UFM1_CAEBR
ID UFM1_CAEBR Reviewed; 93 AA.
AC Q61E22; A8XF37;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Ubiquitin-fold modifier 1;
DE Flags: Precursor;
GN Name=ufm-1 {ECO:0000312|WormBase:CBG12253};
GN ORFNames=CBG12253 {ECO:0000312|WormBase:CBG12253};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Ubiquitin-like modifier which can be covalently attached via
CC an isopeptide bond to substrate proteins as a monomer or a lysine-
CC linked polymer (By similarity). The so-called ufmylation requires the
CC ufm-1-activating E1 enzyme uba-5, the ufm-1-conjugating E2 enzyme ufc-
CC 1, and probably the ufm-1-ligase E3 enzyme ufl-1 (By similarity).
CC {ECO:0000250|UniProtKB:P34661, ECO:0000250|UniProtKB:P61960}.
CC -!- SUBUNIT: Interacts with odr-8; leading to deufmylation.
CC {ECO:0000250|UniProtKB:P34661}.
CC -!- SIMILARITY: Belongs to the UFM1 family. {ECO:0000305}.
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DR EMBL; HE600962; CAP31259.1; -; Genomic_DNA.
DR RefSeq; XP_002642670.1; XM_002642624.1.
DR AlphaFoldDB; Q61E22; -.
DR SMR; Q61E22; -.
DR STRING; 6238.CBG12253; -.
DR EnsemblMetazoa; CBG12253.1; CBG12253.1; WBGene00033229.
DR GeneID; 8584664; -.
DR KEGG; cbr:CBG_12253; -.
DR CTD; 8584664; -.
DR WormBase; CBG12253; CBP17483; WBGene00033229; Cbr-ufm-1.
DR eggNOG; KOG3483; Eukaryota.
DR HOGENOM; CLU_175114_0_0_1; -.
DR InParanoid; Q61E22; -.
DR OMA; INPAQNA; -.
DR OrthoDB; 1575050at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990592; P:protein K69-linked ufmylation; IBA:GO_Central.
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 Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..91
FT /note="Ubiquitin-fold modifier 1"
FT /id="PRO_0000042138"
FT PROPEP 92..93
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT /id="PRO_0000042139"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1)"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255"
SQ SEQUENCE 93 AA; 9756 MW; 617075F12AF3594E CRC64;
MSGEASAPAA KVTFKITLTS DPKLPFKVLS VPEAAPFTSV LRYAAEEFKV PAATSAIITN
DGVGINPAQS AGNIFLKHGS ELRLIPRDRV GGF
