CF451_DICDI
ID CF451_DICDI Reviewed; 297 AA.
AC Q86HE5; Q55DG7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Counting factor 45-1;
DE Flags: Precursor;
GN Name=cf45-1; Synonyms=ctnC; ORFNames=DDB_G0269248;
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], DISRUPTION PHENOTYPE, DEVELOPMENTAL
RP STAGE, AND IDENTIFICATION IN THE CF COMPLEX.
RX PubMed=12912898; DOI=10.1128/ec.2.4.788-797.2003;
RA Brock D.A., Hatton R.D., Giurgiutiu D.-V., Scott B., Jang W., Ammann R.,
RA Gomer R.H.;
RT "CF45-1, a secreted protein which participates in Dictyostelium group size
RT regulation.";
RL Eukaryot. Cell 2:788-797(2003).
RN [2]
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 [3]
RP IDENTIFICATION IN THE CF COMPLEX.
RX PubMed=10444594; DOI=10.1101/gad.13.15.1960;
RA Brock D.A., Gomer R.H.;
RT "A cell-counting factor regulating structure size in Dictyostelium.";
RL Genes Dev. 13:1960-1969(1999).
RN [4]
RP IDENTIFICATION IN THE CF COMPLEX.
RX PubMed=12117815; DOI=10.1242/dev.129.15.3657;
RA Brock D.A., Hatton R.D., Giurgiutiu D.-V., Scott B., Ammann R., Gomer R.H.;
RT "The different components of a multisubunit cell number-counting factor
RT have both unique and overlapping functions.";
RL Development 129:3657-3668(2002).
RN [5]
RP IDENTIFICATION IN THE CF COMPLEX.
RX PubMed=16963635; DOI=10.1128/ec.00169-06;
RA Brock D.A., van Egmond W.N., Shamoo Y., Hatton R.D., Gomer R.H.;
RT "A 60-kilodalton protein component of the counting factor complex regulates
RT group size in Dictyostelium discoideum.";
RL Eukaryot. Cell 5:1532-1538(2006).
CC -!- FUNCTION: Cell-counting factor that limits the maximum size of the
CC multicellular structure during aggregation. {ECO:0000250}.
CC -!- SUBUNIT: Monomer (By similarity). Component of the counting factor (CF)
CC complex, which includes cf60, cf50, cf45-1 and ctnA. {ECO:0000250,
CC ECO:0000269|PubMed:10444594, ECO:0000269|PubMed:12117815,
CC ECO:0000269|PubMed:12912898, ECO:0000269|PubMed:16963635}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in vegetative and early developing
CC cells. Increases at 2.5 hours of development, and then decreases
CC slightly. At 10 hours, there is a strong decrease followed by a almost
CC complete decline at 25 hours. {ECO:0000269|PubMed:12912898}.
CC -!- DISRUPTION PHENOTYPE: Formation of large groups.
CC {ECO:0000269|PubMed:12912898}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01252, 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; AY212268; AAO52749.1; -; Genomic_DNA.
DR EMBL; AAFI02000005; EAL71974.1; -; Genomic_DNA.
DR RefSeq; XP_646164.1; XM_641072.1.
DR AlphaFoldDB; Q86HE5; -.
DR SMR; Q86HE5; -.
DR STRING; 44689.DDB0191161; -.
DR PaxDb; Q86HE5; -.
DR EnsemblProtists; EAL71974; EAL71974; DDB_G0269248.
DR GeneID; 8617116; -.
DR KEGG; ddi:DDB_G0269248; -.
DR dictyBase; DDB_G0269248; cf45-1.
DR eggNOG; ENOG502SF04; Eukaryota.
DR HOGENOM; CLU_073372_3_0_1; -.
DR InParanoid; Q86HE5; -.
DR OMA; WTSPTMK; -.
DR PhylomeDB; Q86HE5; -.
DR PRO; PR:Q86HE5; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IDA:dictyBase.
DR GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:dictyBase.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0042593; P:glucose homeostasis; IMP:dictyBase.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..297
FT /note="Counting factor 45-1"
FT /id="PRO_0000384449"
FT DOMAIN 24..235
FT /note="Ch-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT REGION 231..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..296
FT /note="S-G-S motif repeats"
FT /evidence="ECO:0000250"
FT ACT_SITE 29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 297 AA; 29304 MW; A77398C3965A3BCB CRC64;
MNKLISLLLV CLVAIALVNA DCAIDFDSDT VNSVTSSDWS CLAASNDRVI MQVFSGGYGY
TSGIASAVQG AQAAGISTID LYAFLCNQCS GNSPSSSAIQ SIVSQLQNDG VSYNMLWIDV
EQCDGCWGDL GDNAAFVQEA VETAQNLGVN VGVYSSIGEW SQTVGNLSGL GVDLWYAHYD
NNPSFSDSSF YEFGGWTSPT MKQYAGNGNE CGVSVDMNFF GSGTCSASTG SGSGSSSGSS
SGSSSGSSSG SGSSSGSGSS SGSSSGSGSG SSSSGSGSGS GSSSGSGSSS GSGSGSS
