UFM1_XENTR
ID UFM1_XENTR Reviewed; 85 AA.
AC B3DL37;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000250|UniProtKB:P61960};
DE Flags: Precursor;
GN Name=ufm1 {ECO:0000250|UniProtKB:P61960};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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. {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; BC167299; AAI67299.1; -; mRNA.
DR RefSeq; NP_001016988.1; NM_001016988.2.
DR AlphaFoldDB; B3DL37; -.
DR SMR; B3DL37; -.
DR STRING; 8364.ENSXETP00000028621; -.
DR PaxDb; B3DL37; -.
DR GeneID; 549742; -.
DR KEGG; xtr:549742; -.
DR CTD; 51569; -.
DR Xenbase; XB-GENE-973175; ufm1.
DR eggNOG; KOG3483; Eukaryota.
DR HOGENOM; CLU_175114_0_0_1; -.
DR InParanoid; B3DL37; -.
DR OrthoDB; 1575050at2759; -.
DR PhylomeDB; B3DL37; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000027207; Expressed in egg cell and 13 other tissues.
DR ExpressionAtlas; B3DL37; differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR GO; GO:0071569; P:protein ufmylation; 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_0000391989"
FT PROPEP 84..85
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT /id="PRO_0000391990"
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; 9175 MW; F3B35B7D43582ED5 CRC64;
MSKVTFKITL TSDPRLPYKV LCVPENTPFT AVLKFAAEEF KVPAATSAII TNDGIGLNPA
QTAGNVFLKH GSELRLIPRD RVGSC