LOCUS       NP_001119751             793 aa            linear   ROD 30-JUL-2024
DEFINITION  E3 UFM1-protein ligase 1 [Rattus norvegicus].
ACCESSION   NP_001119751 XP_001061009 XP_232850
VERSION     NP_001119751.1
DBSOURCE    REFSEQ: accession NM_001126279.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Qin,B., Yu,J., Nowsheen,S., Wang,M., Tu,X., Liu,T., Li,H., Wang,L.
            and Lou,Z.
  TITLE     UFL1 promotes histone H4 ufmylation and ATM activation
  JOURNAL   Nat Commun 10 (1), 1242 (2019)
   PUBMED   30886146
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Yoo,H.M., Kang,S.H., Kim,J.Y., Lee,J.E., Seong,M.W., Lee,S.W.,
            Ka,S.H., Sou,Y.S., Komatsu,M., Tanaka,K., Lee,S.T., Noh,D.Y.,
            Baek,S.H., Jeon,Y.J. and Chung,C.H.
  TITLE     Modification of ASC1 by UFM1 is crucial for ERalpha transactivation
            and breast cancer development
  JOURNAL   Mol Cell 56 (2), 261-274 (2014)
   PUBMED   25219498
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Zhang,Y., Zhang,M., Wu,J., Lei,G. and Li,H.
  TITLE     Transcriptional regulation of the Ufm1 conjugation system in
            response to disturbance of the endoplasmic reticulum homeostasis
            and inhibition of vesicle trafficking
  JOURNAL   PLoS One 7 (11), e48587 (2012)
   PUBMED   23152784
REFERENCE   4  (residues 1 to 793)
  AUTHORS   Lemaire,K., Moura,R.F., Granvik,M., Igoillo-Esteve,M.,
            Hohmeier,H.E., Hendrickx,N., Newgard,C.B., Waelkens,E., Cnop,M. and
            Schuit,F.
  TITLE     Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect
            pancreatic beta cells from ER stress-induced apoptosis
  JOURNAL   PLoS One 6 (4), e18517 (2011)
   PUBMED   21494687
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 793)
  AUTHORS   Shiwaku,H., Yoshimura,N., Tamura,T., Sone,M., Ogishima,S.,
            Watase,K., Tagawa,K. and Okazawa,H.
  TITLE     Suppression of the novel ER protein Maxer by mutant ataxin-1 in
            Bergman glia contributes to non-cell-autonomous toxicity
  JOURNAL   EMBO J 29 (14), 2446-2460 (2010)
   PUBMED   20531390
REFERENCE   6  (residues 1 to 793)
  AUTHORS   Wu,J., Lei,G., Mei,M., Tang,Y. and Li,H.
  TITLE     A novel C53/LZAP-interacting protein regulates stability of
            C53/LZAP and DDRGK domain-containing Protein 1 (DDRGK1) and
            modulates NF-kappaB signaling
  JOURNAL   J Biol Chem 285 (20), 15126-15136 (2010)
   PUBMED   20228063
REFERENCE   7  (residues 1 to 793)
  AUTHORS   Kwon,J., Cho,H.J., Han,S.H., No,J.G., Kwon,J.Y. and Kim,H.
  TITLE     A novel LZAP-binding protein, NLBP, inhibits cell invasion
  JOURNAL   J Biol Chem 285 (16), 12232-12240 (2010)
   PUBMED   20164180
REFERENCE   8  (residues 1 to 793)
  AUTHORS   Tatsumi,K., Sou,Y.S., Tada,N., Nakamura,E., Iemura,S., Natsume,T.,
            Kang,S.H., Chung,C.H., Kasahara,M., Kominami,E., Yamamoto,M.,
            Tanaka,K. and Komatsu,M.
  TITLE     A novel type of E3 ligase for the Ufm1 conjugation system
  JOURNAL   J Biol Chem 285 (8), 5417-5427 (2010)
   PUBMED   20018847
REFERENCE   9  (residues 1 to 793)
  AUTHORS   Foster,L.J., Zeemann,P.A., Li,C., Mann,M., Jensen,O.N. and
            Kassem,M.
