ID A0A341D4X8_NEOAA Unreviewed; 2552 AA.
AC A0A341D4X8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 18-JUN-2025, entry version 33.
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|RefSeq:XP_024621745.1};
OS Neophocaena asiaeorientalis asiaeorientalis (Yangtze finless porpoise)
OS (Neophocaena phocaenoides subsp. asiaeorientalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Phocoenidae; Neophocaena.
OX NCBI_TaxID=1706337 {ECO:0000313|Proteomes:UP000252040, ECO:0000313|RefSeq:XP_024621745.1};
RN [1] {ECO:0000313|RefSeq:XP_024621745.1}
RP IDENTIFICATION.
RC TISSUE=Meat {ECO:0000313|RefSeq:XP_024621745.1};
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_024621745.1; XM_024765977.1.
DR FunCoup; A0A341D4X8; 1141.
DR STRING; 1706337.A0A341D4X8; -.
DR GeneID; 112413842; -.
DR KEGG; nasi:112413842; -.
DR InParanoid; A0A341D4X8; -.
DR Proteomes; UP000252040; Unplaced.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
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; 1.10.10.10: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; 3.30.230.130:FF:000009; 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; 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; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000252040};
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 1146..1325
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 1547..1844
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT DOMAIN 2099..2316
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2103..2150
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 2269..2312
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 84..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2466..2552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..595
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1446
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1677
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2482..2493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2495..2532
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2542..2552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2552 AA; 284262 MW; 9FDF615B8D78E557 CRC64;
MVGERRPGDL MVPLGPRLQA YPEELLRQRP GHDGRPEYLI RWSVLKCEEV GRVGVEEGKA
EHILMWLSAP EVYANCPMLL GERALPKGPQ HETAGGSGSF PRDPGGLDDV AMGEMEADVR
ALVRRAARQL AEGGTSSLTA AVLHTIHVLS AYASIGPLTG VFRETGALDL LMHMLCNPEP
QIRRSAGKML QALAAHDAGS RAHVLLSLSQ QDGIEQHMDF DSRYTLLELF AETTSSEEHC
MAFEGIHLPQ IPGKLLFSLV KRYLCVTSLL DQLNNSPEPG TGDRGSRPSR EDFGREKIRG
