AMSH2_ARATH
ID AMSH2_ARATH Reviewed; 223 AA.
AC Q6NKP9; A8MQQ2; Q2V4P1; Q9SGZ1; Q9XII9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=AMSH-like ubiquitin thioesterase 2;
DE EC=3.4.19.-;
DE AltName: Full=Deubiquitinating enzyme AMSH2;
GN Name=AMSH2; OrderedLocusNames=At1g10600; ORFNames=F20B24.2, T10O24.25;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 3).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20543027; DOI=10.1105/tpc.110.075952;
RA Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D.,
RA Geldner N., Chory J., Schwechheimer C.;
RT "The deubiquitinating enzyme AMSH3 is required for intracellular
RT trafficking and vacuole biogenesis in Arabidopsis thaliana.";
RL Plant Cell 22:1826-1837(2010).
CC -!- FUNCTION: Zinc metalloprotease that cleaves 'Lys-48'- and 'Lys-63'-
CC linked polyubiquitin chains. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6NKP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NKP9-2; Sequence=VSP_039636;
CC Name=3;
CC IsoId=Q6NKP9-3; Sequence=VSP_039635;
CC -!- DOMAIN: The JAMM motif is essential for the protease activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39585.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF17652.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007067; AAD39585.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009398; AAF17652.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28606.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28607.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28608.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM61042.1; -; Genomic_DNA.
DR EMBL; AK317451; BAH20118.1; -; mRNA.
DR EMBL; BT012645; AAT06464.1; -; mRNA.
DR EMBL; AK175458; BAD43221.1; -; mRNA.
DR PIR; E86239; E86239.
DR RefSeq; NP_001031020.1; NM_001035943.2. [Q6NKP9-3]
DR RefSeq; NP_001077505.1; NM_001084036.1. [Q6NKP9-2]
DR RefSeq; NP_001323286.1; NM_001331916.1. [Q6NKP9-1]
DR RefSeq; NP_172530.2; NM_100936.3. [Q6NKP9-1]
DR AlphaFoldDB; Q6NKP9; -.
DR SMR; Q6NKP9; -.
DR STRING; 3702.AT1G10600.1; -.
DR MEROPS; M67.A05; -.
DR iPTMnet; Q6NKP9; -.
DR PaxDb; Q6NKP9; -.
DR PRIDE; Q6NKP9; -.
DR ProteomicsDB; 245041; -. [Q6NKP9-1]
DR EnsemblPlants; AT1G10600.1; AT1G10600.1; AT1G10600. [Q6NKP9-1]
DR EnsemblPlants; AT1G10600.2; AT1G10600.2; AT1G10600. [Q6NKP9-3]
DR EnsemblPlants; AT1G10600.3; AT1G10600.3; AT1G10600. [Q6NKP9-2]
DR EnsemblPlants; AT1G10600.4; AT1G10600.4; AT1G10600. [Q6NKP9-1]
DR GeneID; 837603; -.
DR Gramene; AT1G10600.1; AT1G10600.1; AT1G10600. [Q6NKP9-1]
DR Gramene; AT1G10600.2; AT1G10600.2; AT1G10600. [Q6NKP9-3]
DR Gramene; AT1G10600.3; AT1G10600.3; AT1G10600. [Q6NKP9-2]
DR Gramene; AT1G10600.4; AT1G10600.4; AT1G10600. [Q6NKP9-1]
DR KEGG; ath:AT1G10600; -.
DR Araport; AT1G10600; -.
DR TAIR; locus:2019903; AT1G10600.
DR eggNOG; KOG2880; Eukaryota.
DR InParanoid; Q6NKP9; -.
DR OMA; YEHCANV; -.
DR PhylomeDB; Q6NKP9; -.
DR PRO; PR:Q6NKP9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NKP9; baseline and differential.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR CDD; cd08066; MPN_AMSH_like; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..223
FT /note="AMSH-like ubiquitin thioesterase 2"
FT /id="PRO_0000397099"
FT DOMAIN 49..177
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 127..140
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 72
FT /note="Indirect zinc-binding"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..102
FT /note="MVTLSSPSPSLSCVENVTCKSSHVSRVLISGTDNINHGESSEAKILRDVHIS
FT ERLLEDFTELARENTEKDLETCGTLAAFLERGIFYVTTLIIPKQESTSNS -> MFISQ
FT KGYWRISLSLQERTLRRTSRLVGLSLPFLVLRFSSFMNLM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039635"
FT VAR_SEQ 166..167
FT /note="KS -> N (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039636"
SQ SEQUENCE 223 AA; 24939 MW; 223AC9C0B65C3FF0 CRC64;
MVTLSSPSPS LSCVENVTCK SSHVSRVLIS GTDNINHGES SEAKILRDVH ISERLLEDFT
ELARENTEKD LETCGTLAAF LERGIFYVTT LIIPKQESTS NSCQAMNEVE VFSIQNEREL
YPVGWIHTHP SQGCFMSSVD LHTHYSYQVM VPEAFAIVVA PTDSSKSYGI FKLTDPGGME
VLRGCSETGF HPHKEPEDGN PVYEHCSNVY KNSNLRFEIF DLR
