UFM1_MOUSE
ID UFM1_MOUSE Reviewed; 85 AA.
AC P61961; Q14346; Q3TLT0; Q542A7; Q9CPX2; Q9NZF2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000303|PubMed:21494687};
DE Flags: Precursor;
GN Name=Ufm1 {ECO:0000303|PubMed:21494687, ECO:0000312|MGI:MGI:1915140};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Mammary gland, Pancreas, Placenta, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP STRUCTURE BY NMR.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of mouse hypothetical 9.1 kDa protein, a ubiquitin-like
RT fold.";
RL Submitted (NOV-2002) to the PDB data bank.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21494687; DOI=10.1371/journal.pone.0018517;
RA Lemaire K., Moura R.F., Granvik M., Igoillo-Esteve M., Hohmeier H.E.,
RA Hendrickx N., Newgard C.B., Waelkens E., Cnop M., Schuit F.;
RT "Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect pancreatic
RT beta cells from ER stress-induced apoptosis.";
RL PLoS ONE 6:E18517-E18517(2011).
CC -!- FUNCTION: Ubiquitin-like modifier which can be covalently attached via
CC an isopeptide bond to lysine residues of substrate proteins as a
CC monomer or a lysine-linked polymer (PubMed:21494687). The so-called
CC ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-
CC conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1.
CC Ufmylation is involved in reticulophagy (also called ER-phagy) induced
CC in response to endoplasmic reticulum stress. Ufmylation of TRIP4
CC regulates nuclear receptors-mediated transcription (By similarity).
CC {ECO:0000250|UniProtKB:P61960, ECO:0000269|PubMed:21494687}.
CC -!- SUBUNIT: Interacts with UBA5. Interacts with UFC1.
CC {ECO:0000250|UniProtKB:P61960}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21494687}. Cytoplasm
CC {ECO:0000269|PubMed:21494687}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in
CC secretory tissues (at protein level). {ECO:0000269|PubMed:21494687}.
CC -!- SIMILARITY: Belongs to the UFM1 family. {ECO:0000305}.
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DR EMBL; AK007788; BAB25255.1; -; mRNA.
DR EMBL; AK008280; BAB25572.1; -; mRNA.
DR EMBL; AK089948; BAC41011.1; -; mRNA.
DR EMBL; AK148146; BAE28374.1; -; mRNA.
DR EMBL; AK166332; BAE38712.1; -; mRNA.
DR EMBL; AK167301; BAE39406.1; -; mRNA.
DR EMBL; AK167321; BAE39423.1; -; mRNA.
DR EMBL; BC061065; AAH61065.1; -; mRNA.
DR CCDS; CCDS38430.1; -.
DR RefSeq; NP_080711.1; NM_026435.5.
DR PDB; 1J0G; NMR; -; A=1-85.
DR PDBsum; 1J0G; -.
DR AlphaFoldDB; P61961; -.
DR SMR; P61961; -.
DR BioGRID; 212514; 13.
DR STRING; 10090.ENSMUSP00000118478; -.
DR iPTMnet; P61961; -.
DR PhosphoSitePlus; P61961; -.
DR EPD; P61961; -.
DR jPOST; P61961; -.
DR MaxQB; P61961; -.
DR PaxDb; P61961; -.
DR PeptideAtlas; P61961; -.
DR PRIDE; P61961; -.
DR ProteomicsDB; 300190; -.
DR TopDownProteomics; P61961; -.
DR Antibodypedia; 42138; 73 antibodies from 20 providers.
DR DNASU; 67890; -.
DR Ensembl; ENSMUST00000146598; ENSMUSP00000118478; ENSMUSG00000027746.
DR GeneID; 67890; -.
DR KEGG; mmu:67890; -.
DR UCSC; uc008pfa.2; mouse.
DR CTD; 51569; -.
DR MGI; MGI:1915140; Ufm1.
DR VEuPathDB; HostDB:ENSMUSG00000027746; -.
DR eggNOG; KOG3483; Eukaryota.
DR GeneTree; ENSGT00390000010391; -.
DR HOGENOM; CLU_175114_0_0_1; -.
DR InParanoid; P61961; -.
DR OMA; INPAQNA; -.
DR OrthoDB; 1575050at2759; -.
DR PhylomeDB; P61961; -.
DR TreeFam; TF312934; -.
DR BioGRID-ORCS; 67890; 14 hits in 74 CRISPR screens.
DR ChiTaRS; Ufm1; mouse.
DR EvolutionaryTrace; P61961; -.
DR PRO; PR:P61961; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P61961; protein.
DR Bgee; ENSMUSG00000027746; Expressed in ectoplacental cone and 240 other tissues.
DR ExpressionAtlas; P61961; baseline and differential.
DR Genevisible; P61961; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR GO; GO:0071569; P:protein ufmylation; IDA:UniProtKB.
DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; ISS:UniProtKB.
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; Cytoplasm; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..83
FT /note="Ubiquitin-fold modifier 1"
FT /id="PRO_0000042126"
FT PROPEP 84..85
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT /id="PRO_0000042127"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1)"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1J0G"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:1J0G"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1J0G"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1J0G"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1J0G"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:1J0G"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1J0G"
SQ SEQUENCE 85 AA; 9118 MW; EDB2412E5E5836D8 CRC64;
MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA
QTAGNVFLKH GSELRIIPRD RVGSC
