ID SKR1_CAEEL Reviewed; 176 AA. AC G5ECU1; Q8WSZ9; DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot. DT 14-DEC-2011, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Skp1-related protein {ECO:0000312|WormBase:F46A9.5}; GN Name=skr-1 {ECO:0000312|WormBase:F46A9.5}; GN ORFNames=F46A9.5 {ECO:0000312|WormBase:F46A9.5}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940}; RN [1] {ECO:0000312|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] {ECO:0000312|EMBL:AAL34093.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-176, FUNCTION, INTERACTION WITH CUL-1, AND RP DISRUPTION PHENOTYPE. RX PubMed=11864567; DOI=10.1016/s0960-9822(02)00682-6; RA Nayak S., Santiago F.E., Jin H., Lin D., Schedl T., Kipreos E.T.; RT "The Caenorhabditis elegans Skp1-related gene family: diverse functions in RT cell proliferation, morphogenesis, and meiosis."; RL Curr. Biol. 12:277-287(2002). RN [3] {ECO:0000305} RP FUNCTION, INTERACTION WITH CUL-1 AND MEC-15, TISSUE SPECIFICITY, AND RP DISRUPTION PHENOTYPE. RX PubMed=11864566; DOI=10.1016/s0960-9822(02)00657-7; RA Yamanaka A., Yada M., Imaki H., Koga M., Ohshima Y., Nakayama K.; RT "Multiple Skp1-related proteins in Caenorhabditis elegans: diverse patterns RT of interaction with Cullins and F-box proteins."; RL Curr. Biol. 12:267-275(2002). RN [4] {ECO:0000305} RP INTERACTION WITH DRE-1. RX PubMed=17336909; DOI=10.1016/j.devcel.2007.01.018; RA Fielenbach N., Guardavaccaro D., Neubert K., Chan T., Li D., Feng Q., RA Hutter H., Pagano M., Antebi A.; RT "DRE-1: an evolutionarily conserved F box protein that regulates C. elegans RT developmental age."; RL Dev. Cell 12:443-455(2007). RN [5] {ECO:0000305} RP FUNCTION, INTERACTION WITH SYG-1, AND DISRUPTION PHENOTYPE. RX PubMed=17626846; DOI=10.1126/science.1145727; RA Ding M., Chao D., Wang G., Shen K.; RT "Spatial regulation of an E3 ubiquitin ligase directs selective synapse RT elimination."; RL Science 317:947-951(2007). RN [6] {ECO:0000305} RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=18340346; DOI=10.1038/cdd.2008.30; RA Gao M.X., Liao E.H., Yu B., Wang Y., Zhen M., Derry W.B.; RT "The SCF FSN-1 ubiquitin ligase controls germline apoptosis through CEP- RT 1/p53 in C. elegans."; RL Cell Death Differ. 15:1054-1062(2008). RN [7] {ECO:0000305} RP FUNCTION, INTERACTION WITH SEL-10, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF RP MET-140. RX PubMed=18718460; DOI=10.1016/j.ydbio.2008.07.035; RA Killian D.J., Harvey E., Johnson P., Otori M., Mitani S., Xue D.; RT "SKR-1, a homolog of Skp1 and a member of the SCF(SEL-10) complex, RT regulates sex-determination and LIN-12/Notch signaling in C. elegans."; RL Dev. Biol. 322:322-331(2008). CC -!- FUNCTION: Probable essential component of SCF (SKP1-CUL1-F-box protein) CC E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination CC and subsequent proteasomal degradation of target proteins CC (PubMed:17626846). Regulates cell proliferation during embryonic and CC larval development (PubMed:11864567, PubMed:11864566). Involved in CC synapse elimination in early synapse development (PubMed:17626846). May CC negatively regulate the apoptotic activity of cep-1 in response to CC genotoxic stress (PubMed:18340346). Plays a role in sex determination CC (PubMed:18718460). {ECO:0000269|PubMed:11864566, CC ECO:0000269|PubMed:11864567, ECO:0000269|PubMed:17626846, CC ECO:0000269|PubMed:18340346, ECO:0000269|PubMed:18718460}. CC -!- SUBUNIT: Probable component of the SCF(sel-10) E3 ubiquitin-protein CC ligase complex containing F-box domain-containing protein sel-10 as the CC substrate recognition component (PubMed:17626846). Interacts with cul-1 CC (PubMed:11864567, PubMed:11864566). May interact with the F-box protein CC mec-15 (PubMed:11864566). Interacts with dre-1 (PubMed:17336909). CC Interacts with syg-1 (PubMed:17626846). Interacts with sel-10 CC (PubMed:18718460). {ECO:0000250|UniProtKB:P63208, CC ECO:0000269|PubMed:11864566, ECO:0000269|PubMed:11864567, CC ECO:0000269|PubMed:17336909, ECO:0000269|PubMed:17626846, CC ECO:0000269|PubMed:18718460}. CC -!- INTERACTION: CC G5ECU1; Q17962: CELE_C14B1.3; NbExp=3; IntAct=EBI-323117, EBI-2003707; CC G5ECU1; Q94251: dre-1; NbExp=3; IntAct=EBI-323117, EBI-314286; CC G5ECU1; G5EDX9: fbxa-101; NbExp=4; IntAct=EBI-323117, EBI-2003730; CC G5ECU1; O17198: fbxa-164; NbExp=4; IntAct=EBI-323117, EBI-2412975; CC G5ECU1; O16525: fbxa-196; NbExp=5; IntAct=EBI-323117, EBI-329491; CC G5ECU1; Q2YS43: fog-2; NbExp=4; IntAct=EBI-323117, EBI-2417735; CC G5ECU1; Q18223: fsn-1; NbExp=4; IntAct=EBI-323117, EBI-2003744; CC G5ECU1; Q93794: sel-10; NbExp=5; IntAct=EBI-323117, EBI-323098; CC G5ECU1; P91305: xrep-4; NbExp=3; IntAct=EBI-323117, EBI-2003766; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in the adult. CC {ECO:0000269|PubMed:11864566}. CC -!