ID A0A1S3WKU8_ERIEU Unreviewed; 2324 AA.
AC A0A1S3WKU8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 18-JUN-2025, entry version 43.
DE SubName: Full=Cullin-9 {ECO:0000313|RefSeq:XP_016046907.1};
GN Name=CUL9 {ECO:0000313|RefSeq:XP_016046907.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016046907.1};
RN [1] {ECO:0000313|RefSeq:XP_016046907.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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DR RefSeq; XP_016046907.1; XM_016191421.1.
DR FunCoup; A0A1S3WKU8; 1108.
DR STRING; 9365.ENSEEUP00000005270; -.
DR eggNOG; KOG1815; Eukaryota.
DR InParanoid; A0A1S3WKU8; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd20347; BRcat_RBR_CUL9; 1.
DR CDD; cd20359; Rcat_RBR_CUL9; 1.
DR CDD; cd16624; RING-HC_RBR_CUL9; 1.
DR FunFam; 1.20.120.1750:FF:000014; Cullin 9; 1.
DR FunFam; 2.60.120.260:FF:000046; Cullin 9; 1.
DR FunFam; 3.30.230.130:FF:000009; Cullin 9; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.230.130; Cullin, Chain C, Domain 2; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR056405; ARM_CUL7_CUL9.
DR InterPro; IPR047561; BRcat_RBR_CUL9.
DR InterPro; IPR021097; CPH_domain.
DR InterPro; IPR055486; CUL7/CUL9_N.
DR InterPro; IPR045093; Cullin.
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; IPR002867; IBR_dom.
DR InterPro; IPR047560; Rcat_RBR_CUL9.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR047562; RING-HC_RBR_CUL9.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22771:SF2; CULLIN-9; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF24742; ARM_CUL7_CUL9; 1.
DR Pfam; PF11515; Cul7; 1.
DR Pfam; PF23168; CUL7_CUL9_N; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 3: Inferred from homology;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 954..1133
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 1355..1622
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT DOMAIN 1877..2094
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1881..1928
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 2047..2090
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 275..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2254..2324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..596
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..616
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1256
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2313..2324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2324 AA; 260005 MW; 64CE893568D1D742 CRC64;
