PONJ_DICDI
ID PONJ_DICDI Reviewed; 234 AA.
AC Q54GU3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Ponticulin-like protein J;
DE Flags: Precursor;
GN Name=ponJ; ORFNames=DDB_G0289919;
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.
RX PubMed=18522444; DOI=10.1021/la800085n;
RA Barfoot R.J., Sheikh K.H., Johnson B.R., Colyer J., Miles R.E.,
RA Jeuken L.J., Bushby R.J., Evans S.D.;
RT "Minimal F-actin cytoskeletal system for planar supported phospholipid
RT bilayers.";
RL Langmuir 24:6827-6836(2008).
CC -!- FUNCTION: Binds F-actin and nucleates actin assembly.
CC {ECO:0000269|PubMed:18522444}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- PTM: The GPI-like-anchor contains a phosphoceramide group, rather than
CC a phosphatidyl group. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ponticulin family. {ECO:0000305}.
CC -!- CAUTION: The Dictyosteliida are known to produce a
CC glycosylsphingolipidinositol anchor (GPI-like-anchor). It has not been
CC established whether Dictyosteliida make a glycosylphosphatidylinositol
CC anchor (GPI-anchor) also, and whether their GPI-like-anchor
CC modifications can be interconverted with GPI-anchor modifications in a
CC resculpting process. It has not been established that the GPI-like-
CC anchor modification in Dictyosteliida utilizes the same sequence motif.
CC {ECO:0000305}.
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DR EMBL; AAFI02000149; EAL62472.1; -; Genomic_DNA.
DR RefSeq; XP_635976.1; XM_630884.1.
DR AlphaFoldDB; Q54GU3; -.
DR STRING; 44689.DDB0232304; -.
DR PaxDb; Q54GU3; -.
DR EnsemblProtists; EAL62472; EAL62472; DDB_G0289919.
DR GeneID; 8627391; -.
DR KEGG; ddi:DDB_G0289919; -.
DR dictyBase; DDB_G0289919; ponJ.
DR eggNOG; ENOG502RI2M; Eukaryota.
DR HOGENOM; CLU_1186864_0_0_1; -.
DR InParanoid; Q54GU3; -.
DR OMA; NTEDQTC; -.
DR PRO; PR:Q54GU3; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Actin-binding; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..212
FT /note="Ponticulin-like protein J"
FT /id="PRO_0000367835"
FT PROPEP 213..234
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000367836"
FT REGION 115..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 212
FT /note="GPI-like-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 234 AA; 25152 MW; 2554F04D4D8397C2 CRC64;
MRLLNNLILM VVLFVAVSNA TTKFTFNTFS VRNTEDQTCF TKTAKTTDDS TKVDINKCTV
GCGGSMKIRK GTKSQQYQFE LFSSTDCTGE TTSKVLFVCP NPSIDAISIK STSNTIKCGT
LPPDSEIKED DTATAVVNDE NNNETKNEPK TKTKSTPKSP STPKTNNSNE DSDLTTSSSD
SSSSTKSSPK SKSSTEVNEN KPKSDNETAE GNNASSNIAT FSLVIISLLV ASLF
