ID A0A8P4K931_DICLA Unreviewed; 2643 AA.
AC A0A8P4K931;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=Cullin-9 {ECO:0008006|Google:ProtNLM};
GN Name=LOC127361208 {ECO:0000313|Ensembl:ENSDLAP00005068206.1};
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489 {ECO:0000313|Ensembl:ENSDLAP00005068206.1, ECO:0000313|Proteomes:UP000694389};
RN [1] {ECO:0000313|Ensembl:ENSDLAP00005068206.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
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DR RefSeq; XP_051251585.1; XM_051395625.1.
DR Ensembl; ENSDLAT00005075190.1; ENSDLAP00005068206.1; ENSDLAG00005032921.1.
DR GeneID; 127361208; -.
DR GeneTree; ENSGT00940000153954; -.
DR Proteomes; UP000694389; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd20347; BRcat_RBR_CUL9; 1.
DR CDD; cd20359; Rcat_RBR_CUL9; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 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; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
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; 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; IPR044066; TRIAD_supradom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22771:SF4; CULLIN 7-RELATED; 1.
DR PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 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; PF10557; Cullin_Nedd8; 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 SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000694389};
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 1256..1435
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 1668..1919
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT DOMAIN 2176..2394
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2347..2390
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2544..2643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..127
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..728
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..748
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1587
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2544..2568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2569..2578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2591..2633
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2634..2643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2643 AA; 295188 MW; A7721ACE44067A0F CRC64;
MRIQQCGAPV ENDTANVTRL GSDTLGRKRK QRSRGKTDTK GKVCDTAVTM VGERRNGNLL
VQLGPRLQAY PEELIRQRRN HDGQTEYLIR WCLVTIDDGS SSGGGASEAG GTGGGGGSDS
SGSGGSTSGE TKPENILMWM STEDVYANCP TLLGKRKTDT QRPLQQQEKQ QGGEFSDGGQ
RSGGEFPSDV TFDEVELSDM KEDVKNLVRR ARKQMTKKSD FSISITHTIH VLSAYASIGS