  TITLE     Differential expression profiling of membrane proteins by
            quantitative proteomics in a human mesenchymal stem cell line
            undergoing osteoblast differentiation
  JOURNAL   Stem Cells 23 (9), 1367-1377 (2005)
   PUBMED   16210410
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166498.1.
            
            On or before May 7, 2008 this sequence version replaced
            XP_232850.2, XP_001061009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166498.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21"
     Protein         1..793
                     /product="E3 UFM1-protein ligase 1"
                     /note="E3 UFM1-protein transferase 1; regulator of
                     C53/LZAP and DDRGK1; multiple alpha-helix protein located
                     at ER"
                     /calculated_mol_wt=89454
     Region          2..212
                     /region_name="Required for E3 UFM1-protein ligase
                     activity. /evidence=ECO:0000250|UniProtKB:O94874"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV24.1)"
     Region          2..200
                     /region_name="Mediates interaction with DDRGK1.
                     /evidence=ECO:0000250|UniProtKB:O94874"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV24.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O94874; propagated from
                     UniProtKB/Swiss-Prot (B2GV24.1)"
     Region          7..284
                     /region_name="E3_UFM1_ligase"
                     /note="E3 UFM1-protein ligase 1; pfam09743"
                     /db_xref="CDD:462874"
     Region          121..250
                     /region_name="Involved in CDK5RAP3-binding.
                     /evidence=ECO:0000250|UniProtKB:O94874"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV24.1)"
     Region          200..400
                     /region_name="Mediates interaction with TRIP4.
                     /evidence=ECO:0000250|UniProtKB:O94874"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV24.1)"
     Region          410..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV24.1)"
     Site            433
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8CCJ3; propagated from
                     UniProtKB/Swiss-Prot (B2GV24.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B2GV24.1)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94874; propagated from
                     UniProtKB/Swiss-Prot (B2GV24.1)"
     Region          490..683
                     /region_name="Mediates interaction with CDK5RAP3.
                     /evidence=ECO:0000269|PubMed:20531390"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV24.1)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O94874; propagated from
                     UniProtKB/Swiss-Prot (B2GV24.1)"
     Region          742..769
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV24.1)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CCJ3; propagated from
                     UniProtKB/Swiss-Prot (B2GV24.1)"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CCJ3; propagated from
                     UniProtKB/Swiss-Prot (B2GV24.1)"
     CDS             1..793
                     /gene="Ufl1"
                     /gene_synonym="Maxer; RGD1309308"
                     /coded_by="NM_001126279.1:48..2429"
                     /db_xref="GeneID:313115"
                     /db_xref="RGD:1309308"
ORIGIN      
        1 madaweeirr laadfqraqf aestqrlser ncieivnkli sqkqlevvht ldgkeyitpa
       61 qiskemrdel hvrggrvniv dlqqvinvdl thienrvgdi iksekhvqmv lgqlvdenyl
      121 drlseevndk lqesgqvtvs elcktydlpg dfltqaltqr lgriinghld ldnrgvifte
      181 afvarhkari rglfsaitrp tavnslvsky gfqeqllysv leelvstgrl rgtvvggrqd
      241 kavfvpdiys rtqstwvdsf frqngylefd alsrlgipda vnyikkrykn tpllflkatc
      301 vgqglvdqve asveeaissg twvdvspllp sslsvedaam llqqvmrpfg khasatvfsd
      361 tvvvsekfin dctklfserm hqkaekemkn npvhliteed lkqisilesv ntnkkdkkde
      421 rrkkategsg svrgggggna reykikkvkk kgrkdedsdd esqsshagkk kpditfmfqd
      481 eiegclrkhi pdapeefise laehlikpln kmylevvrsv fmsstsasgt grkrtikdlq
      541 eevsnlynni rlfekgmkyf addtqtaltk hllktvctdi tnlmfnflas dlmmavedpa
      601 titsdmrkki lsklteetkv altklhnsln eksiedflsc ldsateacdi mvkkgdkkre
      661 rqilfqhrqa ladqlkvted palilhltsv llfqfsthsm lhapgrcvpq iiaflhnkip
      721 edqhtllvky qglvvkqlvs qnkksgqged pssddldkeq hdvtnttrke lqelslsikd
      781 lvlkprkssv tee
//
