AMSH1_ARATH
ID AMSH1_ARATH Reviewed; 507 AA.
AC Q8VYB5; Q8LFY1; Q9C747;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=AMSH-like ubiquitin thioesterase 1;
DE EC=3.4.19.-;
DE AltName: Full=Deubiquitinating enzyme AMSH1;
GN Name=AMSH1; OrderedLocusNames=At1g48790; ORFNames=F11I4.4;
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
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=AAG60133.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC073555; AAG60133.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32350.1; -; Genomic_DNA.
DR EMBL; AY072212; AAL60033.1; -; mRNA.
DR EMBL; AY096591; AAM20241.1; -; mRNA.
DR EMBL; AY084581; AAM61146.1; -; mRNA.
DR RefSeq; NP_564533.1; NM_103774.4.
DR AlphaFoldDB; Q8VYB5; -.
DR SMR; Q8VYB5; -.
DR BioGRID; 26526; 3.
DR STRING; 3702.AT1G48790.1; -.
DR MEROPS; M67.A04; -.
DR PaxDb; Q8VYB5; -.
DR PRIDE; Q8VYB5; -.
DR ProteomicsDB; 244421; -.
DR EnsemblPlants; AT1G48790.1; AT1G48790.1; AT1G48790.
DR GeneID; 841301; -.
DR Gramene; AT1G48790.1; AT1G48790.1; AT1G48790.
DR KEGG; ath:AT1G48790; -.
DR Araport; AT1G48790; -.
DR TAIR; locus:2008184; AT1G48790.
DR eggNOG; KOG2880; Eukaryota.
DR HOGENOM; CLU_023304_5_1_1; -.
DR InParanoid; Q8VYB5; -.
DR OMA; GLHGQWQ; -.
DR OrthoDB; 411229at2759; -.
DR PhylomeDB; Q8VYB5; -.
DR PRO; PR:Q8VYB5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYB5; baseline and differential.
DR Genevisible; Q8VYB5; AT.
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 InterPro; IPR015063; USP8_dimer.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..507
FT /note="AMSH-like ubiquitin thioesterase 1"
FT /id="PRO_0000397098"
FT DOMAIN 333..463
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 411..424
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 411
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 413
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 424
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 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 356
FT /note="Indirect zinc-binding"
FT /evidence="ECO:0000250"
FT CONFLICT 11
FT /note="A -> G (in Ref. 4; AAM61146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 57383 MW; A60AF211A0754352 CRC64;
MGSSFETIDI ATSARRIGVD NRISLKFYFR IADNILKQAN IFRAEKNVID LYVMLLRFSS
LALETIPSHR DYRTSLKSNK EYLRMRLLDV LTELEKLKPV VQQRIDELYP KLKPRYNVQA
HPANGSLGWS SAVKPSFNSY DHAKVRNPPG HNSGYMGSRG QQFLNAAPLE ERFRKMSVNF
RPNEETLSKH SILGPGGLSA QWQPPKYDTK VQYPSNIDFS PVVIPSFQQL VDSKPMITNG
SNDEPEKPIV EPSVASNEKI QKNYTEELSS MISFEEPESV NENNLIRQPS PPPVLAEVQD
LVPALCPEVR EPECMIENSL PDESLRSESP LELHIATSMM DTFMRLAKSN TKKNLETCGI
LAGSLKNRKF YITALIIPKQ ESTSDSCQAT NEEEIFEVQD KQSLFPLGWI HTHPTQSCFM
SSIDVHTHYS YQIMLPEAVA IVMAPQDSSR NHGIFRLTTP GGMTVIRNCD RRGFHAHSSP
EDGGPIYNTC KEVYMNPNLK FDVIDLR
