CUL7_PONAB
ID CUL7_PONAB Reviewed; 1729 AA.
AC Q5RCJ3;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Cullin-7;
DE Short=CUL-7;
GN Name=CUL7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Mediates ubiquitination and degradation of IRS1 in
CC a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and
CC binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2).
CC The Cul7-RING(FBXW8) complex also mediates ubiquitination of
CC MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1,
CC leading to its degradation, thereby affecting cell proliferation and
CC differentiation. Acts as a regulator in trophoblast cell epithelial-
CC mesenchymal transition and placental development. Does not promote
CC polyubiquitination and proteasomal degradation of p53/TP53. While the
CC Cul7-RING(FBXW8) and the 3M complexes are associated and involved in
CC common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have
CC additional functions (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
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. Interacts
CC with OBSL1 (By similarity). Interacts (as part of the 3M complex) with
CC HDAC4 and HDAC5; it is negatively regulated by ANKRA2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC Note=Colocalizes with FBXW8 at the Golgi apparatus in neurons;
CC localization to Golgi is mediated by OBSL1. During mitosis, localizes
CC to the mitotic apparatus. CCDC8 is required for centrosomal location
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; CR858277; CAH90514.1; -; mRNA.
DR RefSeq; NP_001125271.1; NM_001131799.1.
DR AlphaFoldDB; Q5RCJ3; -.
DR BMRB; Q5RCJ3; -.
DR STRING; 9601.ENSPPYP00000018598; -.
DR PRIDE; Q5RCJ3; -.
DR GeneID; 100172168; -.
DR KEGG; pon:100172168; -.
DR CTD; 9820; -.
DR eggNOG; ENOG502RDJD; Eukaryota.
DR InParanoid; Q5RCJ3; -.
DR OrthoDB; 469819at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Unplaced.
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:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS: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; ISS: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; ISS: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 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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Golgi apparatus; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..1729
FT /note="Cullin-7"
FT /id="PRO_0000223468"
FT DOMAIN 845..1024
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT REGION 350..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14999"
FT CROSSLNK 1607
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1729 AA; 194424 MW; 8901AAC72F704313 CRC64;
MVGELRYREF RVPLGPGLHA YPDELIRQRV GHDGHPEYQI RWLILRRGDE GDGGSGQVDC
KAEHILLWMS KDEIYANCHK MLGEDGQVIG PSQESTGEVG ALDKSVLEEM ETDVKSLIQR
ALRQLEECVG TIPPAPLLHT VHVLSAYASI EPLTGVFKDP RVLDLLMHML SSPDYQIRWS
AGRMIQALSS HDAGEGQCGE EGKAGEELGR LRDSQDTVAG ASDLIRTRTQ ILLSLSQQEA
IEKHLDFDSR CALLALFAQA TLSEHPMSFE GIQLPQVPGR VLFSLVKRYL HVTSLLDQLN
DSAAEPGAQN TSAPEEWSGE RGQLELEFSM AMGTLISELV QAIRWDQASD RPRSSARSPG
SIFQPQLADV SPGLPATQAQ PSFRRSRHFR PRSEFASGNT YALYVRDTLQ PGMRVRMLDE
YEEISAGDEG EFRQSNNGVP PVQVLWESTG RTYWVHWHML EILGFEEDIE DMVEADEYQG
AVASRVLGRA LPAWRWRPMT ELYAVPYVLP EDEDSEECEH LTLAEWWELL FFIKKLDGPD
HQEVLQILQE NLDGEILDDE ILAELAVPIE LAQDLLLTLP QRLNDSALRD LINCHVYKKY
GPEALAGNPA YPSLLEAQED VLLEAQAQAK DSEDAAKVEA KEPPSQSPNT PLQRLVEGYG
PAGKILLDLE QALSSEGTQE NKVKPLLLQL QRQPQPFLAL MQSLDTPETN RTLHLTVLRI
LKQLVDFPEA LLLPWHEAVD ACMACLRSPN TDREVLQELI FFLHRLTSVS RDYAVVLNQL
GARDAISKAL EKHLGKLELA QELRDMVFKC EKHAHLYREL ITNILGGCIQ MVLGQIEDHR
RTHRPINIPF FDVFLRYLCQ GSSVEVKEDK CWEKVEVSSN PHRASKLTDR NPKTYWESNG
SAGSRYITLH MRQGILIRQL TLLVASEDSS YMPARVVVCG GDSTSSLHTE LNSVNVMPSA
SRVILLENLT RFWPIIQIRI KRCQQGGIDT RIRGLETLGP KPTFWPVFRE QLCRHTRLFY
MVRAQAWSQD MAEDRRSLLH LSSRLNGALR QEQNFADRFL PDNEAAQALG KTCWEALVSP
VVQNITSPDE DGISPLGWLL DQYLECQEAV FNPQSRGPAF FSRVRRLTHL LVHVEPCEAP
PPVVATPRPK GRNRSHDWSS LATRGLPSSI MRNLTRCRRA VVEKQVNNFL TSSWRDDDFV
PRYCEHFNIL QNSSSELFGP RAAFLLALQN GCAGALLKLP FLKAAHVSEQ FARHIDQQIQ
GSRIGGAQEM ERLAQLQQCL QAVLIFSGLE IATTFEHYYQ HYMADRLLGV VSSWLEGAVL
EQIGPCFPNR LPQQMLQSLS TSKELQRQFH VYQLQQLDQE LLKLEDTEKK IQVGHGASGK
EHKSEKEEEA GAAAAVDVAE GEEEEEENED LYYEGAMPEV SVLVLSRHCW PVASICHTLN
PRTCLPSYLR GTLNRYSNFY NKSQSHPALE RGSQRRLQWT WLGWAELQFG NQTLHVSTVQ
MWLLLYLNDL KAVSVESLLA LSGLSADMLN QAIGPLTSSR GPLDLHEQKD IPGGVLKIRD
GSKEPRSRWD IVRLIPPQTY LQAEGEEGRN LEKRRNLLNC LIVRILKAHG DEGLHIDQLV
CLVLEAWQKG PCPPRGLVSS LGKGSACSST DVLSCILHLL GKGTLRRHDD RPQVLSYAVP
VTVMEPHTES LNPGSSGPNP PLTFHTVQIR SRGVPYASCT ATQSFSTFR
