CUL7_RAT
ID CUL7_RAT Reviewed; 1692 AA.
AC D3ZEF4;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Cullin-7 {ECO:0000250|UniProtKB:Q8VE73};
DE Short=CUL-7 {ECO:0000250|UniProtKB:Q8VE73};
GN Name=Cul7;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FBXW8 AND OBSL1, AND SUBCELLULAR LOCATION.
RX PubMed=21572988; DOI=10.1371/journal.pbio.1001060;
RA Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E.,
RA Gygi S.P., Harper J.W., Bonni A.;
RT "An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi
RT morphology and dendrite patterning.";
RL PLoS Biol. 9:E1001060-E1001060(2011).
CC -!- FUNCTION: Core component of the 3M and Cul7-RING(FBXW8) complexes,
CC which mediates the ubiquitination of target proteins. Core component of
CC the 3M complex, a complex required to regulate microtubule dynamics and
CC genome integrity. It is unclear how the 3M complex regulates
CC microtubules, it could act by controlling the level of a microtubule
CC stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity
CC and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin-
CC protein ligase with FBXW8, which mediates ubiquitination and consequent
CC degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1.
CC Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite
CC patterning in brain (PubMed:21572988). Mediates ubiquitination and
CC degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8)
CC complex recognizes and binds IRS1 previously phosphorylated by S6
CC kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates
CC ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated
CC MAP4K1/HPK1, leading to its degradation, thereby affecting cell
CC proliferation and differentiation. Acts as a regulator in trophoblast
CC cell epithelial-mesenchymal transition and placental development. Does
CC not promote polyubiquitination and proteasomal degradation of p53/TP53.
CC While the Cul7-RING(FBXW8) and the 3M complexes are associated and
CC involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may
CC be have additional functions (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:21572988}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:21572988}.
CC -!- SUBUNIT: Component of the 3M complex, composed of core components CUL7,
CC CCDC8 and OBSL1. Part of a Cul7-RING complex consisting of CUL7, RBX1,
CC SKP1 and FBXW8. Interacts with a complex of SKP1 and FBXW8, but not
CC with SKP1 alone. Interacts with CUL9; leading to inhibit CUL9 activity.
CC Interacts with FBXW8; interaction is mutually exclusive of binding to
CC CUL9 or p53/TP53. Interacts with p53/TP53; the interaction
CC preferentially involves tetrameric and dimeric p53/TP53. The CUL7-CUL9
CC heterodimer seems to interact specifically with p53/TP53. Interacts
CC with CUL1; the interactions seems to be mediated by FBXW8 (By
CC similarity). Interacts with OBSL1 and FBXW8. Interacts (as part of the
CC 3M complex) with HDAC4 and HDAC5; it is negatively regulated by ANKRA2
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:21572988}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21572988}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:21572988}. Golgi apparatus
CC {ECO:0000269|PubMed:21572988}. Note=During mitosis, localizes to the
CC mitotic apparatus. CCDC8 is required for centrosomal location (By
CC similarity). Colocalizes with FBXW8 at the Golgi apparatus in neurons;
CC localization to Golgi is mediated by OBSL1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; AABR06058791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D3ZEF4; -.
DR DIP; DIP-60186N; -.
DR IntAct; D3ZEF4; 2.
DR STRING; 10116.ENSRNOP00000024266; -.
DR jPOST; D3ZEF4; -.
DR PaxDb; D3ZEF4; -.
DR PeptideAtlas; D3ZEF4; -.
DR PRIDE; D3ZEF4; -.
DR UCSC; RGD:1587048; rat.
DR RGD; 1587048; Cul7.
DR eggNOG; ENOG502RDJD; Eukaryota.
DR HOGENOM; CLU_001067_1_0_1; -.
DR InParanoid; D3ZEF4; -.
DR PhylomeDB; D3ZEF4; -.
DR TreeFam; TF101154; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:D3ZEF4; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; D3ZEF4; RN.
DR GO; GO:1990393; C:3M complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0001890; P:placenta development; ISS:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021097; CPH_domain.
DR InterPro; IPR031223; CUL7.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR22771:SF3; PTHR22771:SF3; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF11515; Cul7; 1.