MVRERRTGDF MVPLGPQLQA YPEELIRQRP GHDGHPEYLI RWSVLKCGES SRVDVEEGKA
EHILMWLSAP EVYANCPMLL GERTLSKGPQ LESVGSPGSF PRDPGGLDDV AMGELEADVR
ALVRRATRQL AEGGASSLTA AVLHTVHVLS AYASIGPLTG VFRETGALDL LMHMLCNPEP
QIRRSAGKML QALAAHNAGS RAHVLLSLSQ QDGIEQHMDF DSCYTLLELF AETTSSEEHC
MAFESIHLPQ IPGKLLFSLV KRYLCVTSLL DQLNSSPEPG AGDQASASSR EELGLKKSRG
QRELEFSMAV GNLISELVRS LGWARNLSEQ GTSPPRPARS IFQPCMSSPS LLLPTSTFTA
TPRKPGWAFR PRSEFSSRSG YGEYMQQTLR PGMRVRMLDD YEEISAGDEG EFRQSNNGVP
PVQVFWQSTG RTYWVHWHML EILGPEEAVE DTAPAAVKKE EEAAMLGTAF PSWDWKPVDG
LYSLPYLQPE PQKNEELGYL TQAEWWELLF FIKKLDACEQ QPIFQSLREK LDETLSEKAL
GEISVPIEVA EGLLRVLSSR FEGSTLSDLL SSQIYTKYGL PRDELSSSSS SHSPSSTPDP
EEEFRSEASF SEEEAESPQG KAERPEAEAE PAIVKTEPPM AQSDSQLFNQ LLKTEGMALP
PEMKEAADEM ARALRGPGPR SSLHQHVAAI VATVQIPILD SNLQLSGLYA LSQAVEEVTE
RDHPLVRPDR SLRYAVILLL CTWAAVVETP GAEGQDGSLE LLMRSLVGDS SAELLLDLER
MLCQEDSSGS TVGPLLKRLQ QETQPFLLLL RTLDAPGPNK TLLLTALRVM TQLLDHPEAM
VLPWHEVLEP CLNCLSGPNS DSEIVQVLLC FLHRLASVHK DYAVVLCCLG AKETLSKVPD
KHSDQLLLAC ELEHLVTACE KHAQLYSKLT SSILAGCIQM VLGQIEDHRR TQQPINIPFF
DVFLRHLCQG SSVEVKEDKC WEKVEVSSNP HRASKLTDRN PKTYWESNGS TGSHYITLHM
HRGVLVRQLT LLVASEDSSY MPARVMVFGG DSASCISTEL NTVNVLPSAT RVVLLENLNR
FWPIIQIRIK RCQQGGIDTR VRGVEVLGPK PTFWPLFREQ LCRRTCLFYT IQAQAWSQDI
AEDRKRLLQL CPRLNRVLRH EQNFADRFLP DEEAAQALGK TCWEALVSPL VQNITSPDAE
GVSSLGWLLD QYLEQRESSQ NPLSRAASFA SRVRRLCHLL VHVEPPPGPS PEPSPQPFSK
NSKGRDRSPG PSPILPSSSL RNITQCWLSV VQEQVSRFLA AAWRAPDFVP RYCKLYERLQ
RAGSELFGPR AAFTLALRSG FSGALLQQSF LTAAHMSEQF ARHIDQQIQG GLIGGAHGVD
MLGQLQRHLE PIMVLSGLEL ATTFEHFYQH YMADRLLSLG SNWLEGAVLE QIGFCFPNRL
PQQMLQSLST SEELQRQFHV YQLQQFDKLL LEQGNKEEQG LEEEEEEEEE ETEKKLFIEE
PSPTASILVL SPRCWPVSPL CYLYHPRKCL PIEFCDALDR FSNFYIQSQN HPVLDVGPHR
RLQWTWLGRA ELQFGNQTLH VSTVQMWLLL HFNHTEEVSI ETLLKKSDLT GELLLQALLP
LTSETGPLTL HEGQDFPPGG ILRLREPEPQ ACNEALWLIP PQMYLNVEED EGRILEQKRN
LLSCLLVRIL KAQGERGLHI DQLVFLVLEA WKKGPNPPGS LGHTVAGGVA CSSTDVLSCI
LHLLGQGYVQ RRDDRPQILI YGIPEPTGPC RGQADIPFCG SQASKTSKPS PKAVATLASL
QLPAGRTMSP QEVEGLMEQT VRQVQETLNL QPDVAQHLLA HSHWGAEQLL QSYSENPEPL
LLAAGLCVPQ AQDAPTRPDH CPVCVSPLEP DSSLPSLCCR HYCCKSCWNE YLTTRIEQNL
VLNCTCPIAD CSAQPTGAFI RAIVSSPEVI SKYEKALLRG YVESCSNLTW CTNPQGCDRI
LCRQGLGCGT TCSKCGWASC FTCSFPEAHY PASCGHMSQW VDDGGYYDGM SVEAQSKHLA
KLISKRCPSC QAPIEKNEGC LHMTCAKCKH GFCWRCLKSW KPNHKDYYNC SAMVSKAARQ
EKRFQDYNER CTFHHQARDF AVNLRHQVSA IHEVPPPRSF TFLSDACRGL EQARKVLAYA
CVYSFYNQDT EHMDVVEQQT ESLELHTNAL QILLEENLLR CRDLASSLRL LRADCLNTGL
ELLRRIQERL LAILQHSTQD FRVGLQSPSL EVREVKGSNM PAMPPQGSSG VEVEEEEEEE
EDDVPEWQQD EFDDSFSDDE ESENLDRDTF FFGDEEEEDD EAYD
//