CDH1_DICDI
ID CDH1_DICDI Reviewed; 754 AA.
AC Q54KM3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Anaphase-promoting complex subunit cdh1;
GN Name=cdh1; ORFNames=DDB_G0287259;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex
CC that controls progression through mitosis and the G1 phase of the cell
CC cycle. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The APC/C is composed of at least 13 subunits that stay
CC tightly associated throughout the cell cycle: anapc1, anapc2, anapc3,
CC anapc4, anapc5, anapc6, anapc7, anapc8, anapc10, anapc11, cdc20, cdc26
CC and cdh1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
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DR EMBL; AAFI02000099; EAL63831.1; -; Genomic_DNA.
DR RefSeq; XP_637334.1; XM_632242.1.
DR AlphaFoldDB; Q54KM3; -.
DR SMR; Q54KM3; -.
DR STRING; 44689.DDB0266709; -.
DR PaxDb; Q54KM3; -.
DR EnsemblProtists; EAL63831; EAL63831; DDB_G0287259.
DR GeneID; 8626032; -.
DR KEGG; ddi:DDB_G0287259; -.
DR dictyBase; DDB_G0287259; cdh1.
DR eggNOG; KOG0305; Eukaryota.
DR HOGENOM; CLU_014831_4_1_1; -.
DR InParanoid; Q54KM3; -.
DR OMA; RHEICGL; -.
DR Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-DDI-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-DDI-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DDI-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q54KM3; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IBA:GO_Central.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IBA:GO_Central.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR033010; Cdc20/Fizzy.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19918; PTHR19918; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..754
FT /note="Anaphase-promoting complex subunit cdh1"
FT /id="PRO_0000328535"
FT REPEAT 411..448
FT /note="WD 1"
FT REPEAT 452..492
FT /note="WD 2"
FT REPEAT 495..532
FT /note="WD 3"
FT REPEAT 537..576
FT /note="WD 4"
FT REPEAT 610..652
FT /note="WD 5"
FT REPEAT 654..695
FT /note="WD 6"
FT REPEAT 698..737
FT /note="WD 7"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 83786 MW; B8951C9C416777BA CRC64;
MFHSEYEKKL RSPSKSPGSK TNYYNNYSNN NNNTPIPLPL SIFHSTYEDN GSNNNNNNNN
NNINLNSNNN NNNSNNSGSN INNNITTPIK STSTTTTTTT TPITTPTTTT TTTTTTPSYD
SYGDRFIPLS IGLESQNNYS FDESSYEYLY CYPSENSYTI DKQRDESHLA YNIVLKNELL
GSSLSSNFFD SPSSIYKSSI FNNNNNNNNN NNNNNNNNNN NNNNNHVNNN NNNNNNNNID
TPTNNNNNNN NNNNNNNVNI NDTTATTTTT TTTNTNIPTT TTNATNNNNN NSNNTTTTTT
TTTNTTNTTN TNTNTNTNNN LININQSPSK KQSLMSATMN NNNSNNNNNN NFGILKYNQK
QKSTMSNHLD CSPYSLSLLS DDSQKLLSSP RKPQRKISKT PIKILDAPMI KDDFYLNLID
WSSHNILAVG LDTSVYLWNA TTSQVSKLCE MESGQPVSSV GWIQRGGIHL AIGGTDGVVS
IWDVNKKKKI RELQGHNTRV NALAWNNHIL SSGGKDKVIL HHDVRDCSNN YTNRLVGHRH
EICGLKWSPD GQQLASGGND NLLNVWDHSM TQQPQQQHQP PPPPPSSNTS SISQQQQQQN
TSKPLYQFKF HYAAVKAIAW SPHQRGLLAS GGGTHDKCIR FWNTTTGQSI QSIDTGSQVC
NLAWSKNINE LVSTHGYSQN QITVWNYPTM TPVTTLTGHT MRVLYLAVSP DGQTVCTGAG
DNSLRFWNLF PSNKESSFSS NLDSFYNKKG LDIR
