AIMP1_CRIGR
ID AIMP1_CRIGR Reviewed; 359 AA.
AC O54873;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Aminoacyl tRNA synthase complex-interacting multifunctional protein 1;
DE AltName: Full=Multisynthase complex auxiliary component p43;
DE Contains:
DE RecName: Full=Endothelial monocyte-activating polypeptide 2;
DE AltName: Full=EMAP-II;
DE AltName: Full=Small inducible cytokine subfamily E member 1;
GN Name=AIMP1; Synonyms=SCYE1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9405472; DOI=10.1074/jbc.272.51.32573;
RA Quevillon S., Agou F., Robinson J.-C., Mirande M.;
RT "The p43 component of the mammalian multi-synthetase complex is likely to
RT be the precursor of the endothelial monocyte-activating polypeptide II
RT cytokine.";
RL J. Biol. Chem. 272:32573-32579(1997).
CC -!- FUNCTION: Non-catalytic component of the multisynthase complex.
CC Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase.
CC Binds tRNA. Possesses inflammatory cytokine activity. Negatively
CC regulates TGF-beta signaling through stabilization of SMURF2 by binding
CC to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in
CC glucose homeostasis through induction of glucagon secretion at low
CC glucose levels. Promotes dermal fibroblast proliferation and wound
CC repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the
CC endoplasmic reticulum. Plays a role in angiogenesis by inducing
CC endothelial cell migration at low concentrations and endothelian cell
CC apoptosis at high concentrations. Induces maturation of dendritic cells
CC and monocyte cell adhesion. {ECO:0000250|UniProtKB:P31230,
CC ECO:0000250|UniProtKB:Q12904}.
CC -!- SUBUNIT: Homodimer. Part of the multisynthetase complex (MSC), a
CC multisubunit complex that groups tRNA ligases for Arg (RARS1), Asp
CC (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met
CC (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the
CC auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18. Interacts (via
CC N-terminus) with RARS1 (via N-terminus). Part of a complex composed of
CC RARS1, QARS1 and AIMP1. Interacts (via C-terminus) with SMURF2.
CC Interacts (via N-terminus) with HSP90B1/gp96 (via C-terminus).
CC Interacts with PSMA7. Interacts with TARS3.
CC {ECO:0000250|UniProtKB:P31230, ECO:0000250|UniProtKB:Q12904}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12904}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q12904}. Secreted
CC {ECO:0000250|UniProtKB:P31230}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P31230}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P31230}. Note=Enriched in secretory vesicles of
CC pancreatic alpha cells and secreted from the pancreas in response to
CC low glucose levels. Secreted in response to hypoxia. Also secreted in
CC response to both apoptotic and necrotic cell death.
CC {ECO:0000250|UniProtKB:P31230, ECO:0000250|UniProtKB:Q12904}.
CC -!- PTM: Cleaved by caspase-7 in response to apoptosis to produce EMAP-II.
CC {ECO:0000250|UniProtKB:P31230}.
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DR EMBL; AF021800; AAB95207.1; -; mRNA.
DR RefSeq; NP_001231196.1; NM_001244267.1.
DR AlphaFoldDB; O54873; -.
DR SMR; O54873; -.
DR STRING; 10029.NP_001231196.1; -.
DR GeneID; 100689238; -.
DR KEGG; cge:100689238; -.
DR CTD; 9255; -.
DR eggNOG; KOG2241; Eukaryota.
DR OrthoDB; 1434247at2759; -.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0070094; P:positive regulation of glucagon secretion; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR Pfam; PF01588; tRNA_bind; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Apoptosis; Cytokine; Cytoplasm; Endoplasmic reticulum;
KW Golgi apparatus; Inflammatory response; Isopeptide bond; Nucleus;
KW Phosphoprotein; Protein biosynthesis; RNA-binding; Secreted; tRNA-binding;
KW Ubl conjugation.
FT CHAIN 1..359
FT /note="Aminoacyl tRNA synthase complex-interacting
FT multifunctional protein 1"
FT /id="PRO_0000223393"
FT CHAIN 194..359
FT /note="Endothelial monocyte-activating polypeptide 2"
FT /id="PRO_0000019240"
FT DOMAIN 198..299
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT REGION 52..92
FT /note="Required for fibroblast proliferation"
FT /evidence="ECO:0000250"
FT REGION 100..241
FT /note="Interaction with HSP90B1"
FT /evidence="ECO:0000250"
FT REGION 149..163
FT /note="Required for endothelial cell death"
FT /evidence="ECO:0000250"
FT REGION 156..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..239
FT /note="Required for endothelial cell migration"
FT /evidence="ECO:0000250"
FT COMPBIAS 160..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12904"
FT MOD_RES 316
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31230"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q12904"
SQ SEQUENCE 359 AA; 39601 MW; 4D868D1B65D72C23 CRC64;
MCEVFRRLPG TAPGSSPPAP ATHRLRLLGR ELRVRRFMIF CRFWAKMATN DAVLKRLEQK
GAEADQIIEY LKQQVALLKE KAVLQATLRE EKKLRVENAK LKKEIEELKQ ELIQAEIQNG
VKQIPVPVQS DTPVQASSAV STSVIQSTSV STISCSIKEH SKGGGEEKKV KEKTDKKGEK
KEKKLQSAAP SADSKPVDVS RLDLRIGRIV TVKKHPDADS LYVEEVDVGE AAPRTVISGL
VNHVPLDQMQ NRMVVLLCNL KPAKMRGILS QAMVMCASSP EKVEILAPPN GSVPGDRITF
DAFPGEPDKE LNPKKKIWEQ IQPDLHTNAE CVATYKGSPF EVKGKGVCRA QTMANSGIK
