ID D2GXS2_AILME Unreviewed; 708 AA.
AC D2GXS2;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=F-box domain-containing protein {ECO:0000259|PROSITE:PS50181};
DE Flags: Fragment;
GN ORFNames=PANDA_001725 {ECO:0000313|EMBL:EFB26544.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB26544.1};
RN [1] {ECO:0000313|EMBL:EFB26544.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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DR EMBL; GL192370; EFB26544.1; -; Genomic_DNA.
DR RefSeq; XP_011233906.1; XM_011235604.2.
DR RefSeq; XP_019664458.1; XM_019808899.1.
DR AlphaFoldDB; D2GXS2; -.
DR STRING; 9646.ENSAMEP00000019491; -.
DR GeneID; 100467393; -.
DR KEGG; aml:100467393; -.
DR CTD; 55294; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_7_1; -.
DR InParanoid; D2GXS2; -.
DR OMA; AMVPWED; -.
DR OrthoDB; 587035at2759; -.
DR TreeFam; TF101074; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0030332; F:cyclin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0050816; F:phosphothreonine residue binding; IEA:Ensembl.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:2001205; P:negative regulation of osteoclast development; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:1903378; P:positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR GO; GO:0090049; P:regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR GO; GO:1901524; P:regulation of mitophagy; IEA:Ensembl.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR CDD; cd22133; F-box_FBXW7; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19849:SF1; F-BOX_WD REPEAT-CONTAINING PROTEIN 7; 1.
DR PANTHER; PTHR19849; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 6.
PE 4: Predicted;
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 279..325
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 392..417
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 418..457
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 458..497
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 498..537
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 538..577
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 578..617
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 621..660
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..131
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 708
FT /evidence="ECO:0000313|EMBL:EFB26544.1"
SQ SEQUENCE 708 AA; 79833 MW; D9A24E45FAE475F1 CRC64;
MNQELLSVGS KRRRTGGSLR GNPSSSQADE EQMNRVVEEE QQQQQQLRQE EEHTARNGEV
VGAEPRPGDQ NDSQQAQLEE NNNRFISVDE DSSGNQEEQE EDEEHAGEQD EEDEEEEEMD
QESDDFDQSD DSSREDEHTH SNSVTNSTSI VDLPIHQLSS PFYTKTTKMK RKLDHGSEVR
SFSLGKKPCK VSEYTSTTGL VPCSATPTTF GDLRAANGQG QQRRRITSVQ PPSGLQEWLK
MFQSWSGPEK LLALDELIDS CEPTQVKHMM QVIEPQFQRD FISLLPKELA LYVLSFLEPK
DLLQAAQTCR YWRILAEDNL LWREKCKEEG IDEPLHIKRR KVIKPGFIHS PWKSAYIRQH
RIDTNWRRGE LKSPKVLKGH DDHVITCLQF CGNRIVSGSD DNTLKVWSAV TGKCLRTLVG
HTGGVWSSQM RDNIIISGST DRTLKVWNAE TGECIYTLYG HTSTVRCMHL HEKRVVSGSR
DATLRVWDIE TGQCLHVLMG HVAAVRCVQY DGRRVVSGAY DFMVKVWDPE TETCLHTLQG
HTNRVYSLQF DGIHVVSGSL DTSIRVWDVE TGNCIHTLTG HQSLTSGMEL KDNILVSGNA
DSTVKIWDIK TGQCLQTLQG PNKHQSAVTC LQFNKNFVIT SSDDGTVKLW DLKTGEFIRN
LVTLESGGSG GVVWRIRASN TKLVCAVGSR NGTEETKLLV LDFDVDMK
//
