ID   UFM1_COLLI              Reviewed;          85 AA.
AC   B5LVL2;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000250|UniProtKB:P61960};
DE   Flags: Precursor;
GN   Name=UFM1 {ECO:0000250|UniProtKB:P61960};
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gao P., Zhao H., Wang Q.;
RT   "Construction of pituitary cDNA library and sequence analysis of ubiquitin-
RT   fold modifier 1 in laying and incubating pigeon.";
RL   Submitted (JUL-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; EU914822; ACH47031.1; -; mRNA.
DR   RefSeq; XP_005501921.1; XM_005501864.2.
DR   AlphaFoldDB; B5LVL2; -.
DR   SMR; B5LVL2; -.
DR   STRING; 8932.XP_005501921.1; -.
DR   GeneID; 102094349; -.
DR   KEGG; clv:102094349; -.
DR   CTD; 51569; -.
DR   eggNOG; KOG3483; Eukaryota.
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; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..83
FT                   /note="Ubiquitin-fold modifier 1"
FT                   /id="PRO_0000391983"
FT   PROPEP          84..85
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
FT                   /id="PRO_0000391984"
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;  9057 MW;  E5C9FCBF4E55C96F CRC64;
     MSKVTFKVTL TSDPRLPYKV LSVPEGTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA
     QTAGNVFLKH GSDLRLIPRD RVGSS