DD3_DICDI
ID DD3_DICDI Reviewed; 616 AA.
AC Q58A42; Q54RK9;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Protein DD3-3;
DE Flags: Precursor;
GN Name=DD3-3; ORFNames=DDB_G0283095;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=15883003; DOI=10.1016/j.bbrc.2005.03.244;
RA Sakuragi N., Ogasawara N., Tanesaka E., Yoshida M.;
RT "Functional analysis of a novel gene, DD3-3, from Dictyostelium
RT discoideum.";
RL Biochem. Biophys. Res. Commun. 331:1201-1206(2005).
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 INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA Skelton J., Ivens A., Bozzaro S.;
RT "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT bacteria in Dictyostelium.";
RL BMC Genomics 9:291-291(2008).
CC -!- FUNCTION: May participate in O-glycosylation.
CC {ECO:0000269|PubMed:15883003}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expression appears at the growth phase stage and
CC rapidly increases after starvation began. It reaches its peak at 3
CC hours and is continually expressed for 12 hours after starvation has
CC begun. {ECO:0000269|PubMed:15883003}.
CC -!- INDUCTION: Down-regulated by phagocytic stimuli.
CC {ECO:0000269|PubMed:18559084}.
CC -!- DISRUPTION PHENOTYPE: Displays down-regulation of regA, cAMP-dependent
CC phosphodiesterase, and overexpression of protein tyrosine kinase during
CC early development and its shutdown during late development.
CC {ECO:0000269|PubMed:15883003}.
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DR EMBL; AB120173; BAD93186.1; -; mRNA.
DR EMBL; AAFI02000050; EAL65877.1; -; Genomic_DNA.
DR RefSeq; XP_639227.1; XM_634135.1.
DR AlphaFoldDB; Q58A42; -.
DR BioGRID; 1248916; 1.
DR STRING; 44689.DDB0231683; -.
DR PaxDb; Q58A42; -.
DR EnsemblProtists; EAL65877; EAL65877; DDB_G0283095.
DR GeneID; 8623913; -.
DR KEGG; ddi:DDB_G0283095; -.
DR dictyBase; DDB_G0283095; DD3-3.
DR eggNOG; ENOG502QRWS; Eukaryota.
DR HOGENOM; CLU_020767_1_0_1; -.
DR InParanoid; Q58A42; -.
DR OMA; YYPYWAP; -.
DR PhylomeDB; Q58A42; -.
DR PRO; PR:Q58A42; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..616
FT /note="Protein DD3-3"
FT /id="PRO_0000393565"
FT TOPO_DOM 22..563
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 27..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 616 AA; 69498 MW; 2E001672576E6DB8 CRC64;
MRFLSSLIIL LIITIYSSVN GDIYMHSPPG SNNRNQEQGQ NRDNNQRLFN SQNNDKGGYC
RGEALEWYEK SYLPVEWTNQ HGCGSGETEC NIVIQYMCTD NAKAADTEYI RDGTVTTTIS
ANDITQSSTK ETNEYKFGMH ESYHHYQNCT GRERNKGLFI ANQNIGNNAD RTRQSNNGNN
YGYECQEERD YYPYWAPSPW KDVAIITDNR DLCKWYRSES QNVQPKYYCK AATTNNNQPR
SIDPVICANQ GGVWTKVDSH DIGAPECIKA EWTQVNTLGH VLEDGHNPMY NWSLPHSGME
PCIATGTCSC VLRVRYNISS SDLKGNGDEF TDYKSNGPKG ATNVNDPNVV VAGQNVTLNI
NPNQYGRTFQ DRSHVFSIIA RPDSLKKAKI WNLLVKGKRG NIVQSHPAQE YQFVPKTLHI
KVNEYIHYQW TGCDFNPQNY DGTGIKGSDR SNMCQIKTLN HNYPMTDDEL NDDNALFADM
ETRLRFARLG QKSCLTYDEL MTKNNNNKDA VEVDPQNCMV LNNAGTRFNG GVQKMSKTGS
YYYMSTRNNN FSNRNQKGAI HVDPLLAGWQ IGLIASGCSL FVIISATAGC VTFARFHPHS
GMHRAVSKVP GLKRLV