ID   UFL1_CHICK              Reviewed;         789 AA.
AC   Q5ZMG1;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=E3 UFM1-protein ligase 1;
DE            EC=2.3.2.- {ECO:0000250|UniProtKB:O94874};
DE   AltName: Full=E3 UFM1-protein transferase 1 {ECO:0000305};
GN   Name=UFL1 {ECO:0000250|UniProtKB:O94874};
GN   ORFNames=RCJMB04_2c12 {ECO:0000303|PubMed:15642098};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: E3 protein ligase that mediates ufmylation, the covalent
CC       attachment of the ubiquitin-like modifier UFM1 to lysine residues on
CC       target proteins, and which plays a key role in reticulophagy (also
CC       called ER-phagy) induced in response to endoplasmic reticulum stress.
CC       In response to endoplasmic reticulum stress, recruited to the
CC       endoplasmic reticulum membrane, and mediates ufmylation of proteins,
CC       thereby promoting reticulophagy of endoplasmic reticulum sheets.
CC       Ufmylation-dependent reticulophagy inhibits the unfolded protein
CC       response (UPR). Ufmylation in response to endoplasmic reticulum stress
CC       is essential for processes such as hematopoiesis, blood vessel
CC       morphogenesis or inflammatory response. Also involved in the response
CC       to DNA damage: recruited to double-strand break sites following DNA
CC       damage and mediates monoufmylation of histone H4 (By similarity).
CC       Required for hematopoietic stem cell function and hematopoiesis (By
CC       similarity). {ECO:0000250|UniProtKB:O94874,
CC       ECO:0000250|UniProtKB:Q8CCJ3}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:O94874}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:O94874}. Nucleus {ECO:0000250|UniProtKB:O94874}.
CC       Chromosome {ECO:0000250|UniProtKB:O94874}. Note=Recruited to double-
CC       strand breaks following DNA damage. {ECO:0000250|UniProtKB:O94874}.
CC   -!- SIMILARITY: Belongs to the UFL1 family. {ECO:0000305}.
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DR   EMBL; AJ719423; CAG31082.1; -; mRNA.
DR   AlphaFoldDB; Q5ZMG1; -.
DR   SMR; Q5ZMG1; -.
DR   STRING; 9031.ENSGALP00000025077; -.
DR   PaxDb; Q5ZMG1; -.
DR   VEuPathDB; HostDB:geneid_421804; -.
DR   eggNOG; KOG2235; Eukaryota.
DR   InParanoid; Q5ZMG1; -.
DR   PhylomeDB; Q5ZMG1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR   GO; GO:0061666; F:UFM1 ligase activity; ISS:UniProtKB.
DR   GO; GO:0071568; F:UFM1 transferase activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; ISS:UniProtKB.
DR   GO; GO:0016570; P:histone modification; ISS:UniProtKB.
DR   GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:1990592; P:protein K69-linked ufmylation; IBA:GO_Central.
DR   GO; GO:0071569; P:protein ufmylation; ISS:UniProtKB.
DR   GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR   GO; GO:0061709; P:reticulophagy; ISS:UniProtKB.
DR   InterPro; IPR018611; Ufl1.
DR   PANTHER; PTHR31057; PTHR31057; 1.
DR   Pfam; PF09743; E3_UFM1_ligase; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; Cytoplasm; DNA damage; DNA repair; Endoplasmic reticulum;
KW   Membrane; Nucleus; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..789
FT                   /note="E3 UFM1-protein ligase 1"
FT                   /id="PRO_0000050773"
FT   REGION          2..212
FT                   /note="Required for E3 UFM1-protein ligase activity"
FT                   /evidence="ECO:0000250|UniProtKB:O94874"
FT   REGION          407..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  89104 MW;  2D7FE3B11B670E2B CRC64;
     MAADWEEIRR LAADFQRAQF AEAAHRLSER NCIEIVTKLI AEKQLEVVHT LDGKEYVTPA
     QISKEIWDEL SVCGGRINIV DLQQIINVDL LHIENRANDI VKSDKAVQLV LGQLINESYL
     DQLAEEINDK LQETGQVTIS ELCKAYDLPG DFLTQALSKR LGRIIHGRLD QENRGVIFTE
     AFVSRHRARI RGLFSAITRP TPVSNLITRY GFQEHLLYSV LEELVNTSRL KGTVVGGKQD
     KAVFVPDIYA RTQSNWVDSF FKQNGYLEFD ALYRLGIPDP AGYIKKRYKS TKLLFLRAAC
     VGQEIVDRVE ASVDEVISSG SWIDVATLLP SSLSVEDIGI LLQQVMRSLN KNSSGLVFSD
     TIVVSEKFIS SCTDLFSDMM KQKAEKEMKN SPVHLITEED LKQSYVLENS YTNKKDKKDE
     RRKKATEGSG SVRGGGGGNA REIKIKKTKK KGRKDADSDE ESQATGTGRN KQLEFHFMSQ
     EEMQDVLKTH LQDCPEELIT ELAEHLMRPL TKSYQEVVRS VFTSSTSSSG ASGRQTMKDL
     QEEFSNLYNN IRLFEKGTKY FTDETQTNLA KHLLKTVCTD ITNLIFNFLA SDSMMTTENY
     STITSEVRTK ILGKLPEDTR GPLTKLHTSL NGKSLEDFLS YLDAAADICD IMVKKGDKKK
     ERQVLFQHRQ ALIEQLKVTE DPALVLHLTA VLLFQFSTHC MLHAPGRSVP QIINFLSGKI
     PEDQHSLLIK YQGLVVKQLI SQSKKAEQED DNKTEEEEGA DTIRKELQEI TTSVKDLVLR
     PRKSSVTEE