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UFSP_ARATH
ID   UFSP_ARATH              Reviewed;         645 AA.
AC   Q9STL8; Q304B1; Q3EAM8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable Ufm1-specific protease;
DE            Short=UfSP;
DE            EC=3.4.22.-;
GN   OrderedLocusNames=At3g48380; ORFNames=T29H11.100;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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: Thiol protease which recognizes and hydrolyzes the peptide
CC       bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein
CC       bound to a number of target 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=Q9STL8-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the peptidase C78 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK226935; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB41160.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL049659; CAB41160.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE78408.1; -; Genomic_DNA.
DR   EMBL; AK226935; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T06704; T06704.
DR   RefSeq; NP_680114.1; NM_148861.4. [Q9STL8-1]
DR   AlphaFoldDB; Q9STL8; -.
DR   SMR; Q9STL8; -.
DR   STRING; 3702.AT3G48380.3; -.
DR   MEROPS; C78.A02; -.
DR   iPTMnet; Q9STL8; -.
DR   PaxDb; Q9STL8; -.
DR   ProteomicsDB; 245295; -. [Q9STL8-1]
DR   EnsemblPlants; AT3G48380.1; AT3G48380.1; AT3G48380. [Q9STL8-1]
DR   GeneID; 823996; -.
DR   Gramene; AT3G48380.1; AT3G48380.1; AT3G48380. [Q9STL8-1]
DR   KEGG; ath:AT3G48380; -.
DR   Araport; AT3G48380; -.
DR   eggNOG; KOG2433; Eukaryota.
DR   InParanoid; Q9STL8; -.
DR   PhylomeDB; Q9STL8; -.
DR   PRO; PR:Q9STL8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9STL8; baseline and differential.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   Pfam; PF07910; Peptidase_C78; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Hydrolase; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..645
FT                   /note="Probable Ufm1-specific protease"
FT                   /id="PRO_0000280374"
FT   ACT_SITE        472
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        596
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        598
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   645 AA;  71466 MW;  60A468DFF685D57D CRC64;
     MVPSSETATV RVLCQKLLLS PNHPGTLQWL IGSPFFPPFT VVSTFRCIHH SPDFQQESDD
     LRKLLPKGFE VIGGLIIGDS DAEKSAFEAV RAARRLRKHL SEGGELDDEK IVGASCDVGT
     GTIHFFISKS ENTTKLEPVG SVVYEDKSGK YLWENGCLLH CELPIKLPFY YPASSPSDSK
     EKFSDAIDAV ITQFKEPYVV YIAETLKKAS GGVPKPVVLR GKDLGFGADA SNINRLPSAD
     QVSDIKMLSC SHLCLNNKTA PAVNSAENAD KIHISVLLNR SEKLPTSGAP VAEYFPAMEE
     ARLIVVDLNL DVLTYAPKDL PLMHAVSNLV IPALVDQLYS LKKIILPHLL VEHPQLRIYH
     FNPPGVLHPI TSMYELNYGE TEMKQVDVRK LLHLRLGLPL DRPLLRIANA LDLSVNDDSK
     SNMNRRGSTL LKDVHIGIPS SGVSEGVASI IQGSYEYYHY LQDGFDDSGW GCAYRSLQTI
     ISWFRLQHYT SISVPSHREI QQTLVEIGDK DPSFVGSREW IGAIELSFVL DKLLGVSCKI
     MNFRSGSELP EKCRELAMHF ENQGTPIMIG GGVLAYTLLG VDYDEGSGDC AFLILDPHYT
     GSEDHKKIVN GGWCGWKKAV DSKGKSFFLH NKFYNLLLPQ RPNMV
 
 
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