UFL1_DANRE
ID UFL1_DANRE Reviewed; 793 AA.
AC Q6PGY6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=E3 UFM1-protein ligase 1 {ECO:0000305};
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=zgc:63562 {ECO:0000303|Ref.1};
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 STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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; BC056784; AAH56784.1; -; mRNA.
DR RefSeq; NP_956900.1; NM_200606.1.
DR AlphaFoldDB; Q6PGY6; -.
DR STRING; 7955.ENSDARP00000021768; -.
DR PaxDb; Q6PGY6; -.
DR GeneID; 393578; -.
DR KEGG; dre:393578; -.
DR CTD; 23376; -.
DR ZFIN; ZDB-GENE-040426-1163; ufl1.
DR eggNOG; KOG2235; Eukaryota.
DR InParanoid; Q6PGY6; -.
DR OrthoDB; 289380at2759; -.
DR PhylomeDB; Q6PGY6; -.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q6PGY6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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..793
FT /note="E3 UFM1-protein ligase 1"
FT /id="PRO_0000328124"
FT REGION 2..212
FT /note="Required for E3 UFM1-protein ligase activity"
FT /evidence="ECO:0000250|UniProtKB:O94874"
FT REGION 405..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..793
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"
FT COMPBIAS 449..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 88679 MW; 9D9DB15C5B6FD2A2 CRC64;
MAADWEEIRR LAADFQRAQF AETVQRLSER NCIEIVSKLV EDKKLDVVHT LDGKEYVTPA
QISREIRDEL YMHRGRINVV DLQKIINVDL VHVEGRANEI AKSDRGTQLI LGQLIDEAYL
DRLAEEVNDK LQEAGQVNIA ELCKTYDLPG DFLTEALNAR LGRVIQGQLD QYNRGMIFTQ
AFLSRHKACI CGLFSGITRP TQINNLLNLY GFQENLVYSM LEELVNSARL KGSVVGGRQD
KAIYIPDIYS KAQSTWVESF LKQNGYLEFE SLTRLGIPDP INYIKKRFKS SRLLFLKTAC
VGRTIVDQLE ASVEEAINSA TWVDLQPMLP SILSEEDVGI LLNEVLRSMN VQSSARLLST
SVVSEKFIAG CIALFEDLMQ QKAQKEVKNN PVFLITEDDV KQSSALLETS ASSKKDKRDE
RRKKAAEGGG SVKSGGGGNA REIRIRKTKK KGRKEEDSDE ETTHSSQGRN KLGDVQFLSV
EEIVEVLEEK VCDSSEEMLQ ELAEQLQRPL SKMYQEVVTT AFLSTSSSGA GGSRKKNMKD
LQEEINNLYN NIRLFEKGTK LFSDETQATV AKHVLKTVCT DVTNVLLSFV AAEHMTSDSS
AAMTSEIRLK ILAKLSDEVR SPLMKLHNSL NGKAIEEFLS CLETSAEECG LFLKKGDKKR
ERQALSVHRQ ALCEQLRDAE DPALVLHLTS VLLFQNVTHC MLHAPGRCVP HIIGFLQSKI
PEDQHKLLSQ YQSLVVKQLV VQGHGAEKKT VPPEGAGGPA DSDDTESLQR ELHSLSRDIK
DTVLAQRKPS VTE
