ID   UFM1_DANRE              Reviewed;          90 AA.
AC   Q803Y4; Q6TLE9;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000250|UniProtKB:P61960};
DE   Flags: Precursor;
GN   Name=ufm1 {ECO:0000250|UniProtKB:P61960}; Synonyms=ubfm1;
GN   ORFNames=zgc:55335 {ECO:0000303|Ref.2};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney marrow;
RX   PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA   Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA   Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA   Look A.T., Chen Z.;
RT   "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) 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; AY394956; AAQ94583.1; -; mRNA.
DR   EMBL; BC044145; AAH44145.1; -; mRNA.
DR   RefSeq; NP_997792.1; NM_212627.1.
DR   AlphaFoldDB; Q803Y4; -.
DR   SMR; Q803Y4; -.
DR   STRING; 7955.ENSDARP00000064392; -.
DR   PaxDb; Q803Y4; -.
DR   GeneID; 322756; -.
DR   KEGG; dre:322756; -.
DR   CTD; 51569; -.
DR   ZFIN; ZDB-GENE-040426-2930; ufm1.
DR   eggNOG; KOG3483; Eukaryota.
DR   InParanoid; Q803Y4; -.
DR   OrthoDB; 1575050at2759; -.
DR   PhylomeDB; Q803Y4; -.
DR   TreeFam; TF312934; -.
DR   PRO; PR:Q803Y4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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_0000042134"
FT   PROPEP          84..90
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
FT                   /id="PRO_0000042135"
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"
FT   CONFLICT        47
FT                   /note="G -> S (in Ref. 1; AAQ94583)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   90 AA;  9675 MW;  28AC4AB982AB6ED1 CRC64;
     MSKVTFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATGAII TNDGIGINPA
     QTAGNVFLKH GSELRIIPRD RVGGGHQPRM