ID   UFL1_ARATH              Reviewed;         804 AA.
AC   Q9LX73;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=E3 UFM1-protein ligase 1 homolog;
DE            EC=2.3.2.-;
DE   AltName: Full=E3 UFM1-protein transferase 1 homolog {ECO:0000305};
GN   OrderedLocusNames=At3g46220; ORFNames=F12M12.190;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: E3 UFM1-protein ligase that mediates ufmylation of target
CC       proteins. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9LX73-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the UFL1 family. {ECO:0000305}.
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DR   EMBL; AL355775; CAB90949.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78135.1; -; Genomic_DNA.
DR   PIR; T49263; T49263.
DR   RefSeq; NP_566883.4; NM_114491.7. [Q9LX73-1]
DR   AlphaFoldDB; Q9LX73; -.
DR   STRING; 3702.AT3G46220.2; -.
DR   iPTMnet; Q9LX73; -.
DR   PaxDb; Q9LX73; -.
DR   ProteomicsDB; 245292; -. [Q9LX73-1]
DR   EnsemblPlants; AT3G46220.1; AT3G46220.1; AT3G46220. [Q9LX73-1]
DR   GeneID; 823767; -.
DR   Gramene; AT3G46220.1; AT3G46220.1; AT3G46220. [Q9LX73-1]
DR   KEGG; ath:AT3G46220; -.
DR   Araport; AT3G46220; -.
DR   eggNOG; KOG2235; Eukaryota.
DR   InParanoid; Q9LX73; -.
DR   PhylomeDB; Q9LX73; -.
DR   PRO; PR:Q9LX73; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LX73; baseline and differential.
DR   Genevisible; Q9LX73; AT.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0061666; F:UFM1 ligase activity; IEA:InterPro.
DR   GO; GO:0071568; F:UFM1 transferase activity; IBA:GO_Central.
DR   GO; GO:1990592; P:protein K69-linked ufmylation; IBA:GO_Central.
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; IBA:GO_Central.
DR   InterPro; IPR018611; Ufl1.
DR   PANTHER; PTHR31057; PTHR31057; 1.
DR   Pfam; PF09743; E3_UFM1_ligase; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..804
FT                   /note="E3 UFM1-protein ligase 1 homolog"
FT                   /id="PRO_0000391894"
FT   REGION          397..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   804 AA;  89073 MW;  F39B6A0A85DDD6DD CRC64;
     MDDELLELQR QFEFAQQVKS SVRLSDRNVV ELVQKLQELG VIDFDLLHTV TGKEYITQEQ
     LRNEITREIS KLGRVSVIDL ADTIGVDLYH VEKQAQDVVL NDPGLMLVQG EIISQSYWDS
     IAEEINERLQ ECSQIAVAEL AGQLQVGSEL VQSVLEPRLG TLVKARLEGG QLYTPAYVER
     VTAMVRGASR GIFVPSNLSA LWAPLQQLVQ ETNGASGVAV ENSFFQSIFN RLLKEEEMLG
     SLRAGTHWTP SAFATAQKEC VDSSFSQNSY ISYESMQKLG ISQAVQFLQS RYPDGTPLAA
     VFIHSSMIEM LDSATEDAIE QNSWIDSLSV LPSSFTSQDA NKMLLLCPSV QSALKAEKAL
     ILGESYVLSS GFIKGIYDQI EKEADAFSIQ ASTATLIHPS SKSSESTESI PANTDKGSKK
     KKGKSASTKA ATVETVPDDE EDARPKSKRN QKKGRDSSSS QKLDSKAGGK KESVKAQESN
     NIIPPDEWVM KKIVDSVPEF EDDGTENPDS ILKHLADHMK PMLINSLKER RKKIFTENAD
     RMRRLIDDLQ KKLDESFLNM QLYEKALDLF EDDQSTAVVL HRHLLRTTAA TIADTLLHGL
     DIHNKMKNGT EVEESKTQDL VLLDSSERTA LAKNLNGSLS KKALALVEAL EGKRVDTFMV
     TFRDLAEESG LVLKKLDKKL ERTLLHSYRK DLISQVSTES DPIALLAKVV SLLFIKIHNK
     ALQAPGRAIA AAISHLKEKL DESAYKTLTD YQTATVTLLA LMSASSGEEH DCSADRILTK
     RELLESQMPL LRTLVLGDSQ PQQS