PONK_DICDI
ID PONK_DICDI Reviewed; 187 AA.
AC Q1ZXQ9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Ponticulin-like protein K;
DE Flags: Precursor;
GN Name=ponK; ORFNames=DDB_G0268460;
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}.
CC -!- CAUTION: Different sequence motifs predict both the N-glycosylation
CC modification and the GPI- or GPI-like anchor modification for Asn-161.
CC While it is chemically possible for both modifications to occur, it is
CC not known whether it is enzymatically possible. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAS66948.1; -; Genomic_DNA.
DR RefSeq; XP_001134486.1; XM_001134486.1.
DR AlphaFoldDB; Q1ZXQ9; -.
DR SMR; Q1ZXQ9; -.
DR STRING; 44689.DDB0232303; -.
DR PaxDb; Q1ZXQ9; -.
DR EnsemblProtists; EAS66948; EAS66948; DDB_G0268460.
DR GeneID; 8616424; -.
DR KEGG; ddi:DDB_G0268460; -.
DR dictyBase; DDB_G0268460; ponK.
DR HOGENOM; CLU_1450173_0_0_1; -.
DR PRO; PR:Q1ZXQ9; -.
DR Proteomes; UP000002195; Chromosome 1.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..161
FT /note="Ponticulin-like protein K"
FT /id="PRO_0000367837"
FT PROPEP 162..187
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000367838"
FT REGION 115..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 161
FT /note="GPI-like-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 187 AA; 20414 MW; 5D285D1E70E659AA CRC64;
MKNLILLFLL ISIINLIQSL PLDSVINFYV NSTVGSCKGK QLEVSLDVCN NGCSNSFKIT
SSKDNVNNYN FTSYIETDDK QCLTNNYTIN LFNCSIDNAA LVGPYSVKCI FKETPSPSNS
SNPSPSPNTT SSSSLSSSSL NSNEPNQTTK PPKTNEPQKN NSTSNIPNFF AIFGFLVLII
FILGDKI
