SENP5_MACFA
ID SENP5_MACFA Reviewed; 755 AA.
AC Q8WP32;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Sentrin-specific protease 5;
DE EC=3.4.22.-;
DE AltName: Full=Sentrin/SUMO-specific protease SENP5;
GN Name=SENP5; ORFNames=QtsA-16408;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
CC -!- FUNCTION: Protease that catalyzes two essential functions in the SUMO
CC pathway: processing of full-length SUMO3 to its mature form and
CC deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak
CC proteolytic activity against full-length SUMO1 or SUMO1 conjugates.
CC Required for cell division. {ECO:0000250|UniProtKB:Q96HI0}.
CC -!- SUBUNIT: Interacts with CCAR2. {ECO:0000250|UniProtKB:Q96HI0}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AB074445; BAB72076.1; -; mRNA.
DR RefSeq; NP_001270238.1; NM_001283309.1.
DR AlphaFoldDB; Q8WP32; -.
DR SMR; Q8WP32; -.
DR STRING; 9541.XP_005545351.1; -.
DR MEROPS; C48.008; -.
DR GeneID; 102117667; -.
DR CTD; 205564; -.
DR eggNOG; KOG0778; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019783; F:ubiquitin-like protein peptidase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016926; P:protein desumoylation; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR InterPro; IPR045577; SENP3_5_cons_dom.
DR InterPro; IPR033465; SENP5.
DR PANTHER; PTHR12606:SF10; PTHR12606:SF10; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR Pfam; PF19722; SENP3_5_N; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..755
FT /note="Sentrin-specific protease 5"
FT /id="PRO_0000101724"
FT REGION 269..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..724
FT /note="Protease"
FT ACT_SITE 646
FT /evidence="ECO:0000250"
FT ACT_SITE 663
FT /evidence="ECO:0000250"
FT ACT_SITE 713
FT /evidence="ECO:0000250"
SQ SEQUENCE 755 AA; 86290 MW; 40EC773CA29B8CEA CRC64;
MKKQRKILWR KGIHLAFSEK WNTGFGGFKK FYFHQHLCIL KAKLGRPITR NRQLRHFQGG
KKALQIQKTW VKDEPPCAKT KFSVDTPHAS TLSSPVKRKD TKHFVSSSRT LLRLQAEKLL
SSAKNSDHEY CREKNLLKTV TDFPSNSALG QANGHRPRTD PQASDFPMKF NGESQSPGES
GAIVITLSNH KRKGFCYGCC RGPEHHRNGG PLIPKQFQLN RHRRIKLSPL MMYEKLSMIR
FRYRILRSQH FRTKSKVCKL RKAQRSWVQK VTGDHQETLR ENGEGGSGSP FPSPEPKDPS
CRQQPYFPDM DSNAVVKGTN SHVPDGHTKG SPFLGKELSL DEAFPDQQNG SATHAWDQSS
CASPKWECTE LIHDIPLPEH HSNTMFVSET EKEIATLGQE NRTSSLSDDG VKLSVSGADT
SVSSVDGPVS QKAVHSENSY QMEEDGSLKQ NILSSELLDH PYCKSPLEAP LVCSGLKLEN
QVGGGKDSQK ASPVDDEQLS VCLSGFLDEV MKKYGSLVPL SEKEVLGRLK DVFNEDFSNR
KPFINREITN YRARHQKCNF RIFYNKHMLD MDDLATLDGQ NWLNDQVINM YGELIMDAVP
DKVHFFNSFF HRQLVTKGYN GVKRWTKKVD LFKKSLLLIP IHLEVHWSLI TVTLSNRIIS
FYDSQGIHFK FCVENIRKYL LTEAREKNRP EFLQGWQTAV TKCIPQQKND SDCGVFVLQY
CKCLALEQPF QFSQEDMPRV RKRIYKELCE CRLMD