SKP1B_DICDI
ID SKP1B_DICDI Reviewed; 162 AA.
AC Q557E4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=SCF ubiquitin ligase complex protein SKP1b;
DE AltName: Full=Glycoprotein FP21 isoform B;
DE Contains:
DE RecName: Full=SCF ubiquitin ligase complex protein SKP1b(4-162);
DE Contains:
DE RecName: Full=SCF ubiquitin ligase complex protein SKP1b(6-162);
GN Name=fpaB-1; Synonyms=fp21B, fpa1B, fpa2, skp1B; ORFNames=DDB_G0273251;
GN and
GN Name=fpaB-2; Synonyms=fp21B, fpa1B, fpa2, skp1B; ORFNames=DDB_G0273615;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND CLEAVAGE
RP OF INITIATOR METHIONINE.
RC STRAIN=AX3;
RX PubMed=9373134; DOI=10.1016/s0378-1119(97)00194-7;
RA West C.M., Kozarov E., Teng-Umnuay P.;
RT "The cytosolic glycoprotein FP21 of Dictyostelium discoideum is encoded by
RT two genes resulting in a polymorphism at a single amino acid position.";
RL Gene 200:1-10(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP PROTEIN SEQUENCE OF 4-38.
RX PubMed=1577798; DOI=10.1016/s0021-9258(19)50132-6;
RA Gonzalez-Yanes B., Cicero J.M., Brown R.D. Jr., West C.M.;
RT "Characterization of a cytosolic fucosylation pathway in Dictyostelium.";
RL J. Biol. Chem. 267:9595-9605(1992).
RN [5]
RP HYDROXYLATION AT PRO-143, GLYCOSYLATION AT PRO-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=9660787; DOI=10.1074/jbc.273.29.18242;
RA Teng-umnuay P., Morris H.R., Dell A., Panico M., Paxton T., West C.M.;
RT "The cytoplasmic F-box binding protein SKP1 contains a novel
RT pentasaccharide linked to hydroxyproline in Dictyostelium.";
RL J. Biol. Chem. 273:18242-18249(1998).
RN [6]
RP DEVELOPMENTAL STAGE, GLYCOSYLATION, MUTAGENESIS OF PRO-143, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11358877; DOI=10.1093/glycob/11.4.283;
RA Sassi S., Sweetinburgh M., Erogul J., Zhang P., Teng-Umnuay P., West C.M.;
RT "Analysis of Skp1 glycosylation and nuclear enrichment in Dictyostelium.";
RL Glycobiology 11:283-295(2001).
RN [7]
RP GLYCOSYLATION.
RX PubMed=11886837; DOI=10.1093/glycob/12.2.17r;
RA West C.M., van der Wel H., Gaucher E.A.;
RT "Complex glycosylation of Skp1 in Dictyostelium: implications for the
RT modification of other eukaryotic cytoplasmic and nuclear proteins.";
RL Glycobiology 12:17R-27R(2002).
RN [8]
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, HYDROXYLATION AT
RP PRO-143, GLYCOSYLATION AT PRO-143, AND MASS SPECTROMETRY.
RX PubMed=12244067; DOI=10.1074/jbc.m208824200;
RA Van Der Wel H., Fisher S.Z., West C.M.;
RT "A bifunctional diglycosyltransferase forms the Fucalpha1,2Galbeta1,3-
RT disaccharide on Skp1 in the cytoplasm of dictyostelium.";
RL J. Biol. Chem. 277:46527-46534(2002).
RN [9]
RP GLYCOSYLATION BY AGTA.
RX PubMed=15123660; DOI=10.1074/jbc.m313858200;
RA Ketcham C., Wang F., Fisher S.Z., Ercan A., van der Wel H., Locke R.D.,
RA Sirajud-Doulah K., Matta K.L., West C.M.;
RT "Specificity of a soluble UDP-galactose:fucoside alpha1,3-
RT galactosyltransferase that modifies the cytoplasmic glycoprotein Skp1 in
RT Dictyostelium.";
RL J. Biol. Chem. 279:29050-29059(2004).
CC -!- SUBUNIT: Multiprotein complex (SCF) with cullin and F-box-containing
CC protein. Capable of undergoing aggregation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the life cycle.
CC {ECO:0000269|PubMed:11358877}.
CC -!- PTM: O-linked glycan consists of linear Gal-Gal-Fuc-Gal-GlcNAc.