LVGVFKETGA LNLLMELLCN KETQTRRSAG KMLRALASHD AGSRAYVLLS LSQQDGIEQH
MDFDNRYTLL ELFAETTSSE EHGISFEGIH LPQIPGKLLF SLVKRYLCVT SLMDKLNTAG
AESPSDRQDA SPSPASSNAA HQTEHLRVQR EFDFTMAMAN LISELVRVMG WDRNRQPPDG
SAHHLDGGGA CGEDQREEVL SRPLLRSIFQ PRFCASPVIL AATSAVAAPA ATPPKKKTGN
GYKTRSDFAS RSAYVEYVQD NLKSGMMVRM LEDYEEVSAG DEGEFRYSND GSPPVQVYWN
SLSRTYWVHW HMVEIVGSGG SSQAEKETQE KASSLTETLK LTAVSQTFFS KPPGGLYSLP
YLSEGLQREP LALSRAEWWE ILFFIKKLEP KQQQEVNGIL LQSLEDQDVV LDDSALIGLS
VPGDVAKKLL HYLKQKLPSS CLSDLLCSHA FCKHYLRRGG GSLEDEELLA ESSLSSSGLG
GGGGGGGQSS SSSSSASASS SSAMGSVSKK AKKEPPADSG CGSPETESEL PSEDDSKYPE
DLEDKMKVFN NPRVQGKKTV LEKLGEVVDI LKKGGAGSDQ AQQLAAVLFI TRLLEDKGTQ
EKNSMRSDSA QTIRDKVLKL LVELLGSSSK DLVTSTLRLT HLLMLKYEWR VSFATEGGVK
AVLSCMQEFS TVTHIQQLAL ATLKVITGAS KHDLRSVGSS VPLSESGTQM MLEIFASIGS
ATPEGSKGLL GAVPAAIDLM LQTKGCMLSV RNGLLVIIML ISNHKSLAEQ LVAADVTTVL
KKCLTLSGAE TMLAIIALNH ISMVHKLESK DCREQLDFKD TELQMLVVSL KELTATKEVI
QTLEQLLCDD TSQLEEERSQ VTHSRDTYQD LVRLMEQHRA DRAVQLSILR ILNKFLDNYQ
EDMLPWHESI EPCLSSMTAF INDREVVQLF IRFLYRLASL NKDYAVVMCR LGTKDALVKA
LDKHSTNLLL VTELRDLITD CEKYASLYKK MTTSVLAGCI QMVLGQIEEH RRSHQPINIP
FFDVFLRNLC QGSSVELKED KCWEKVEVSS NHHRANKLTD KNPKTYWESN GCTGSHFINI
YMHKGVIIRQ LAILVASEDS SYMPARILVL GGDEPTNINT ELNTVNVTPS ASRVVLLENM
TRFWSIIQIR VKRCQQGGID TRVHGFEVLG PKPTFWPVFK EQLCCRTFLF YSTKAHTWCQ
EVLEDQSQLL QLFNKLNSAL RHEQMFADRF LPDAEAAEAL GRTCWEALIT PIVHSITLSE
SSAASPLSWL LSEYLENAES ARRCKSRAAI FNSRVRRLTH LLVHVDTSRP DGEELRPPVR
SNGKEGKNKD NSAASSSSSS SSAKPKVKSS SSIAGIALCW QGVVQRQVKK FLESSCSLPD
FVERYRSLYL QLKNAMEELF GQQTAFVLAL RHGFSAALLQ LSILKAMHVS ERFAQYIDQM
IQASGVACGS VETLERLQQF LEPMLFLSGL ELANTFEHFY RYYLGDRLLA QGNVWLETAV
IDQIGSCFPS RFPQQMLKNL SESAELQQEF HLYRLQQLDR CLQEHDQMME EEWAESEEEA
EVQVLVLSPR CWAVSSLCFL DEPTKHFPAE LCSYLNQFTQ FYTHSQYMYG LNHSKPRRLQ
WTWLGHAELQ FGCWTLHVST LQMFILLQFN SQEEVRVDAL LQATGLSAAV LLHALLPLIS
EGGPLICSQP NEPIQGVLQL NQQVASRSQE GVPASVQLLP KQTYLNVDED AAGTLERKRN
YIYCLIVHIM KQEKEMHIDN LVFKVLDSCQ KHEASRFSCS TSDVLSCIMH VINKGCVRRN
EDNPHIVEFL PEDPSTPQKG QAQFSFSRTE IRKDAADSVA DISLMSAPRQ FEDGVLDAVL
FSMGRTMTQE EVRQLMQRTV QQVSGTLSLD LDRAEHLLVH CKWNVDLLVQ RYTDDPDTLI
MAAGLKFRNP QPPPSPASTC PVCLGPRTAA TEPVPSLSCM HYCCQSCWQE YLTARIEQNL
VMNCNCPITD CQAQPTSLFF LSILTDKDTI AKYENALLRG YVECCSNLTW CTNPQGCDQI
LCKENMGSMG TCSKCCWSSC FSCNFPEAHY PASCSHMSQW MDDGGYYEGM SMEAQSKHLA
KLISKRCPSC QAQIEKNEGC LHMTCAKCNH GFCWRCLKPW KPTHKDYYNC SAMVSKAARQ
EKKFQDYNER CTFHHQAKDF AVNLENKVSS INEALQMKSL TFVIDACKVL AQARKVLAYS
CVYSYYNQET EKMDVMEQQT EALDLHTNAL QILLEETLLQ CTDLASCVRL LKPEHLNTGL
ELIRRIQERL LAILQHSTQD FRVGYQSKSS QEPESTQASN LSNNTDANKV SKSERASDSG
DSDNNNNTGE EGAEEAEDED DEYDEEYVPE WHEDYDEDDI DEDDFFSDDD ESENLERDFS
PFD
//
