UFM1_CAEEL
ID UFM1_CAEEL Reviewed; 94 AA.
AC P34661;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ubiquitin-fold modifier 1;
DE Short=cUfm1 {ECO:0000303|PubMed:29251776};
DE Flags: Precursor;
GN Name=ufm-1 {ECO:0000312|WormBase:ZK652.3};
GN Synonyms=tag-277 {ECO:0000312|WormBase:ZK652.3};
GN ORFNames=ZK652.3 {ECO:0000312|WormBase:ZK652.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Bristol N2;
RA Kohara Y., Shin'i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23449979; DOI=10.1074/jbc.m113.458000;
RA Hertel P., Daniel J., Stegehake D., Vaupel H., Kailayangiri S., Gruel C.,
RA Woltersdorf C., Liebau E.;
RT "The ubiquitin-fold modifier 1 (Ufm1) cascade of Caenorhabditis elegans.";
RL J. Biol. Chem. 288:10661-10671(2013).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=12211038; DOI=10.1002/prot.10197;
RA Cort J.R., Chiang Y., Zheng D., Montelione G.T., Kennedy M.A.;
RT "NMR structure of conserved eukaryotic protein ZK652.3 from C. elegans: a
RT ubiquitin-like fold.";
RL Proteins 48:733-736(2002).
RN [6] {ECO:0007744|PDB:5XDA}
RP X-RAY CRYSTALLOGRAPHY (3.29 ANGSTROMS) OF 11-94 IN COMPLEX WITH ODR-8, AND
RP INTERACTION WITH ODR-8.
RX PubMed=29251776; DOI=10.1002/1873-3468.12951;
RA Kim K.H., Ha B.H., Kim E.E.;
RT "Structural basis for Ufm1 recognition by UfSP.";
RL FEBS Lett. 592:263-273(2018).
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 (PubMed:23449979).
CC {ECO:0000250|UniProtKB:P61960, ECO:0000269|PubMed:23449979}.
CC -!- SUBUNIT: Interacts with odr-8; leading to deufmylation.
CC {ECO:0000269|PubMed:29251776}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestine and head neurons.
CC {ECO:0000269|PubMed:23449979}.
CC -!- SIMILARITY: Belongs to the UFM1 family. {ECO:0000305}.
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DR EMBL; FO080278; CCD62548.1; -; Genomic_DNA.
DR EMBL; AF303260; AAG50218.1; -; mRNA.
DR PIR; S44903; S44903.
DR RefSeq; NP_498705.1; NM_066304.5.
DR PDB; 1L7Y; NMR; -; A=1-94.
DR PDB; 5XDA; X-ray; 3.29 A; G/H/I/J/K/L=11-94.
DR PDBsum; 1L7Y; -.
DR PDBsum; 5XDA; -.
DR AlphaFoldDB; P34661; -.
DR BMRB; P34661; -.
DR SMR; P34661; -.
DR BioGRID; 41308; 10.
DR DIP; DIP-25558N; -.
DR IntAct; P34661; 1.
DR STRING; 6239.ZK652.3.2; -.
DR EPD; P34661; -.
DR PaxDb; P34661; -.
DR PeptideAtlas; P34661; -.
DR EnsemblMetazoa; ZK652.3.1; ZK652.3.1; WBGene00044324.
DR GeneID; 176100; -.
DR KEGG; cel:CELE_ZK652.3; -.
DR CTD; 176100; -.
DR WormBase; ZK652.3; CE00449; WBGene00044324; ufm-1.
DR eggNOG; KOG3483; Eukaryota.
DR GeneTree; ENSGT00390000010391; -.
DR HOGENOM; CLU_175114_0_0_1; -.
DR InParanoid; P34661; -.
DR OMA; INPAQNA; -.
DR OrthoDB; 1575050at2759; -.
DR PhylomeDB; P34661; -.
DR SignaLink; P34661; -.
DR EvolutionaryTrace; P34661; -.
DR PRO; PR:P34661; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00044324; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
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 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..93
FT /note="Ubiquitin-fold modifier 1"
FT /id="PRO_0000042140"
FT PROPEP 94
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT /id="PRO_0000042141"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1)"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT CROSSLNK 93
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:5XDA"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:5XDA"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:5XDA"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5XDA"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:5XDA"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:5XDA"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:5XDA"
SQ SEQUENCE 94 AA; 9791 MW; 618B28AA399E1F65 CRC64;
MSGGTAATTA GSKVTFKITL TSDPKLPFKV LSVPESTPFT AVLKFAAEEF KVPAATSAII
TNDGVGVNPA QPAGNIFLKH GSELRLIPRD RVGH
