ID   STABP_XENLA             Reviewed;         416 AA.
AC   Q63ZM7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=STAM-binding protein-like;
DE            EC=3.4.19.-;
GN   Name=stambp;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-
CC       linked polyubiquitin chains. Does not cleave 'Lys-48'-linked
CC       polyubiquitin chains (By similarity). Functions at the endosome and is
CC       able to oppose the ubiquitin-dependent sorting of receptors to
CC       lysosomes (By similarity). {ECO:0000250|UniProtKB:O95630}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O35864};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O35864};
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; BC082885; AAH82885.1; -; mRNA.
DR   RefSeq; NP_001088078.1; NM_001094609.1.
DR   AlphaFoldDB; Q63ZM7; -.
DR   SMR; Q63ZM7; -.
DR   BioGRID; 104855; 1.
DR   MEROPS; M67.006; -.
DR   DNASU; 494775; -.
DR   GeneID; 494775; -.
DR   KEGG; xla:494775; -.
DR   CTD; 494775; -.
DR   Xenbase; XB-GENE-5926903; stambp.L.
DR   OrthoDB; 411229at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 494775; Expressed in blastula and 19 other tissues.
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   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN           1..416
FT                   /note="STAM-binding protein-like"
FT                   /id="PRO_0000194873"
FT   DOMAIN          249..380
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          214..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           327..340
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   COMPBIAS        230..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         327
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         329
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         340
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         342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT   BINDING         382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT   SITE            272
FT                   /note="Indirect zinc-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FJ0"
SQ   SEQUENCE   416 AA;  47595 MW;  D003FF93D50FA876 CRC64;
     MPEHSDASLP PEERIRALVL KGTSVEVNDD IPPKRYYRSG VELIRMANVY SGEGSIENAF
     ILYNKYITLF IEKLPKHRDY KTANVPEKKE TLKKLKEIAF PKAEELKKEL HKRYKKEYEE
     YSEKQRKEEE ERARRLALQQ QLDAEKQRVA LLKQQQEQQE QVQAFEEMMR RKELEAERLR
     ILHQFSKDEP EAEPLGSPLI PGMNEPPVTP LLPSYGTVQP HPPAVDRSLK PSSYGSNSSG
     VTSDGLRHVK IPRDVCCKFL QLSENNTQRG VETCGILCGK LLQNEFTVTH VIVPKQSGGP
     DYCNTESEEE LFLIQDQQGL ITLGWIHTHP TQTAFLSSVD LHTHCSYQMM LPESIAIVCS
     PKFQETGFFK LTDYGMKEIG ECRQKGFHPH CKEPPLFSAG GHVSVTEQDV TMMDLR