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Database: UniProt
Entry: Q54TR1
LinkDB: Q54TR1
Original site: Q54TR1 
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   29-OCT-2014, entry version 55.
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; Mycetozoa; Dictyosteliida; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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.,
RA   Hatton R.D., Gomer R.H.;
RT   "The secreted Dictyostelium protein CfaD is a chalone.";
RL   J. Cell Sci. 121:2473-2480(2008).
RN   [3]
RP   ERRATUM.
RA   Bakthavatsalam D., Brock D.A., Nikravan N.N., Houston K.D.,
RA   Hatton R.D., 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
RT   cell proliferation.";
RL   BMC Biochem. 10:4-4(2009).
CC   -!- FUNCTION: Inhibitor that slows proliferation of secreting cells
CC       (also 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
CC       type cells and exhibit supernumerary centrosomes and a cytokinesis
CC       defect. They also produce fewer spores at culmination. Form large
CC       fruiting bodies with large spore heads.
CC       {ECO:0000269|PubMed:18611962, ECO:0000269|PubMed:19187549}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
CC       ProRule:PRU10089}.
CC   -!- CAUTION: Lacks catalytic activity, even though the active site
CC       residues are conserved. {ECO:0000305}.
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DR   EMBL; AAFI02000042; EAL66564.1; -; Genomic_DNA.
DR   RefSeq; XP_640530.1; XM_635438.1.
DR   ProteinModelPortal; Q54TR1; -.
DR   STRING; 44689.DDB_0229857; -.
DR   MEROPS; C01.107; -.
DR   PRIDE; Q54TR1; -.
DR   EnsemblProtists; DDB0229857; DDB0229857; DDB_G0281605.
DR   GeneID; 8623140; -.
DR   KEGG; ddi:DDB_G0281605; -.
DR   dictyBase; DDB_G0281605; cfaD.
DR   eggNOG; COG4870; -.
DR   InParanoid; Q54TR1; -.
DR   OMA; PSAHEHE; -.
DR   PhylomeDB; Q54TR1; -.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:dictyBase.
DR   GO; GO:0005576; C:extracellular region; IDA:dictyBase.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:dictyBase.
DR   GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; PTHR12411; 1.
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   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Disulfide bond; Glycoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    531       Counting factor associated protein D.
FT                                /FTId=PRO_0000384376.
FT   ACT_SITE    333    333       {ECO:0000250}.
FT   ACT_SITE    475    475       {ECO:0000250}.
FT   ACT_SITE    495    495       {ECO:0000250}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    423    423       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    330    373       {ECO:0000250}.
FT   DISULFID    364    406       {ECO:0000250}.
FT   DISULFID    466    517       {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
//
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