ID A0A8C5KHN2_JACJA Unreviewed; 2518 AA.
AC A0A8C5KHN2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=Cullin-9 {ECO:0000256|ARBA:ARBA00069618};
DE AltName: Full=p53-associated parkin-like cytoplasmic protein {ECO:0000256|ARBA:ARBA00077902};
GN Name=Cul9 {ECO:0000313|Ensembl:ENSJJAP00000008844.1};
OS Jaculus jaculus (Lesser Egyptian jerboa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Dipodoidea;
OC Dipodidae; Dipodinae; Jaculus.
OX NCBI_TaxID=51337 {ECO:0000313|Ensembl:ENSJJAP00000008844.1, ECO:0000313|Proteomes:UP000694385};
RN [1] {ECO:0000313|Ensembl:ENSJJAP00000008844.1}
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_004649532.1; XM_004649475.1.
DR Ensembl; ENSJJAT00000015281.1; ENSJJAP00000008844.1; ENSJJAG00000012861.1.
DR GeneID; 101605072; -.
DR CTD; 23113; -.
DR GeneTree; ENSGT00940000153954; -.
DR OMA; KPWKPNH; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000694385; Unassembled WGS sequence.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:Ensembl.
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; 1.10.10.10:FF:000207; Cullin 9; 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; 3.30.40.10:FF:000278; cullin-9 isoform X2; 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; 1.25.10.10; 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; IPR016157; Cullin_CS.
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; 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; 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; PS01256; CULLIN_1; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000694385};
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 1140..1319
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 1536..1804
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT DOMAIN 2059..2276
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2063..2110
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 2229..2272
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 275..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2434..2518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..590
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2441..2451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2454..2498
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2508..2518
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2518 AA; 281310 MW; FBDA07FEDA6CB204 CRC64;
MVGERRSGDL MVPLGPRLQA YPEELIRQRL GHDGRPEYLI RWSVLKCGEE DKVNVEEGKA
EHILMWLSAP EVYANCPMLL HERTVSKGPQ YESARGLGSF SQDPGSLDEL AVAEMEADVR
ALVRRAARQL AEGGTSSLTA AVLHTIHVLS AYASIGPLTG VFRETGALDL LMHMLCHPEP
