CSN1_RAT
ID CSN1_RAT Reviewed; 471 AA.
AC P97834;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=COP9 signalosome complex subunit 1;
DE Short=SGN1;
DE Short=Signalosome subunit 1;
DE AltName: Full=G protein pathway suppressor 1;
DE Short=GPS-1;
DE AltName: Full=JAB1-containing signalosome subunit 1;
DE AltName: Full=MFH protein;
GN Name=Gps1; Synonyms=Cops1, Csn1;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Pineal gland;
RX PubMed=9863633; DOI=10.1016/s0303-7207(98)00133-6;
RA Nitz B., Ivell R., Hartung S., Middendorff R., Olcese J.;
RT "A fusca gene homologue in mammalian tissues: developmental regulation in
RT the rat testes.";
RL Mol. Cell. Endocrinol. 144:131-138(1998).
RN [2]
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).
RN [3]
RP PROTEIN SEQUENCE OF 125-130 AND 134-143, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454 AND SER-463, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Essential component of the COP9 signalosome complex (CSN), a
CC complex involved in various cellular and developmental processes. The
CC CSN complex is an essential regulator of the ubiquitin (Ubl)
CC conjugation pathway by mediating the deneddylation of the cullin
CC subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl
CC ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The
CC complex is also involved in phosphorylation of p53/TP53, c-jun/JUN,
CC IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association
CC with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN
CC promotes and protects degradation by the Ubl system, respectively.
CC Suppresses G-protein- and mitogen-activated protein kinase-mediated
CC signal transduction (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9.
CC In the complex, it probably interacts directly with COPS2, COPS3, COPS4
CC and COPS5. Interacts directly with inositol kinase ITPK1. Interacts
CC with CAPN8. {ECO:0000250|UniProtKB:Q13098,
CC ECO:0000250|UniProtKB:Q99LD4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis.
CC {ECO:0000269|PubMed:9863633}.
CC -!- DOMAIN: The PCI domain is necessary and sufficient for the interactions
CC with other CSN subunits of the complex. Mediates the interaction with
CC CAPN8 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminal part (1-196), which is not required for
CC deneddylating activity and CSN complex formation, is nevertheless
CC essential for other aspects of CSN complex function, such as repression
CC of c-fos/FOS expression. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CSN1 family. {ECO:0000305}.
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DR EMBL; X87885; CAA61139.1; -; mRNA.
DR EMBL; BC061746; AAH61746.1; -; mRNA.
DR PIR; S57449; S57449.
DR RefSeq; NP_001257868.1; NM_001270939.1.
DR RefSeq; NP_446421.3; NM_053969.3.
DR AlphaFoldDB; P97834; -.
DR SMR; P97834; -.
DR BioGRID; 250638; 1.
DR STRING; 10116.ENSRNOP00000066704; -.
DR iPTMnet; P97834; -.
DR PhosphoSitePlus; P97834; -.
DR jPOST; P97834; -.
DR PaxDb; P97834; -.
DR PRIDE; P97834; -.
DR GeneID; 117039; -.
DR KEGG; rno:117039; -.
DR CTD; 2873; -.
DR RGD; 621532; Gps1.
DR eggNOG; KOG0686; Eukaryota.
DR InParanoid; P97834; -.
DR OrthoDB; 859626at2759; -.
DR PhylomeDB; P97834; -.
DR Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:P97834; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0008180; C:COP9 signalosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000338; P:protein deneddylation; ISO:RGD.
DR InterPro; IPR033008; CSN1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR019585; Rpn7/CSN1.
DR InterPro; IPR045135; Rpn7_N.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR14145; PTHR14145; 1.
DR PANTHER; PTHR14145:SF2; PTHR14145:SF2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF10602; RPN7; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT CHAIN 1..471
FT /note="COP9 signalosome complex subunit 1"
FT /id="PRO_0000120961"
FT DOMAIN 249..411
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 445..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13098"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13098"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 387
FT /note="V -> L (in Ref. 2; AAH61746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 53428 MW; ED919C9A9F3C8711 CRC64;
MQIDVDPQED PQNAPDVNYV VENPTLDLEQ YAASYSGLMR IERLQFIADR CPPLRVEALK
MALSFVQRTF NVDMYEEIHR KLSEATRELQ NAPDAIPESG VEPPPLDTAW VEATRKKALL
KLEKLDTDLK NYKGNSIKES IRRGHDDLGD HYLDCGDLSN ALKCYSRARD YCTSAKHVIN
MCLNVIKVSV YLQNWSHVLS YVSKAESTPE IAEQRGERDS QTQAILTKLK CAAGLAELAA
RKYKQAAKCF LLASFDHCDF PELLSPSNVA VYGGLCALAT FDRQELQRNV ISSSSFKLFL
ELEPQVRDII FKFYESKYAS CLKMLDEMKD NLLLDMYLAP HVRTLYTQIR NRALIQYFSP
YVSADMHKMA AAFNTTVAAL EDELTQVILE GLINARIDSH SKILYARDVD QRSTTFEKSL
LMGKEFQRRA KAMILRAAVL RNQIHVKSPP REGSQGELTP ANSQSRMSTN M