QRELEFSMAV GNLISELVRN MGWARNLSEQ AASPPRPTRS IFQPGISGPS LLLPTNVATP
RRQGRAFRQR AGFSSRSGYG EYVQQTLQPG MRVRMLDDYE EISAGDEGEF RQSNNGVPPV
QVFWQSTGRT YWVHWHMLEI LGPEETAEDM ASAAVEKGAG TAVLGTALPS WDWKPVDGLY
SLPYLQPEPQ KNEELGYLTQ AEWWELLFFI KKLDVCEQQP IFQNLRENLD ETLGEKALGE
ISVPIAMAEG LLQVLSNRFE GSTLSDLLNS QIYTKYGLPP KALSSSSSSR SHSSSPVLEE
ESKSEANFSE EEAESPKAKP LKLEAEPARG KTEPPMAQSD SQLFNQLLVT EGIALPAEMK
EAASEMARAL RGPGPRSSLD QHVAAVVATV QISSLDTDLQ LSGLYALSQA VEEVTERDHP
LVSPDRSLRE KLVKTLVELL TNQVGEKMVV VLALRLLYLL MTKHEWRPLF AREGGIYAVL
VCMQEYKTSV LVQQAGLAAL KMLAIASSSE IPTLVAGRDS IHPLFDAQMT REIFASIDSA
TRPGAESLLL AVPAAVILML NTEGCSSAVR NGLLLLNLLL CNHHTLGDQI ITRELRDTLF
RHSGIAPGTE AMPTTRTILT MLLNRYSEPP GSPEHAAALE TPGTQGQDGS PELLIRSLVG
GPSAELLLDL ERVLCREGSP GGAVRPLLKR LQQESQPFLL FLRTLDAPGP NKTLLLTALR
VMTRLLDHPE AMVLPWHEVL EPCLNCLSGP SSDLEIVQEL LCFLYRLASM HKDYAVVLCC
LGAKEALAKV LDKHPAQLLL ACELRDLVTE CEKHAQLYSN LTSSILAGCI QMVLGQIEDH
RRTHRPINIP FFDVFLRHLC QGSSVEVKED KCWEKVEVSS NPHRASKLTD RNPKTYWESN
GSTGSHYITL HMHRGVLVRQ LTLLVASEDS SYMPARVVVF GGDSVSCIST ELNTVNVMPS
ASRVVLLENL NRFWPVIQIR IKRCQQGGID TRVRGVEVLG PKPTFWPLFR EQLCRRTCLF
YTIRAQAWSR DIAEDRKRLL QLCPRLNRVL RHEQNFADRF LPDDEAAQAL GKTCWEALVS
PLVQNITSPD VEGVSSLGWL LDQYLEQRES SRNPLSRAAA FASRVRRLCH LLVHVEPPPG
PSPEPSTRPF SKNSKGQDRS PGPSPVLPSS SLRNITQCWL SVVQEQVSRF LAAAWRAPDF
VPRYCKLYGR LQRAGSELFG PRAAFMLALR SGFSGALLQQ SFLTAAHMSE QFARHIDQQI
QGGLMGGTSG VEMLGRLQWH LEPIMVLSGL ELATTFEHFY QHYMADRLLS VGSSWLEGAV
LEQIGPCFPN RLPQQMLRSL STSEELQRQF HVYQLQQLDK LLLEQEDEEE QGLEEEEVRA
RERVGEQGKT RPKKGAQEPL NPSVSQEEEE EEKAEKELFI EDPSPTVSVL VLSPRCWPVS
PLCYLYHPRK CLPTEFCDAL DRFSNFYNQS QNHPVLDMGP HRRLQWTWLG RAELQFGDQT
LHVSTVQMWL LLNFNQTEEV SVEALLKNSD LSPKLLLQAL LPLTADSGPL TLQEGQDFPC
GGVLQLREPG LWPQGEALWL LPPQTYLNVE KDEGQTLEQK RNLLSCLLVR ILKAHGEKGL
HIDQLVCLVL EAWQKGPNPP GSLGRAVAGG VACTSTDVLS CILHLLGQGY VERRDDRPQI
LMYASPEPMG PCRGQAEVPL CGSQTSETSK PSPEVVAALA SLQLPAGRTM SPQEVEGLME
HTVRQVQETL NLEPDVAQHL LAHSHWGAEQ LLQRYSDNPE PLLLAAGLCV PQAQAAPARP
DHCPVCVSPL EPDDDLPSLC CMHYCCKSCW KEYLTTRIEQ NLVLNCTCPI ADCPAQPTGA
FIRTIISSPE VISKYEKALL RGYVESCANL TWCTNPQGCD RVLCRQGLGC GTSCSKCGWA
SCFNCSFPEA HYPASCGHMS QWVDDGGYYD GMSVEAQSKH LAKLISKRCP SCQAPIEKNE
GCLHMTCAKC NHGFCWRCLK SWKPNHKDYY NCSAMVSKAA RQEKRFQDYN ERCTFHHQAR
DFAVNLQNRV SAIHEVPPPR SFTFLSDACR GLEQARKVLA YACVYSFYNQ DTEHMDVVEQ
QTEALELHTN ALQILLEETL LRCRDLGSSL RLLRAEHLST GLELLRRIQE RLLAILQHST
QDFRVGLQSP SSEAREAKGS NVPGSQPQGS SGLQVEEEEE DDDDEDDVPE WQQDEFEEEL
DNDSFSYDEE SENLDRETFF FGDEEEDDEG YD
//
