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OTULL_RAT
ID   OTULL_RAT               Reviewed;         353 AA.
AC   Q3B7D8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Inactive ubiquitin thioesterase OTULINL;
GN   Name=Otulinl {ECO:0000312|RGD:1563205};
GN   Synonyms=Fam105a {ECO:0000312|RGD:1563205};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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).
CC   -!- FUNCTION: Lacks deubiquitinase activity.
CC       {ECO:0000250|UniProtKB:Q9NUU6}.
CC   -!- SUBUNIT: Does not bind ubiquitin or ubiquitin-like proteins.
CC       {ECO:0000250|UniProtKB:Q9NUU6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NUU6}.
CC       Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NUU6};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NUU6}. Nucleus
CC       envelope {ECO:0000250|UniProtKB:Q9NUU6}.
CC   -!- DOMAIN: The N-terminal region that precedes the OTU domain mediates
CC       interaction with cellular membranes. {ECO:0000250|UniProtKB:Q9NUU6}.
CC   -!- SIMILARITY: Belongs to the peptidase C65 family. Otulin subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Although highly similar to the deubiquitinase OTULIN, lacks
CC       both the conserved active site residue Cys at position 136 which is
CC       replaced by an Asp residue and the conserved active site residue His at
CC       residue 347 which is replaced by a Gln residue, and does not have
CC       deubiquitinase activity. {ECO:0000250|UniProtKB:Q9NUU6}.
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DR   EMBL; BC107649; AAI07650.1; -; mRNA.
DR   RefSeq; NP_001032737.1; NM_001037648.1.
DR   AlphaFoldDB; Q3B7D8; -.
DR   SMR; Q3B7D8; -.
DR   STRING; 10116.ENSRNOP00000062926; -.
DR   PaxDb; Q3B7D8; -.
DR   GeneID; 310190; -.
DR   KEGG; rno:310190; -.
DR   UCSC; RGD:1563205; rat.
DR   CTD; 54491; -.
DR   RGD; 1563205; Otulinl.
DR   eggNOG; ENOG502QVY0; Eukaryota.
DR   InParanoid; Q3B7D8; -.
DR   OrthoDB; 1416236at2759; -.
DR   PhylomeDB; Q3B7D8; -.
DR   PRO; PR:Q3B7D8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   InterPro; IPR023235; FAM105.
DR   InterPro; IPR023236; OTULINL.
DR   PANTHER; PTHR33662; PTHR33662; 1.
DR   Pfam; PF16218; Peptidase_C101; 1.
DR   PRINTS; PR02055; PROTEINF105.
DR   PRINTS; PR02056; PROTEINF105A.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome.
FT   CHAIN           1..353
FT                   /note="Inactive ubiquitin thioesterase OTULINL"
FT                   /id="PRO_0000274406"
FT   DOMAIN          125..353
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          1..80
FT                   /note="Required for membrane binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUU6"
SQ   SEQUENCE   353 AA;  41793 MW;  6068015EDB4FDFB4 CRC64;
     MKATRSAPRE RERSRTTSGS DQVHSWILVP SQVLHAVWRI ARASVMTALS LLSATLSYFR
     SLYLYLGHQL KWWIGYLQRK FKRNLSVEAE VDLLSYCARE WKGETPRARL MRKAYEELFW
     RYHVKCVRPV KRDNYDALRS VLFQIFSQGL SFPSWMKEKD IVKLPEKLLF SQGCNWIQQY
     SFGPEKYTGS NVFGKLRKCV ELLKLQWTEF SGMRDYHKRG SMCNSLFSDA ILECKLYEAL
     KFLMLYQVTE VYEQMKTNKI VPSLFRLLFS RESSPDPLSF MMNHLNSIGD TCGLDQIDMF
     ILGYSLQVKI KVFRLFKFNS RDFAVYYPEE PLREWPEISL LTENDHQYHI PVF
 
 
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