CC -!- PTM: Not glycosylated in prespore cells.
CC -!- PTM: FpaA and fpaB seem to be identically glycosylated. Glycosylation
CC is required for nuclear enrichment.
CC -!- PTM: Hydroxylated by phyA. {ECO:0000269|PubMed:12244067,
CC ECO:0000269|PubMed:9660787}.
CC -!- MASS SPECTROMETRY: [SCF ubiquitin ligase complex protein SKP1b]:
CC Mass=19130; Method=MALDI; Note=The mass corresponds to the peptide with
CC Ser-2 acetylated, Pro-143 hydroxylated and modified by a GlcNAc
CC residue.; Evidence={ECO:0000269|PubMed:12244067};
CC -!- MISCELLANEOUS: There are two genes coding for Skp1, they only differ in
CC a single position in the coding region.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; U73686; AAB88390.1; -; Genomic_DNA.
DR EMBL; AAFI02000011; EAL70498.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL70843.1; -; Genomic_DNA.
DR PIR; A55969; A55969.
DR RefSeq; XP_644424.1; XM_639332.1.
DR RefSeq; XP_644826.1; XM_639734.1.
DR AlphaFoldDB; Q557E4; -.
DR SMR; Q557E4; -.
DR STRING; 44689.DDB0185043; -.
DR iPTMnet; Q557E4; -.
DR PaxDb; Q557E4; -.
DR EnsemblProtists; EAL70498; EAL70498; DDB_G0273615.
DR EnsemblProtists; EAL70843; EAL70843; DDB_G0273251.
DR GeneID; 8618928; -.
DR GeneID; 8619049; -.
DR KEGG; ddi:DDB_G0273251; -.
DR KEGG; ddi:DDB_G0273615; -.
DR dictyBase; DDB_G0273251; fpaB-1.
DR dictyBase; DDB_G0273615; fpaB-2.
DR eggNOG; KOG1724; Eukaryota.
DR HOGENOM; CLU_059252_6_1_1; -.
DR InParanoid; Q557E4; -.
DR OMA; PHEENKE; -.
DR PhylomeDB; Q557E4; -.
DR Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR Reactome; R-DDI-69231; Cyclin D associated events in G1.
DR Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-917937; Iron uptake and transport.
DR Reactome; R-DDI-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q557E4; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0043223; C:cytoplasmic SCF ubiquitin ligase complex; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0097602; F:cullin family protein binding; IPI:dictyBase.
DR GO; GO:1990444; F:F-box domain binding; IPI:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IDA:dictyBase.
DR GO; GO:0071987; F:WD40-repeat domain binding; IPI:dictyBase.
DR GO; GO:0016567; P:protein ubiquitination; TAS:dictyBase.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR Gene3D; 3.30.710.10; -; 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; PTHR11165; 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; SSF54695; 1.
DR SUPFAM; SSF81382; SSF81382; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW Hydroxylation; Nucleus; Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12244067,
FT ECO:0000269|PubMed:9373134"
FT CHAIN 2..162
FT /note="SCF ubiquitin ligase complex protein SKP1b"
FT /id="PRO_0000312588"
FT CHAIN 4..162
FT /note="SCF ubiquitin ligase complex protein SKP1b(4-162)"
FT /id="PRO_0000328246"
FT CHAIN 6..162
FT /note="SCF ubiquitin ligase complex protein SKP1b(6-162)"
FT /id="PRO_0000328247"
FT REGION 100..162
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000305|PubMed:12244067"
FT MOD_RES 143
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12244067,
FT ECO:0000269|PubMed:9660787"
FT CARBOHYD 143
FT /note="O-linked (GlcNAc...) hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12244067,
FT ECO:0000269|PubMed:9660787"
FT MUTAGEN 143
FT /note="P->A: Lack of glycosylation."
FT /evidence="ECO:0000269|PubMed:11358877"
SQ SEQUENCE 162 AA; 18702 MW; 623558D36CEBDBED CRC64;
MSLVKLESSD EKVFEIEKEI ACMSVTIKNM IEDIGESDAP IPLPNVTSTI LEKVLDYCRH
HHQHPSPQGD DKKDEKRLDD IPPYDRDFCK VDQPTLFELI LAANYLDIKP LLDVTCKTVA
NMIRGKTPEE IRKIFNIKND FTPEEEEQIR KENEWCEDKG GN
