STALP_MOUSE
ID STALP_MOUSE Reviewed; 436 AA.
AC Q76N33; Q76LY0; Q8VEK5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=AMSH-like protease;
DE Short=AMSH-LP;
DE EC=3.4.19.- {ECO:0000250|UniProtKB:Q96FJ0};
DE AltName: Full=AMSH family protein;
DE Short=AMSH-FP;
DE AltName: Full=STAM-binding protein-like 1;
GN Name=Stambpl1; Synonyms=Amshlp;
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 [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12943674; DOI=10.1016/s0006-291x(03)01550-x;
RA Kitajima K., Matsumoto K., Tahara M., Takahashi H., Nakamura T.,
RA Nakamura T.;
RT "A newly identified AMSH-family protein is specifically expressed in
RT haploid stages of testicular germ cells.";
RL Biochem. Biophys. Res. Commun. 309:135-142(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ishii N., Sugamura K.;
RT "Cloning of a gene for the mouse AMSH-like-protein.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AMSH-FPalpha, ALM alpha;
CC IsoId=Q76N33-1; Sequence=Displayed;
CC Name=2; Synonyms=AMSH-FPbeta, ALM beta;
CC IsoId=Q76N33-2; Sequence=VSP_014649;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is widely
CC expressed while isoform 2 is testis-specific.
CC {ECO:0000269|PubMed:12943674}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18343.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB066211; BAD00166.1; -; mRNA.
DR EMBL; AB066212; BAD00167.1; -; mRNA.
DR EMBL; AB066213; BAD00168.1; -; mRNA.
DR EMBL; AB010121; BAD06408.1; -; mRNA.
DR EMBL; AB010122; BAD06409.1; -; mRNA.
DR EMBL; BC018343; AAH18343.1; ALT_INIT; mRNA.
DR CCDS; CCDS29756.1; -. [Q76N33-1]
DR RefSeq; NP_083958.3; NM_029682.4. [Q76N33-1]
DR RefSeq; XP_006527514.1; XM_006527451.3. [Q76N33-1]
DR RefSeq; XP_006527515.1; XM_006527452.3. [Q76N33-1]
DR RefSeq; XP_006527516.1; XM_006527453.3.
DR RefSeq; XP_006527517.1; XM_006527454.3.
DR RefSeq; XP_006527519.1; XM_006527456.3.
DR RefSeq; XP_006527520.1; XM_006527457.3.
DR RefSeq; XP_017173797.1; XM_017318308.1.
DR AlphaFoldDB; Q76N33; -.
DR SMR; Q76N33; -.
DR STRING; 10090.ENSMUSP00000059927; -.
DR MEROPS; M67.003; -.
DR iPTMnet; Q76N33; -.
DR PhosphoSitePlus; Q76N33; -.
DR EPD; Q76N33; -.
DR jPOST; Q76N33; -.
DR MaxQB; Q76N33; -.
DR PaxDb; Q76N33; -.
DR PeptideAtlas; Q76N33; -.
DR PRIDE; Q76N33; -.
DR ProteomicsDB; 258635; -. [Q76N33-1]
DR ProteomicsDB; 258636; -. [Q76N33-2]
DR Antibodypedia; 45641; 106 antibodies from 20 providers.
DR DNASU; 76630; -.
DR Ensembl; ENSMUST00000054956; ENSMUSP00000059927; ENSMUSG00000024776. [Q76N33-1]
DR Ensembl; ENSMUST00000119603; ENSMUSP00000112938; ENSMUSG00000024776. [Q76N33-1]
DR Ensembl; ENSMUST00000239240; ENSMUSP00000159218; ENSMUSG00000024776. [Q76N33-1]
DR GeneID; 76630; -.
DR KEGG; mmu:76630; -.
DR UCSC; uc008hgc.1; mouse. [Q76N33-1]
DR CTD; 57559; -.
DR MGI; MGI:1923880; Stambpl1.
DR VEuPathDB; HostDB:ENSMUSG00000024776; -.
DR eggNOG; KOG2880; Eukaryota.
DR GeneTree; ENSGT00940000153710; -.
DR HOGENOM; CLU_023304_0_1_1; -.
DR InParanoid; Q76N33; -.
DR OMA; FGVQDQH; -.
DR OrthoDB; 411229at2759; -.
DR PhylomeDB; Q76N33; -.
DR TreeFam; TF323215; -.
DR Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR BioGRID-ORCS; 76630; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Stambpl1; mouse.
DR PRO; PR:Q76N33; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q76N33; protein.
DR Bgee; ENSMUSG00000024776; Expressed in spermatid and 210 other tissues.
DR ExpressionAtlas; Q76N33; baseline and differential.
DR Genevisible; Q76N33; MM.
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; 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 GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Hydrolase; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..436
FT /note="AMSH-like protease"
FT /id="PRO_0000194875"
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:0007744|PubMed:21183079"
FT VAR_SEQ 1..166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12943674"
FT /id="VSP_014649"
FT CONFLICT 194
FT /note="I -> M (in Ref. 3; AAH18343)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="V -> M (in Ref. 3; AAH18343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 49640 MW; 6AF263DF5EC4FD9B CRC64;
MEQPFTVNSL KKLAAMPDHT DVSLSPEERV RALSKLGCNI SINEDITPRR YFRSGVEMER
MASVYLEEGN LENAFVLYNK FITLFVEKLP SHRDYQQCAV PEKQDIMKKL KEIAFPRTDE
LKTDLLRKYN IEYQEYLQSK NKYKAEILKK LEHQRLIEAE RQRIAQMRQQ QLESEQFLFF
EDQLKKQELA RGQIRGQDSP VLSEQTDGSA LSCFSTHQSN SLRNAFADHP HKSDGSNFAN
YSPPVNRALK PAATLSAVQN LVVEGLRCVV LSRDLCHKFL LLADSNTVRG IETCGILCGK
LTHNEFTITH VVVPKQSAGP DYCDVENVEE LFNVQDQHGL LTLGWIHTHP TQTAFLSSVD
LHTHCSYQLM LPEAIAIVCS PKHKDTGIFR LTNAGMLEVS TCKKKGFHPH TKDPKLFSIC
SHVLVKDIKT TVLDLR