QVRRSAGKML QALAAHDAGS RAHVLLSLSQ QDGIEQHMDF DSRYTLLELF AETTSSEEHC
MAFEGIHLPQ IPGKLLFSLV KRYLCVTSLL DQLNNSPEPG AGHPDSPSPT KESSRGQREL
EFSMAVGNLI SELVRSMGWA RNLSDQGTAP PRPSRSIFQP CISGPPLLLP NIVTTPRRQG
QAFRQRSEFS SRSGYGDYVQ QTLQPGMRVR ILDDYEEISA GDEGEFRQSN SGVPPVQVFW
QSTGRTYWVH WHMLEILGPE EARGDSVSAS LEKGASVLDT AFSSGDWKPL YGLYSLPYLQ
PEPQKKEDLG YLTQAEWWEL LFFIKKLDLS EQQPIFQNLR EKLDKAMSET ALGEISVPIE
MAEGLLQVLS SRFEGSTLCD LLNSQIYTKY GLLPDELSSL SSSRSGSSTP DPDEESKSAS
SLLEETGSPK AEAEPLKVEA EPAKVKTEPP KAQSDSQLFN QLLVAEGMAL SAETKEAADE
MARALRGPGP RSSLDQHVAA VVATVQMSSS DTHLQLSGLC ALSQAVEEIT EQEHPLVRPD
RPLREKLVKT LVDLLTNQVG EKMVVVLALR LLYLLMTKYE WRPLFAREGG IYAVLICMQE
YKTSVLVQQA GLAALKMLAI ASSSELPAFV TGRDSVQPLF GTQMTREIFA SIDSATRPGS
ESLLLSIPAA VILMLNTEGC SSAVRNGLLL LSLLLCNHHT LGDQIITQEL RDTLFRHSGI
APGTEPMPTT RTILMMLLNR YSEPRGSPER AALETASTPG QDGSPELLIR SLVGDPSAEL
FLDLERVLCR ESSPRGAVSP LLKCLQQESQ PFLLLLRTLD APGPNRTLLL TVLRVMTRLL
DYPETLVLPW HEVLEPCLNC LNGPSSDSEV VQELTCFLHR LALTHKDYAV VLCCLGAKEA
LSKVLDKHST QLLLASELRD LVTECEEYAQ LYSNLTSSIL AGCIQMALGQ IEDHRRTHRP
INIPFFDVFL MHLCQGSSVE VKEDKCWEKV EVSSNPHRAS KLMDRNPKTY WESNGSTGSH
YITLHMRRGV LIRQLTLLVA SEDSSYMPAR VVVFGGDSAR SINTELNTVN VMPSASRVTL
LENLTRFWPI IQIRIKRCQQ GGIDTRVRGV EVLGPKPTFW PLFREQLCRR TCLFYTMWAQ
AWSRDIAEDR RRLLQLCPRL NRVLRHEQNF ADRFLPDDKA AQALGKTCWE ALVSPLVQNI
TSPDAEGVSS LGWLLDQYLE QRESSRIPQS RAAAFCSRVR RLCHLLVHVE PPPGPSEPSS
KNSKGQDRSP VPCPVLPSST LRNITQCWLS VVQEQVSRFL AAAWRAPDLV PRYCKLYEHL
QRAGAELFGP RAAFTLALRT GFSGALLQQS FLTAAHMTEQ FARHIDQQIQ GGLLGGAPGV
EMLGRLQQHL EPIMVLSGLE LATTFEHFYQ HYMADRLLSL GSSWLEGAVL EQIGLCFPNR
LPQLMLRSLS TSEELQRQFH VYRLQQLDRF LLEQEDKEDP GLEEKEEEDE DVEAKKEMFT
EDPSPTVSIL VLSPRCWPVS PLCYLHHPRK CLPTELCDAL DGFATFYSHS QNYPVPGMGP
HRRLQWTWLG RAELQCGDQT LHVSTVQMWL LLSVSRAEEV SVEVLLENSD LAPELLHQAL
LPLTSESGPL ILQEAQDFPH GGVLRLREPT SWPSEKVLWL IPPQTYLSVE KDEGRTLEQK
RNLLSCLLVR ILKAHGEKGL HIDQLVCLVL EAWQKGPDPP GSLGRTVAGG VLCTTTDVLS
CILHLLGQGY VERRDDRPQI LVYGTPEPMG PCRGQADIPF CGNQNTEMYK PSPEAVAALA
SLQLPAGRTM SPQEVEGLME QTVRQVQETL NVEPDVAQHL LAHSHWGAEQ LLQSYSDKPE
PLLLAAGLRV PEAQAVPLRP DHCPVCVSPL EPEDDLPSLC CMHYCCKSCW NEYLTTRIEQ
NLVLNCTCPI ADCPAQPTGA FIRAIVSSPE VISKYEKALL RGYVESCSNL TWCTNPQGCD
RILCRQGLSC GTTCSKCGWA SCFSCSFPEA HYPASCGHMS QWVDDGGYYD GMSVEAQSKH
LAKLISKRCP SCQAPIEKNE GCLHMTCAKC NHGFCWRCLK SWKPNHKDYY NCSAMVSKAA
RQEKRFQDYN ERCTFHHQAR EFAVNLRNQA AAIHEVPPPK SFTFLHDACR ALEQARKVLA
YACVYSFYSQ DTEYMDVVEQ QTENLELHTN ALQILLEETL LRCEDLASSL RLLRADCLST
GMELLRRIQE RLLAILQHST QDFRVGLQSP SVEAQEAKAS NMPSNQIQGS SGLEAEEEEE
EEEEEEEEEE DEEDAPAWQQ EFDEELDNDT FSYDEESENL DRETFFFGDE DDDDESYD
//
