UFM1_RAT
ID UFM1_RAT Reviewed; 85 AA.
AC Q5BJP3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000250|UniProtKB:P61960};
DE Flags: Precursor;
GN Name=Ufm1 {ECO:0000312|RGD:1304890};
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 [LARGE SCALE MRNA].
RC TISSUE=Liver;
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: Ubiquitin-like modifier which can be covalently attached via
CC an isopeptide bond to lysine residues of substrate proteins as a
CC monomer or a lysine-linked polymer. The so-called ufmylation, requires
CC the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme
CC UFC1, and the UFM1-ligase E3 enzyme UFL1. Ufmylation is involved in
CC reticulophagy (also called ER-phagy) induced in response to endoplasmic
CC reticulum stress. Ufmylation of TRIP4 regulates nuclear receptors-
CC mediated transcription. {ECO:0000250|UniProtKB:P61960}.
CC -!- SUBUNIT: Interacts with UBA5. Interacts with UFC1.
CC {ECO:0000250|UniProtKB:P61960}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61960}. Cytoplasm
CC {ECO:0000250|UniProtKB:P61960}.
CC -!- SIMILARITY: Belongs to the UFM1 family. {ECO:0000305}.
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DR EMBL; BC091395; AAH91395.1; -; mRNA.
DR RefSeq; NP_001119552.1; NM_001126080.2.
DR AlphaFoldDB; Q5BJP3; -.
DR SMR; Q5BJP3; -.
DR STRING; 10116.ENSRNOP00000054923; -.
DR iPTMnet; Q5BJP3; -.
DR PhosphoSitePlus; Q5BJP3; -.
DR jPOST; Q5BJP3; -.
DR PaxDb; Q5BJP3; -.
DR PRIDE; Q5BJP3; -.
DR GeneID; 365797; -.
DR KEGG; rno:365797; -.
DR UCSC; RGD:1304890; rat.
DR CTD; 51569; -.
DR RGD; 1304890; Ufm1.
DR eggNOG; KOG3483; Eukaryota.
DR HOGENOM; CLU_175114_0_0_1; -.
DR InParanoid; Q5BJP3; -.
DR OMA; INPAQNA; -.
DR OrthoDB; 1575050at2759; -.
DR PhylomeDB; Q5BJP3; -.
DR TreeFam; TF312934; -.
DR PRO; PR:Q5BJP3; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000038176; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q5BJP3; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR GO; GO:0071569; P:protein ufmylation; ISS:UniProtKB.
DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; ISS:UniProtKB.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR005375; UFM1.
DR PANTHER; PTHR15825; PTHR15825; 1.
DR Pfam; PF03671; Ufm1; 1.
DR PIRSF; PIRSF038027; Ubiquitin-like_Ufm1; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..83
FT /note="Ubiquitin-fold modifier 1"
FT /id="PRO_0000042130"
FT PROPEP 84..85
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT /id="PRO_0000042131"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1)"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000250|UniProtKB:P61960"
SQ SEQUENCE 85 AA; 9118 MW; EDB6102E5E5836D8 CRC64;
MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA
QTAGNVFLKH GSELRLIPRD RVGSC