PONB_DICDI
ID PONB_DICDI Reviewed; 145 AA.
AC Q54M25;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Ponticulin-like protein B;
DE Flags: Precursor;
GN Name=ponB; ORFNames=DDB_G0286247;
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 DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12890554; DOI=10.1016/s0167-4781(03)00115-5;
RA Hitt A.L., Iijima-Shimizu M., DuBay M.J., Antonette L.L., Urushihara H.,
RA Wilkerson C.G.;
RT "Identification of a second member of the ponticulin gene family and its
RT differential expression pattern.";
RL Biochim. Biophys. Acta 1628:79-87(2003).
RN [3]
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 -!- DEVELOPMENTAL STAGE: Expressed by cells, when grown on bacterial lawns,
CC or by cells cultured under conditions that give rise to fusion-
CC competent gametes, i.e. in a suspension of bacteria in the dark for 15
CC hour at 21 degrees Celsius. Does not appear to be expressed by
CC axenically grown vegetative cells or by cells during the asexual,
CC developmental life-cycle induced by removing axenic cells from HL-5
CC media. In contrast, ponticulin is expressed by vegetative cells and
CC during the early stages of the asexual developmental cycle.
CC {ECO:0000269|PubMed:12890554}.
CC -!- INDUCTION: Up-regulated in cells that are either actively phagocytosing
CC bacteria or in cells that have been cultured under conditions that
CC promote the generation of cells that are competent to fuse with the
CC opposite mating type during sexual reproduction.
CC {ECO:0000269|PubMed:12890554}.
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; AAFI02000085; EAL64299.1; -; Genomic_DNA.
DR RefSeq; XP_637806.1; XM_632714.1.
DR AlphaFoldDB; Q54M25; -.
DR PaxDb; Q54M25; -.
DR EnsemblProtists; EAL64299; EAL64299; DDB_G0286247.
DR GeneID; 8625520; -.
DR KEGG; ddi:DDB_G0286247; -.
DR dictyBase; DDB_G0286247; ponB.
DR HOGENOM; CLU_1790515_0_0_1; -.
DR PRO; PR:Q54M25; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; ISS:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; ISS:dictyBase.
DR GO; GO:0030246; F:carbohydrate binding; ISS:dictyBase.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..117
FT /note="Ponticulin-like protein B"
FT /id="PRO_0000312132"
FT PROPEP 118..145
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000312133"
FT REGION 107..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 117
FT /note="GPI-like-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 145 AA; 15188 MW; E9A8C75B8EFD9221 CRC64;
MLFIKSLLLL LSLIFAVSNA TGYVGFKVDG PGCNATKIIT LENGACQTVC TNLYGKVTPT
NDPSKFNLNP FIDVDCKTPL MAEQQVTCLP DNKPFKVSTL TVTCIPDTTS SSTSPSSTSP
SSTSPASTLI GSIAFVTLAA LFALI
