ID   UFM1_SALSA              Reviewed;         100 AA.
AC   B9ENM6;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000250|UniProtKB:P61960};
DE   Flags: Precursor;
GN   Name=ufm1 {ECO:0000250|UniProtKB:P61960};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT057251; ACM09123.1; -; mRNA.
DR   RefSeq; NP_001139996.1; NM_001146524.1.
DR   AlphaFoldDB; B9ENM6; -.
DR   SMR; B9ENM6; -.
DR   STRING; 8030.ENSSSAP00000016813; -.
DR   GeneID; 100286585; -.
DR   KEGG; sasa:100286585; -.
DR   CTD; 51569; -.
DR   OMA; INPAQNA; -.
DR   OrthoDB; 1575050at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa11.
DR   Bgee; ENSSSAG00000008037; Expressed in actinopterygian pyloric caecum and 15 other tissues.
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_0000391987"
FT   PROPEP          84..100
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
FT                   /id="PRO_0000391988"
FT   REGION          78..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   100 AA;  10630 MW;  DA82DC2A0B2AEF1C CRC64;
     MSKVTFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA
     QTAGNVFLKH GSELRIIPRD RVGGRGVGTD RPSSSSSKTQ