- DISRUPTION PHENOTYPE: The majority of animals are either embryonic or CC larval lethal. Rare surviving animals develop into uncoordinated CC sterile adults with hyperplasia of tissues including the uterus and the CC spermatheca of the somatic gonad (PubMed:18718460). RNAi-mediated CC knockdown results in a reduction in brood size of the injected parent CC and embryonic lethality of offspring between gastrulation and the two- CC cell phase of embryogenesis (PubMed:11864566). RNAi-mediated knockdown CC causes synapse clusters that are retained rather than eliminated in the CC secondary synapse region, anterior to the vulva during synapse CC development (PubMed:17626846). RNAi-mediated knockdown leads to an CC increase in germ cell apoptosis in response to genotoxic stress CC (PubMed:18340346). RNAi-mediated knockdown within 16 hours of RNAi CC administration results in defects in embryonic divisions including CC spindle mispositioning, abnormal polar bodies and ectopic furrows, and CC hyperplasia of the somatic gonad and hypodermis in larvae CC (PubMed:11864567). All embryos laid 16 hours post RNAi treatment arrest CC and contain almost twice the number of cells as wild-type embryos CC (PubMed:11864567). Zygotic RNAi-mediated knockdown results in 90% CC sterility (PubMed:11864567). {ECO:0000269|PubMed:11864566, CC ECO:0000269|PubMed:11864567, ECO:0000269|PubMed:17626846, CC ECO:0000269|PubMed:18340346, ECO:0000269|PubMed:18718460}. CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284601; CAB03110.1; -; Genomic_DNA. DR EMBL; AF440505; AAL34093.1; -; mRNA. DR PIR; T21573; T21573. DR RefSeq; NP_492513.1; NM_060112.5. DR AlphaFoldDB; G5ECU1; -. DR SMR; G5ECU1; -. DR ComplexPortal; CPX-958; SCF-rpm-1 ubiquitin ligase complex. DR IntAct; G5ECU1; 20. DR MINT; G5ECU1; -. DR STRING; 6239.F46A9.5.4; -. DR EPD; G5ECU1; -. DR PaxDb; 6239-F46A9-5-3; -. DR PeptideAtlas; G5ECU1; -. DR EnsemblMetazoa; F46A9.5.1; F46A9.5.1; WBGene00004807. DR GeneID; 172775; -. DR KEGG; cel:CELE_F46A9.5; -. DR UCSC; F46A9.5.1; c. elegans. DR AGR; WB:WBGene00004807; -. DR WormBase; F46A9.5; CE10580; WBGene00004807; skr-1. DR eggNOG; KOG1724; Eukaryota. DR GeneTree; ENSGT00390000012652; -. DR HOGENOM; CLU_059252_4_0_1; -. DR InParanoid; G5ECU1; -. DR OMA; MREIEKP; -. DR OrthoDB; 1017722at2759; -. DR PhylomeDB; G5ECU1; -. DR Reactome; R-CEL-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-CEL-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-CEL-68949; Orc1 removal from chromatin. DR Reactome; R-CEL-69231; Cyclin D associated events in G1. DR Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity. DR Reactome; R-CEL-8951664; Neddylation. DR Reactome; R-CEL-917937; Iron uptake and transport. DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2. DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; G5ECU1; -. DR PRO; PR:G5ECU1; -. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00004807; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal. DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central. DR GO; GO:0046660; P:female sex differentiation; IGI:UniProtKB. DR GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:UniProtKB. DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IGI:WormBase. DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:UniProtKB. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:WormBase. DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB. DR GO; GO:0090128; P:regulation of synapse maturation; NAS:ComplexPortal. DR GO; GO:1905806; P:regulation of synapse pruning; IDA:SynGO. DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; NAS:ComplexPortal. DR CDD; cd18322; BTB_POZ_SKP1; 1. DR InterPro; IPR016897; SKP1. DR InterPro; IPR001232; SKP1-like. DR InterPro; IPR036296; SKP1-like_dim_sf. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR016072; Skp1_comp_dimer. DR InterPro; IPR016073; Skp1_comp_POZ. DR PANTHER; PTHR11165:SF24; S-PHASE KINASE-ASSOCIATED PROTEIN 1; 1. DR PANTHER; PTHR11165; SKP1; 1. DR Pfam; PF01466; Skp1; 1. DR Pfam; PF03931; Skp1_POZ; 1. DR PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1. DR SMART; SM00512; Skp1; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR SUPFAM; SSF81382; Skp1 dimerisation domain-like; 1. PE 1: Evidence at protein level; KW Developmental protein; Neurogenesis; Reference proteome; KW Ubl conjugation pathway. FT CHAIN 1..176 FT /note="Skp1-related protein" FT /evidence="ECO:0000305" FT /id="PRO_0000433874" FT MUTAGEN 140 FT /note="M->I: In sm151; weak loss of function mutation, does FT not bind to sel-10 protein." FT /evidence="ECO:0000269|PubMed:18718460" SQ SEQUENCE 176 AA; 20032 MW; 3FCDC4D52BC2DF35 CRC64; MADQKKVSEA AKEREIKISS SDNEIFLVPR NVIRLSNTIN TLLMDLGLDD EEGTNAEPIP VQNVTASILK KVISWCNHHH SDPISTEDSD NREKRTDDIG SWDVEFLKVD QGTLFELILA ANYLDIKGLL DVTCKTVANM IKGKSPEEIR RTFNIKNDFT PEEEEQIRKE NAWCED //