PSA_DICDI
ID PSA_DICDI Reviewed; 168 AA.
AC P12729; Q55FX7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Prespore-specific protein A;
DE AltName: Full=Cell surface antigen PsA;
DE AltName: Full=Ponticulin-like protein G;
DE AltName: Full=Protein D19;
DE Flags: Precursor;
GN Name=pspA; Synonyms=D19, ponG, psaA; ORFNames=DDB_G0267412;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-100.
RC STRAIN=AX2;
RX PubMed=2850494; DOI=10.1128/mcb.8.8.3458-3466.1988;
RA Early A.E., Williams J.G., Meyer H.E., Por S.B., Smith E., Williams K.L.,
RA Gooley A.A.;
RT "Structural characterization of Dictyostelium discoideum prespore-specific
RT gene D19 and of its product, cell surface glycoprotein PsA.";
RL Mol. Cell. Biol. 8:3458-3466(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX2;
RX PubMed=2550894; DOI=10.1093/nar/17.16.6473;
RA Early A.E., Williams J.G.;
RT "Identification of sequences regulating the transcription of a
RT Dictyostelium gene selectively expressed in prespore cells.";
RL Nucleic Acids Res. 17:6473-6484(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX2;
RX PubMed=3243026; DOI=10.1002/dvg.1020090419;
RA Early A.E., McRobbie S.J., Duffy K.T., Jermyn K.A., Tilly R.,
RA Ceccarelli A., Williams J.G.;
RT "Structural and functional characterization of genes encoding Dictyostelium
RT prestalk and prespore cell-specific proteins.";
RL Dev. Genet. 9:383-402(1988).
RN [4]
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 [5]
RP PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION.
RX PubMed=8681966; DOI=10.1111/j.1432-1033.1996.0511z.x;
RA Zachara N.E., Packer N.H., Temple M.D., Slade M.B., Jardine D.R.,
RA Karuso P., Moss C.J., Mabbutt B.C., Curmi P.M.G., Williams K.L.,
RA Gooley A.A.;
RT "Recombinant prespore-specific antigen from Dictyostelium discoideum is a
RT beta-sheet glycoprotein with a spacer peptide modified by O-linked N-
RT acetylglucosamine.";
RL Eur. J. Biochem. 238:511-518(1996).
RN [6]
RP POLYMORPHISM.
RX PubMed=1582556; DOI=10.1093/genetics/130.4.749;
RA Gooley A.A., Marshchalek R., Williams K.L.;
RT "Size polymorphisms due to changes in the number of O-glycosylated tandem
RT repeats in the Dictyostelium discoideum glycoprotein PsA.";
RL Genetics 130:749-756(1992).
RN [7]
RP GPI-ANCHOR, AND GLYCOSYLATION.
RX PubMed=8404891; DOI=10.1111/j.1432-1033.1993.tb18192.x;
RA Haynes P.A., Gooley A.A., Ferguson M.A., Redmond J.W., Williams K.L.;
RT "Post-translational modifications of the Dictyostelium discoideum
RT glycoprotein PsA. Glycosylphosphatidylinositol membrane anchor and
RT composition of O-linked oligosaccharides.";
RL Eur. J. Biochem. 216:729-737(1993).
RN [8]
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: May bind F-actin and nucleates actin assembly.
CC {ECO:0000305|PubMed:18522444}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- DEVELOPMENTAL STAGE: Appears first in the multicellular stage soon
CC after tip formation and is selectively expressed on prespore cells.
CC -!- PTM: O-glycosylated in the repeat region. The oligosaccharides contain
CC N-acetylglucosamine and fucose as the major constituents.
CC {ECO:0000269|PubMed:8404891, ECO:0000269|PubMed:8681966}.
CC -!- PTM: The GPI-like-anchor contains a phosphoceramide group, rather than
CC a phosphatidyl group.
CC -!- POLYMORPHISM: Allelic variation results in a protein with three, four
CC or five tandem copies of Pro-Thr-Val-thr. {ECO:0000269|PubMed:1582556}.
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; M20909; AAA52100.1; -; Genomic_DNA.
DR EMBL; X15980; CAA34102.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EAL73158.1; -; Genomic_DNA.
DR PIR; A54733; A31196.
DR RefSeq; XP_647406.1; XM_642314.1.
DR AlphaFoldDB; P12729; -.
DR BMRB; P12729; -.
DR STRING; 44689.DDB0191129; -.
DR PaxDb; P12729; -.
DR EnsemblProtists; EAL73158; EAL73158; DDB_G0267412.
DR GeneID; 8616213; -.
DR KEGG; ddi:DDB_G0267412; -.
DR dictyBase; DDB_G0267412; pspA.
DR HOGENOM; CLU_1589455_0_0_1; -.
DR OMA; YANAYDY; -.
DR PhylomeDB; P12729; -.
DR PRO; PR:P12729; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:dictyBase.
DR GO; GO:0009986; C:cell surface; IDA:dictyBase.
DR GO; GO:0005576; C:extracellular region; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IDA:dictyBase.
DR GO; GO:1902168; P:response to catechin; IDA:dictyBase.
DR GO; GO:0031153; P:slug development involved in sorocarp development; IEP:dictyBase.
PE 1: Evidence at protein level;
KW Actin-binding; Cell membrane; Direct protein sequencing; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2850494"
FT CHAIN 20..147
FT /note="Prespore-specific protein A"
FT /id="PRO_0000022164"
FT PROPEP 148..168
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022165"
FT REPEAT 116..119
FT /note="1"
FT REPEAT 120..123
FT /note="2"
FT REPEAT 124..127
FT /note="3"
FT REGION 116..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..127
FT /note="3 X 4 AA tandem repeats of T-P-T-V"
FT LIPID 147
FT /note="GPI-like-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 114
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 116
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 118
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 120
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 122
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 124
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 126
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 128
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 130
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 132
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 134
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 138
FT /note="O-linked (GlcNAc) threonine"
FT CARBOHYD 140
FT /note="O-linked (GlcNAc) serine"
SQ SEQUENCE 168 AA; 17879 MW; 470B71EE9AA09F62 CRC64;
MKFQHTFIAL LSLLTYANAY DYFTTTLANQ NPVCASVDVI QNVCTEVCGR FVRYIPDATN
TNQFTFAEYT TNQCTVQVTP AVTNTFTCAD QTSSHALGSD WSGVCKITAT PAPTVTPTVT
PTVTPTVTPT PTNTPNPTPS QTSTTTGSAS TVVASLSLII FSMILSLC
