STALP_PONAB
ID STALP_PONAB Reviewed; 436 AA.
AC Q5R558;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=AMSH-like protease;
DE Short=AMSH-LP;
DE EC=3.4.19.- {ECO:0000250|UniProtKB:Q96FJ0};
DE AltName: Full=STAM-binding protein-like 1;
GN Name=STAMBPL1; Synonyms=AMSHLP;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-
CC linked polyubiquitin chains. Acts as a positive regulator of the TORC1
CC signaling pathway by mediating 'Lys-63'-linked deubiquitination of
CC SESN2, thereby inhibiting SESN2-interaction with the GATOR2 complex.
CC Does not cleave 'Lys-48'-linked polyubiquitin chains.
CC {ECO:0000250|UniProtKB:Q96FJ0}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q96FJ0};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96FJ0};
CC -!- DOMAIN: The JAMM motif is essential for the protease activity.
CC {ECO:0000250|UniProtKB:O35864}.
CC -!- SIMILARITY: Belongs to the peptidase M67C family. {ECO:0000305}.
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DR EMBL; CR861012; CAH93108.1; -; mRNA.
DR RefSeq; NP_001126841.1; NM_001133369.1.
DR AlphaFoldDB; Q5R558; -.
DR SMR; Q5R558; -.
DR STRING; 9601.ENSPPYP00000002847; -.
DR MEROPS; M67.003; -.
DR GeneID; 100173848; -.
DR KEGG; pon:100173848; -.
DR CTD; 57559; -.
DR eggNOG; KOG2880; Eukaryota.
DR InParanoid; Q5R558; -.
DR OrthoDB; 411229at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
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 Acetylation; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein;
KW Protease; Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..436
FT /note="AMSH-like protease"
FT /id="PRO_0000194876"
FT DOMAIN 269..397
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 347..360
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 347
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 349
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 360
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 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT SITE 292
FT /note="Indirect zinc-binding"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
SQ SEQUENCE 436 AA; 49740 MW; DED87DF5062D66EA CRC64;
MDQPFTVNSL KKLAAMPDHT DISLSPEERV RALSKLGCNV TISEDITPRR YFRSGVEMER
MASVYLEEGN LENAFVLYNK FITLFVEKLP NHRDYQQCAV PEKQDIMKKL KEIAFPRTDE
LKNDLLKKYN VEYQEYLQSK NQYKAEILKK LEHQRLIEAE RKRIAQMRQQ QLESEQFLFF
EDQLKKQELA RGQMRSQQTS GLSEQIDGSA LSCFSTHQNN SLLNVFADQP NKSDATNYAS
HSPPVNRALT PAATLSAVQN LVVEGLRCVV LPKDLCHKFL QLAESNTVRG IETCGILCGK
LTHNEFTITH VIVPKQSAGP DYCDVENVEE LFNVQDQHDL LTLGWIHTHP TQTAFLSSVD
LHTHCSYQLM LSEAIAIVCS PKHKDTGIFR LTNAGMLEVS ACKKKGFHPH TKEPRLFSIC
KHVLVKDIKI IVLDLR