DR Pfam; PF00888; Cullin; 1.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
DR PROSITE; PS51284; DOC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Golgi apparatus; Isopeptide bond;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..1692
FT /note="Cullin-7"
FT /id="PRO_0000422125"
FT DOMAIN 791..970
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT REGION 1319..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1374
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 1570
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1692 AA; 192660 MW; BA6B35D511F3883C CRC64;
MVGELRYREF RVPLGPGLHA YPDELIRQRV GHNGHPEYQI RWLILRRGDD GDSSQVDCKA
EHILLWMTDD EIYANCHKML GEDGQVIRPS QESAEAGALD KSVLGEMETD VKSLIQRALR
QLEECVGAVP PAPLLHTVHV LSAYASIEPL TGVFKDRRVL DLVMHMLSSP DYQIRWSAGR
MIQALSSHDA GTRTQILLSL SQQEAIEKHL DFDSRCALLA LFAQATLTEH PMSFEGVQLP
QVPGRLLFSL VKRYLCVTFL LDRLNGNAED QDAQNNFIPE ELNAGRGRVE LEFSMAMGTL
ISELVQAMRW DWASSRSESS SPIFQPPPTE FFRPRAQRFR RSRRFRPRTA FASVNTYALY
VRDTLRPGMR VRMLEDFEEI SAGDEGQFRQ SNDGMPPVQV LWDSTGHTYW VHWHMLEILG
FEEDIEDVVD IDDQGAMVHG GLGVAPPFQH WKPIAQLFAE PYVVPEEEDR EEREHLTQAE
WWELFFFIKK LNAEERQHVV ELLQEFLEGE HVLDFEILPE LTVPVELAQD LMLSLPQQLD
DSALRDLFNC YVYRKYGPEV LVGKRNRPFV LDDQLNLFRI ETDSEAQDPP SQSASPALRQ
LVEGLGPSGK LLVDLERALS SEAPQENEVK PCLLQLQEEP QPFLTLMRSL DTPASNKALH
LTALRILMQL VNFPEALLLP WHEAMDACMT CLRSPNTDRE VLQELIFFLH RLTSTSRDYA
VILNQLGARD AISKVLEKHR GKLELAQELR DMVFKCEKHA HLYRKLTTNI LGGCIQMVLG
QIEDHRRTHR PIQIPFFDVF LRYLCQGSSA EVKKNKYWEK VEVSSNPHRA SRLTDRNAKT
YWESNGTAGS HFITVHMRPG VLIRQLTLLV AGEDSSYMPA WVVVCGGDSI SSVNTELNAV
NVMPHASRVI LLENLTRFWP IVQIRIKRCQ QGGINTRIRG LEVLGPKPTF WPVFREQLCR
HTRLFYMVRA QAWSQDIAED RRSLLHLSSR LNGALRQEQN FADRFLPDEE AALALSKTCW
EALVSPLVQN ITSPDEDSTS SLGWLLNQYL ECREAAYNPQ SRAAAFSSRV RHLTHLLVHV
EPCEAAPPVV AISQSKGRNR SHDWSSLTTR GLPSSIMRNL TRCWRSVVEE QVNKFLTSSW
KDDDFVPRYC ERYYILQKSS SELFGPRAAF LLAMRNGCAD ALLRLPFLRA AHVSEQFARH
IDQRIQGSRM GGARGMEMLA QLQRCLESVL ILSPLEIATT FEHYYQHYMA DRLLSVGSSW
LEGAVLEQIG PCFPGRLPQQ MLQTLNISEE LQRRFHVYQL QQLDQELLKL EDTEKKIQVA
HEDSGKEHKS KKEDAAGETA AVAMADEEEE EGKKEEGEEE EGEGEEELEE EEERYYEGTM
PEVCVLVLSP RFWPVASVCH MLNPTTCLPS YLRGTINHYS NFYSKSQSHS GLEKESPRQL
QWTWQGRAEV QFGDQILHVS TVQMWLLLHL NHLKAVSVES LQALSELPPE VLNKAIGPLT
SSRGPLDLQE QKNIPGGVLK IRDDSEEPRP RRGNVWLIPP QTYLKAEDEE GRNLEKRRNL
LNCLVVRILK AHGDEGLHID QLVHLVLEAW EKGPCPPRGL VSSLGRGAAC RSSDVLSCIL
HLLGKGTLRR HDDRPQMLFY AVPITVMEPH TESLNPGSSG PNPPLTFHTL QIRSRGVPYA
SCTGTQTFST FR
