ID   UFM1_BOVIN              Reviewed;          85 AA.
AC   Q2KJG2;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000250|UniProtKB:P61960};
DE   Flags: Precursor;
GN   Name=UFM1 {ECO:0000250|UniProtKB:P61960};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) 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. 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; BC105359; AAI05360.1; -; mRNA.
DR   RefSeq; NP_001039779.1; NM_001046314.1.
DR   AlphaFoldDB; Q2KJG2; -.
DR   SMR; Q2KJG2; -.
DR   PeptideAtlas; Q2KJG2; -.
DR   PRIDE; Q2KJG2; -.
DR   Ensembl; ENSBTAT00000077211; ENSBTAP00000058608; ENSBTAG00000051486.
DR   GeneID; 530547; -.
DR   KEGG; bta:530547; -.
DR   CTD; 51569; -.
DR   VEuPathDB; HostDB:ENSBTAG00000051486; -.
DR   VGNC; VGNC:107013; UFM1.
DR   GeneTree; ENSGT00390000010391; -.
DR   InParanoid; Q2KJG2; -.
DR   OMA; INPAQNA; -.
DR   OrthoDB; 1575050at2759; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000051486; Expressed in caput epididymis and 107 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0042308; P:negative regulation of protein import into nucleus; IEA:Ensembl.
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_0000244597"
FT   PROPEP          84..85
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
FT                   /id="PRO_0000244598"
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;  9168 MW;  EDA6112E5E5836D8 CRC64;
     MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA
     QTAGNVFLKH GSELRIIPRD RVGHC