ID   U17L6_HUMAN             Reviewed;         398 AA.
AC   Q6QN14;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein 6;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 17-like protein 6;
DE   AltName: Full=Ubiquitin thioesterase 17-like protein 6;
DE   AltName: Full=Ubiquitin-specific-processing protease 17-like protein 6;
GN   Name=USP17L6P; Synonyms=USP17C, USP17D, USP17N;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE, FUNCTION, CATALYTIC ACTIVITY,
RP   MUTAGENESIS OF CYS-89, AND SUBCELLULAR LOCATION.
RX   PubMed=17109758; DOI=10.1186/1471-2164-7-292;
RA   Shin J.-M., Yoo K.-J., Kim M.-S., Kim D., Baek K.-H.;
RT   "Hyaluronan- and RNA-binding deubiquitinating enzymes of USP17 family
RT   members associated with cell viability.";
RL   BMC Genomics 7:292-292(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   IDENTIFICATION, AND NOMENCLATURE.
RX   PubMed=15780755; DOI=10.1016/j.ygeno.2004.11.013;
RA   Burrows J.F., McGrattan M.J., Johnston J.A.;
RT   "The DUB/USP17 deubiquitinating enzymes, a multigene family within a
RT   tandemly repeated sequence.";
RL   Genomics 85:524-529(2005).
CC   -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC       from specific proteins to regulate different cellular processes that
CC       may include cell proliferation, progression through the cell cycle,
CC       cell migration, and the cellular response to viral infection. Seems to
CC       be non-functional in the regulation of apoptosis.
CC       {ECO:0000269|PubMed:17109758}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:17109758};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17109758}. Cytoplasm
CC       {ECO:0000269|PubMed:17109758}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP17 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: The RS447 megasatellite DNA is a highly polymorphic conserved
CC       tandem repetitive sequence which contains a copy of the USP17 gene. It
CC       is present with an interindividual variation in copy number, ranging
CC       from 20 to 103, and can be found in the genome both on chromosome 4 and
CC       chromosome 8. The high similarity between the UPS17-like genes makes
CC       impossible to clearly assign data to one of the genes of the family.
CC       Oligonucleotides designed in RNAi experiments are for instance not
CC       specific of a given UPS17-like gene. {ECO:0000305}.
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DR   EMBL; AY533200; AAS59847.1; -; mRNA.
DR   EMBL; AC116655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q6QN14; -.
DR   SMR; Q6QN14; -.
DR   MEROPS; C19.A82; -.
DR   MEROPS; C19.A87; -.
DR   BioMuta; HGNC:37179; -.
DR   DMDM; 187663985; -.
DR   AGR; HGNC:37179; -.
DR   GeneCards; USP17L6P; -.
DR   HGNC; HGNC:37179; USP17L6P.
DR   neXtProt; NX_Q6QN14; -.
DR   InParanoid; Q6QN14; -.
DR   PhylomeDB; Q6QN14; -.
DR   Pharos; Q6QN14; Tbio.
DR   PRO; PR:Q6QN14; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q6QN14; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR   GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR   CDD; cd02661; Peptidase_C19E; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006:SF651; INACTIVE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 17-LIKE PROTEIN 4-RELATED; 1.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Nucleus; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..398
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 17-like
FT                   protein 6"
FT                   /id="PRO_0000331648"
FT   DOMAIN          80..375
FT                   /note="USP"
FT   ACT_SITE        89
FT                   /note="Nucleophile"
FT   ACT_SITE        334
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MUTAGEN         89
FT                   /note="C->S: Abolishes enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:17109758"
FT   CONFLICT        9
FT                   /note="R -> G (in Ref. 1; AAS59847)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="S -> P (in Ref. 1; AAS59847)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        364
FT                   /note="S -> T (in Ref. 1; AAS59847)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   398 AA;  44690 MW;  350E31797F7EFD44 CRC64;
     MEDDSLYLRG EWQFNHFSKL TSSRPDAAFA EIQRTSLPEK SPLSCETRVD LCDDLAPVAR
     QLAPREKLPL SSRRPAAVGA GLQNMGNTCY VNASLQCLTY TPPLANYMLS REHSQTCHRH
     KGCMLCTMQA HITRALHNPG HVIQPSQALA AGFHRGKQED AHEFLMFTVD AMKKACLPGH
     KQVDHHSKDT TLIHQIFGGY WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVQQALEQL
     VKPEELNGEN AYHCGVCLQR APASKTLTLH TSAKVLILVL KRFSDVTGNK IAKNVQYPEC
     LDMQPYMSQQ NTGPLVYVLY AVLVHAGWSC HNGHYFSYVK AQEGQWYKMD DAEVTASSIT
     SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGSED
//