ID A0A1S3RYY6_SALSA Unreviewed; 2528 AA.
AC A0A1S3RYY6;
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-like isoform X5 {ECO:0000313|RefSeq:XP_014057443.1};
GN Name=LOC106605930 {ECO:0000313|RefSeq:XP_014057443.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014057443.1};
RN [1] {ECO:0000313|Proteomes:UP000087266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=double haploid {ECO:0000313|Proteomes:UP000087266};
RX PubMed=20887641;
RA Davidson W.S., Koop B.F., Jones S.J., Iturra P., Vidal R., Maass A.,
RA Jonassen I., Lien S., Omholt S.W.;
RT "Sequencing the genome of the Atlantic salmon (Salmo salar).";
RL Genome Biol. 11:403-403(2010).
RN [2] {ECO:0000313|RefSeq:XP_014057443.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014057443.1};
RG RefSeq;
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 RefSeq; XP_014057443.1; XM_014201968.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000087266; Chromosome ssa01.
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; 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; 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; 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 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:UP000087266};
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 1188..1367
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 1610..1862
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT DOMAIN 2128..2346
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2299..2342
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 60..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2418..2448
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 60..81
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..684
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..709
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2528 AA; 282750 MW; 3D357C587155CDDD CRC64;
MRQSVAIMVG ERRNGNLLVQ LGTKLQAYPE ELIRQRRTHD GQTEYLIRWC LLAIDDGSGS
GGGSNEAGGG GGSSSGVGGS SGSTSGESKT ENILMWMSTE DVYANCPTLL GKRKADTQRP
LQEEERPSGE FPADVTFDEV ELSDMKDDVK NLVTRARKQM AKKSDFAISI THTIHVLSAY
ASIGSLVGVF KETGALDLLM ELLCNKERQT RRSAGKMLRA LASHDAGSRA YVLLSLSQQD
GIEQHMDFDN RYTLLELFAE TTSSEEHGIS FEGIHLPQIP GKLLFSLVKR YLCVTSLMDK
LNTAGVESSS ERQDAAGSSG TGHQLENLRV QREFEFTMAM ANLISELVRV MGWDRNRQPP
QSAGLAQGSA CGEDQEDEPP RRVVRSIFQP RFSASASASP AAAAASNIAA ATPPKKKTGN
GFKTRTDFAS RSAYVEYVQE NLKSGMLVRM LEDYEEVSAG DEGDFRYSND GSPPVQVYWT
SLSRTYWVHW HMVEILGTGT SGQGEKDAQE KASSLTETIK LTTVSQTLFS KPPGGLYSLP
YLAEGLQSDG ATLSRAEWWE VLFFIKKLEP KQQQEINNIL RQSLDEQMSD VDEATLIQLL
VPGEVARKLL HYLKQTLQNS CLWDLLCSHA FSKHYLRRGG GGLEDDELLP DGSLGSSGLG
GGRSNSSSDA TAAASSSSAM GSLSKKPKKE SPTDYCSDTE SELPMEDESN YPEDLKEKMK
VFNNPKVQGK KTALEKLGEV VDIMKKSGSD PVQQLAGIKF IIQVLEDEGP QERSTLRTDA
VQTIRDKVLK FLVEILSGQP KENVVSTLRL TRALMVKYEW RVSFATEGGV KAILSCMQEY
PTVPQVQQVA LATLMVITGA SKHDLGSMSS CYLPLSESGT PMMLGVFASI GSATAEGSKG
LLAAIPAGIE LMLNTPRCML SVRNGLLVII MLISSSKSLA EQLVACDVSA VLKKCLSASR
PVNMLAIIAL NHISMVHKLE KKESKDELDF KDTELKMLVV SLKEMTATKE VILTLEQLLC
DDASQLEEER NQVTRSRETY QDLVRLMDQH RADRAAQLSI LRILNKFLDN YLEDLLPWHE
SIEPCLSSMT AFINDREVVQ LLIRFLYRLA SVNKDYAVVM CRLGTKDALV KALDKHSINL
LLVTELRDLI TDCEKYASLY KKMTTSVLAG CIQMVLGQIE EHRRSHQPIN IPFFDIFLRN
LCQGSSVELK EDKCWEKVEV SSNHHRANKL TDKNPKTYWE SNGCTGSHFI NIYMHKGVVI
RQLAVLVASE DSSYMPARMV VLGGDDPTNI NTELNTVNVP PSANRIVLLE SITRFWSIVQ
IRIKRCQQGG IDTRVHGFEV LGPKPTFWPV FKEQLCCRTY LFYTTKAHTW CQEILEDKAQ
LLQLFNKLNS ALRHEQMFAD RFLPDAEAAE ALGRTCWEAL ITPIVQSITI SETQVLSPLS
WLLSEYLDNA ESARRCKSRA AIFNSRVRRL THLLVHVDTS RVDTEELKPP IKCKGINRSK
DLKNGKEGKN KDVAAVSSSS SSNSVKPKMK NTSSIAGIAL CWQGVVQRQV KKFLDSTCSL
PDFVERYRNM YLRLKNAMEE LFGQQTAFVL ALRHGFSAAL LQLSILTAMH VSERFAQYID
LMIQESGVDS GNVETLNQLQ QFLEPMLFLS GLELANTFEH FYRYYLGDRL LGQGKVWLES
AVIMQIGTCF PNRFPQQMLK NLSESEELQQ EFHLYRLQQL DKTLQDVDEE MMDDQPSEPE
EESEVKVLIL SPRCWAVSSP CYMDNHSRYF PKQLCTYLAE FTDFYSNSQC MYNLTHSKPR
RLQWTWLGHA ELRYGSCTLY VSTLQMYILL QFNHQADVSV EALQQATGLS PTMLAHALSP
LTAGKGILTQ DSPDNDLVKG VLRLNKKALS QSLENHSYCY LLPKQTYLNV DEDAARSLER
KRNFIYCIII QIMKAEKEMH IDNLVFRVLD TCQKREATRS PGSVRFSCST TDVLSCVMHV
ISKGYIRRNE DSPHIVEFLP EDPSTPQKGQ AHFSFSKAEL KNNPSSSNAD ISLEGIIAAP
PSAEDGVLEA VLLSMGRTMN QEEVRQLMQR TVQQVSGTLS LDLDQAEHLL VHCKWNVDVL
IQRYTDDPDS LVLAAGLKGL NPQPPPSPVA SCPVCLISQS GEAEPAPTLC CMHYCCRSCW
QEYLTARIEQ NLVMNCNCPI TDCRAQPTSQ FFFNILTDKD TIAKYENALL RGYVECCSNL
TWCTNPLGCD QILCKENIGS MGTCSKCCWS SCFSCNFPEA HYPASCSHMS QWMDDGGYYE
GMTMEAQSKH LAKLISKRCP SCQAQIEKNE GCLHMTCAKC NHGFCWRCLK PWKPTHKDYY
NCSAMVSKAA RQEKKFQDYN ERCTFHNQAK DFAINLESKV SSINEALQMK SLTFVIDACK
VLAQARKVLA YSCVYSYYNQ DTEKMDVMEQ QMEALELHTN ALQILLEETL LQCTDLASCV
RLLKPEHLNT GLELIRRIQE RLVAILQHST QQIIRVSSCL VSPNTGLSSG LQLQNRTGTG
ICSSFKSL
//
