STBPA_DANRE
ID STBPA_DANRE Reviewed; 418 AA.
AC Q6TH47; B7ZV76; Q7SXP3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=STAM-binding protein-like A;
DE EC=3.4.19.- {ECO:0000250|UniProtKB:O95630};
GN Name=stambpa; Synonyms=amsh, stambp;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2008) 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; AY398309; AAQ97742.1; -; mRNA.
DR EMBL; BC055512; AAH55512.1; -; mRNA.
DR EMBL; BC171484; AAI71484.1; -; mRNA.
DR RefSeq; NP_956792.1; NM_200498.1.
DR AlphaFoldDB; Q6TH47; -.
DR SMR; Q6TH47; -.
DR STRING; 7955.ENSDARP00000071164; -.
DR MEROPS; M67.003; -.
DR PaxDb; Q6TH47; -.
DR GeneID; 797422; -.
DR KEGG; dre:797422; -.
DR CTD; 797422; -.
DR ZFIN; ZDB-GENE-040426-1551; stambpa.
DR eggNOG; KOG2880; Eukaryota.
DR InParanoid; Q6TH47; -.
DR OrthoDB; 411229at2759; -.
DR PhylomeDB; Q6TH47; -.
DR Reactome; R-DRE-5689901; Metalloprotease DUBs.
DR PRO; PR:Q6TH47; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0032154; C:cleavage furrow; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..418
FT /note="STAM-binding protein-like A"
FT /id="PRO_0000194872"
FT DOMAIN 251..382
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 199..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 329..342
FT /note="JAMM motif"
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 331
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="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 384
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 BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT SITE 274
FT /note="Indirect zinc-binding"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT CONFLICT 153
FT /note="Q -> H (in Ref. 2; AAH55512)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="Q -> E (in Ref. 1; AAQ97742)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="G -> V (in Ref. 1; AAQ97742)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="D -> N (in Ref. 1; AAQ97742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47510 MW; 826B0EC26683BF3F CRC64;
MSEHTDCSVS SEDRVRALTK LGSSVDVSED VPPRRYFRSG MEIIRMANIY ADEGNVEHAF
ILYNKYITLF IEKLPKHREY KTANIPEKKE TMRKLKEIAF PKAEELKKLL LKQYDKEHAE
YLVRKRAEDA ARAVEMLKQQ EQEAQRQRLA ELQQRQREQE QFSAFEEMIR RQELEKERRR
IVQEFSIPVS PTAPDVLLPD VHGPPQASLS PQTPPAGATN HQGLPAFDRS LKPSVPVSAG
HSALVNGLRQ LFVPAELCQR FLKLAETNTA RAVETCGILC GKLMKNAFTV THVIVPKQCG
GPDYCDTENE EELFLIQDQN DLITLGWIHT HPTQTAFLSS VDLHTHCSYQ MMLPESIAIV
CSPKFNETGY FRLTDYGMDD VGTCKQRGFH PHPKDPPLFA ASHHVSITDG SVTMLDLR
