UFC1_OSMMO
ID UFC1_OSMMO Reviewed; 167 AA.
AC C1BKD1;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Ubiquitin-fold modifier-conjugating enzyme 1 {ECO:0000305};
DE AltName: Full=Ufm1-conjugating enzyme 1 {ECO:0000250|UniProtKB:Q9Y3C8};
GN Name=ufc1 {ECO:0000250|UniProtKB:Q9Y3C8};
OS Osmerus mordax (Rainbow smelt) (Atherina mordax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Stomiati; Osmeriformes; Osmeridae;
OC Osmerus.
OX NCBI_TaxID=8014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA von Schalburg K., Leong J., Cooper G., Davidson W.S., Koop B.F.;
RT "Osmerus mordax full-length cDNAs.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E1-like enzyme which specifically catalyzes the second step
CC in ufmylation. Accepts the ubiquitin-like modifier UFM1 from the E1
CC enzyme UBA5 and forms an intermediate with UFM1 via a thioester
CC linkage. Ufmylation is involved in reticulophagy (also called ER-phagy)
CC induced in response to endoplasmic reticulum stress.
CC {ECO:0000250|UniProtKB:Q9Y3C8}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UFC1
CC subfamily. {ECO:0000305}.
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DR EMBL; BT075060; ACO09484.1; -; mRNA.
DR AlphaFoldDB; C1BKD1; -.
DR SMR; C1BKD1; -.
DR GO; GO:0061657; F:UFM1 conjugating enzyme activity; 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 Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR014806; Ufc1.
DR PANTHER; PTHR12921; PTHR12921; 1.
DR Pfam; PF08694; UFC1; 1.
DR PIRSF; PIRSF008716; DUF1782; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
PE 2: Evidence at transcript level;
KW Ubl conjugation pathway.
FT CHAIN 1..167
FT /note="Ubiquitin-fold modifier-conjugating enzyme 1"
FT /id="PRO_0000391957"
FT ACT_SITE 116
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3C8"
SQ SEQUENCE 167 AA; 19261 MW; BDF1B0CE1B373D31 CRC64;
MADDATRKAV SDIPLLKTNS GPRDKELWVQ RLREEYLALI KYVENNKVAD NDWFRLESNK
EGTRWFGKCW YIHDLMKYEF DVEFDIPVTY PTTAPEVAIP ELDGKTAKMY RGGKICLTDH
FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLISKGIVV HKEQQNN