAMVMCASS PEKVEILAPP
NGSVPGDRIT FDAFPGEPDK ELNPKKKIWE QIQPDLHTNA ECVATYKGAP FEVKGKGVCR
AQTMANSGIK


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