CFAD_DICDI
ID CFAD_DICDI Reviewed; 531 AA.
AC Q54TR1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Counting factor associated protein D;
DE Flags: Precursor;
GN Name=cfaD; ORFNames=DDB_G0281605;
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).
RN [2]
RP FUNCTION, INTERACTION WITH APRA, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18611962; DOI=10.1242/jcs.026682;
RA Bakthavatsalam D., Brock D.A., Nikravan N.N., Houston K.D., Hatton R.D.,
RA Gomer R.H.;
RT "The secreted Dictyostelium protein CfaD is a chalone.";
RL J. Cell Sci. 121:2473-2480(2008).
RN [3]
RP ERRATUM OF PUBMED:18611962.
RA Bakthavatsalam D., Brock D.A., Nikravan N.N., Houston K.D., Hatton R.D.,
RA Gomer R.H.;
RL J. Cell Sci. 121:2782-2782(2008).
RN [4]
RP FUNCTION, INTERACTION WITH APRA, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19187549; DOI=10.1186/1471-2091-10-4;
RA Choe J.M., Bakthavatsalam D., Phillips J.E., Gomer R.H.;
RT "Dictyostelium cells bind a secreted autocrine factor that represses cell
RT proliferation.";
RL BMC Biochem. 10:4-4(2009).
CC -!- FUNCTION: Inhibitor that slows proliferation of secreting cells (also
CC known as chalone). Requires aprA for activity.
CC {ECO:0000269|PubMed:18611962, ECO:0000269|PubMed:19187549}.
CC -!- SUBUNIT: Interacts with aprA. {ECO:0000269|PubMed:18611962,
CC ECO:0000269|PubMed:19187549}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18611962,
CC ECO:0000269|PubMed:19187549}. Note=Concentrated in subcellular
CC structures, possibly vesicles.
CC -!- DEVELOPMENTAL STAGE: Expressed at highest levels in vegetatively
CC growing cells and declines during development (at protein level).
CC -!- DISRUPTION PHENOTYPE: Cells proliferate more rapidly than wild type
CC cells and exhibit supernumerary centrosomes and a cytokinesis defect.
CC They also produce fewer spores at culmination. Form large fruiting
CC bodies with large spore heads. {ECO:0000269|PubMed:18611962,
CC ECO:0000269|PubMed:19187549}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
CC -!- CAUTION: Lacks catalytic activity, even though the active site residues
CC are conserved. {ECO:0000305}.
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DR EMBL; AAFI02000042; EAL66564.1; -; Genomic_DNA.
DR RefSeq; XP_640530.1; XM_635438.1.
DR AlphaFoldDB; Q54TR1; -.
DR SMR; Q54TR1; -.
DR STRING; 44689.DDB0229857; -.
DR MEROPS; C01.067; -.
DR PaxDb; Q54TR1; -.
DR EnsemblProtists; EAL66564; EAL66564; DDB_G0281605.
DR GeneID; 8623140; -.
DR KEGG; ddi:DDB_G0281605; -.
DR dictyBase; DDB_G0281605; cfaD.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_11_0_1; -.
DR InParanoid; Q54TR1; -.
DR OMA; GIMNMAK; -.
DR PhylomeDB; Q54TR1; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR PRO; PR:Q54TR1; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:dictyBase.
DR GO; GO:0005576; C:extracellular region; IDA:dictyBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IDA:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IDA:dictyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:dictyBase.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..531
FT /note="Counting factor associated protein D"
FT /id="PRO_0000384376"
FT ACT_SITE 333
FT /evidence="ECO:0000250"
FT ACT_SITE 475
FT /evidence="ECO:0000250"
FT ACT_SITE 495
FT /evidence="ECO:0000250"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 330..373
FT /evidence="ECO:0000250"
FT DISULFID 364..406
FT /evidence="ECO:0000250"
FT DISULFID 466..517
FT /evidence="ECO:0000250"
SQ SEQUENCE 531 AA; 58638 MW; 248E0C8E1FE13DA5 CRC64;
MNKFILLLSL VTLSCVLAVP QLPAAQQYYM KGSFNIPYFN IVEPIELIYD SVNNRQYISV
YNGMDITINF YNQDNTYNVG PVKYDMVCTT TPGNGSLVNV LPTEPSSWVY NGTSTVNGVQ
VFGYSQKITQ YGRTGFYNFY VDANGVPVQF YMDGVDYVFG SHPDVYVLNF DIYTTDISSY
ESYFDIPVLC NNAKEAPAKE NQFDGLFSSI GDNLLAKEEQ ASNLFKEYKA QYNKEYSSQD
EHDERFINFK AARKIIATHN AKESSYKLGM NHYADLSNKE FNTLVKPKVA RPSVTGADSV
HDDESLRSIP STVDWRNQNC VTPVKDQGIC GSCWTFGSTG SLEGTNCVTN GELVSLSEQQ
LVDCAILTGS QGCGGGFASS AFQYVMEIGS LATESNYPYL MQNGLCRDRT VTPSGVSITG
YVNVTSGSES ALQNAIATTG PVAIAIDASV DDFRYYMSGV YNNPACKNGL DDLDHEVLAI
GYGTYQGQDY FLVKNSWSTN WGMDGYVYMA RNDNNLCGVS SQATYPIPTK N
