ID A0A8C6VFI3_NAJNA Unreviewed; 2147 AA.
AC A0A8C6VFI3;
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 7 {ECO:0008006|Google:ProtNLM};
OS Naja naja (Indian cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=35670 {ECO:0000313|Ensembl:ENSNNAP00000003537.1, ECO:0000313|Proteomes:UP000694559};
RN [1] {ECO:0000313|Ensembl:ENSNNAP00000003537.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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 Ensembl; ENSNNAT00000003712.1; ENSNNAP00000003537.1; ENSNNAG00000002200.1.
DR GeneTree; ENSGT00940000153954; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000694559; 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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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 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; 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; 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; 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 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; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000694559};
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 879..1058
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 1272..1529
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT DOMAIN 1754..1971
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1758..1805
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1924..1967
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 1379..1417
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2147 AA; 245366 MW; 72D31060A799BBED CRC64;
MVGEKRNGNL GPKLQAYAEE LIRQRRGHDG RTEYLIRWSI LSLDDNVENT THAASTENKM
DNILMWMSAE EVYANCPTLL GKRKPEGQRV KEEKSPSTFP SDVTVDEASL HEMKADVRSL
VQRANRQMAR TSGPESSILN TVHVLSAYAS IGSLTGVFKE TGALDLLMKM LCNEEKQIRR
SAGKMLRALA SHDAGSRAYV LLSLSQQDGI EQHMDFDSRY TLLELFAETT SSEEHCMSFE
GIHLPQIPGK LLFSLVKRYL CVTSLMDKLN STTELGGDHQ DSSAPSSTFG EKSRAQREFD
FSMAMANLIS ELVRVMGWDR SQERELLSLT NAQPRIIRSI FQPKGSTCTA VQVPLVTSKP
SPRKKESLPF MTLSDFSSRS SYVEYVQESL KPGMTVRMLE EYEEIDAGDE GEFRQSNSGM
PPVQVLWQST GQTYWVHWHM IEIIGSREQN EEDACVERDR GATQTFYCKP LGGLYCLPYL
VDQLYENSGM LNRAEWWELL FFIKKLEQHE QQEIVQFIQR NHEEQGLIQL SISVELARKL
LPLLSKYCQG CTQNDLQNSH IYLKYTLSKG SSEQDCQSVD MTSAKDSGFS EAMAFKNQRN
PFLLKCLLQC CLQQRRLTHT FLFSLGKTRG STWDFICSAI YKVTTIDFKS FFVLLREKMV
KMLVELLSNQ LKEKLLMVTA LRLLYVLMAK YDWRILFATE GGVRAVLGCM QEYSTSALIL
QAGLAALKVL VGAGNCELIG TSGKSYPLNH SDAQMMREIF ASIGSASSKE SDNLLCVICI
ILLSFYQQVV QEFIRFLHRL ATTNKDCAVV MCRVGTKEAL TKAMDKHNSN LLLVTELRDL
VTDCEKYASL YKKMTTSILA GCIQMVLGQI EEHRRSHQPI NIPFFDVFLR NLCQGSNVEV
KEDKCWERIE VSSNPHRANK LTDKNPKTYW ESNGSTGSHY INVYIHRGVV VRQMTLIVAS
EDSSYMPARI VVMGGENTSS ITNELNTVNV LPTANRVVLL ENMGRFWPII QIKIKRCQQG
GIDTRVRGIE VLGPKPTFWP IFKEQLCRRT YLFYTTKAHT WCQEILEDRM QLLQLFNRLN
SALRHEQVFA NRFLPDDEAA QALGKTCWEA LITPLVQSIT SPDSSGISPM SWLLTQYLEN
LHAARNSMSR ASIFNSRVRR LSHLLVHVDS AGPELEELKP PIKTSESLYP RNLPSYNKKV
EMCLCLFSVV QVKCFLESSW QAPDFVEQYC RTYQRLRTAM EELFGQQISF MLALCHGFSG
ALLQLSFLTA MHVSEQFARY IDRWIQQSWA DSGNVETFQC LQQSLEPVLF LADLELANTF
ERFYRYYLGD RLLSQGKTWL ESSVVDHIGI CFPNRFPQQM LKNLSDMEEQ QQQFHLFQLQ
QLDKHLLELD QQGNQEEEEE EEENEEEEAE VKVLALSPRC WTISPLCYLE DPARFFPSSL
TFSVFLSDFF SSLLGRSHFG MEHTKPQRLQ WTWLGHAELK YQGYILQVST LQMYILLCFN
HAEEVSVETL LEVTGLSPVL LSHALKPLTK ENGILTQRQS LLRLNEGTLC QASGQRLWLL
PKQMYLNVEE NEGCALEKKR NTICCLLVQI LKAEKEMHID NLVFKVWNSR KFLNFCCSST
DVLSCILHLL SQGYIQRQED NPHILEYISA DPTTPHRGQA QLDTFGLDTE QVLMETVLLP
MGRTMNQEEV ELLMTQTVEK VSDTLSVTAD IAQHLLIHCK WNVDVLIQRY TEDQESMLFF
SGLQVRNPQP PSSPVTQCPV CVNPLSETDD LPLLCCMHYC CKSCWNEYLT TRIEQNLILN
CTCPISDCPA QPTTAFIRSI ISSKEVIAKY EKALLRGYVE CCSNLTWCTN PQGCDQILCK
EGLCYGEACS KCSWISCFSC NFPEAHYPAS CSHMSQWMDD GGFYEGMTVE AQSKHLAKLI
SKRCPSCQAQ IEKNEGCLHM TCAKCNHGFC WRCLKPWKPT HKDYYNCSAM VSKAARQEKR
FQDYNERCIF HHKAKEFAMN LRSRVSTVSD MPQIRTLTFV VDACKVLEQA RKVLAYSCIY
SYYNQDTEKM DIMEQQSENL ELHTNALQIL LEEMLLYCQD LASSIRLLKA KHFNIGLELV
RRIQERLLSI LHHATQDFRV GFQTRQSSEQ GGIKLSNVLN GTSAYKQ
//
