SP85_DICDI
ID SP85_DICDI Reviewed; 532 AA.
AC P54704; O61133; O61134; O61135; Q550L6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Spore coat protein SP85;
DE AltName: Full=Cellulose-binding protein SP85;
DE AltName: Full=Prespore protein 14E6;
DE AltName: Full=Prespore protein B;
DE Flags: Precursor;
GN Name=pspB; Synonyms=PsB, SP85; ORFNames=DDB_G0276939;
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].
RC STRAIN=AX3;
RX PubMed=8050366; DOI=10.1242/dev.120.6.1601;
RA Powell-Coffman J.A., Firtel R.A.;
RT "Characterization of a novel Dictyostelium discoideum prespore-specific
RT gene, PspB, reveals conserved regulatory sequences.";
RL Development 120:1601-1611(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 159-177; 179-188 AND
RP 420-427, AND BINDING TO CELLULOSE.
RC STRAIN=AX3, WS380B, and WS576;
RX PubMed=9692967; DOI=10.1021/bi9808013;
RA Zhang Y., Brown R.D. Jr., West C.M.;
RT "Two proteins of the Dictyostelium spore coat bind to cellulose in vitro.";
RL Biochemistry 37:10766-10779(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
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 CHARACTERIZATION, AND INTERACTION WITH SP65.
RX PubMed=10564654; DOI=10.1242/jcs.112.23.4367;
RA Zhang Y., Zhang P., West C.M.;
RT "A linking function for the cellulose-binding protein SP85 in the spore
RT coat of Dictyostelium discoideum.";
RL J. Cell Sci. 112:4367-4377(1999).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 352-TRP--HIS-354; 390-ARG--LYS-392;
RP 417-LYS--GLN-419 AND 445-ARG--GLU-448.
RX PubMed=12624193; DOI=10.1099/mic.0.25984-0;
RA Metcalf T., Kelley K., Erdos G.W., Kaplan L., West C.M.;
RT "Formation of the outer layer of the Dictyostelium spore coat depends on
RT the inner-layer protein SP85/PsB.";
RL Microbiology 149:305-317(2003).
RN [7]
RP GLYCOSYLATION.
RX PubMed=14551185; DOI=10.1074/jbc.m308756200;
RA Wang F., Metcalf T., van der Wel H., West C.M.;
RT "Initiation of mucin-type O-glycosylation in Dictyostelium is homologous to
RT the corresponding step in animals and is important for spore coat
RT function.";
RL J. Biol. Chem. 278:51395-51407(2003).
RN [8]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH SP65.
RX PubMed=17416892; DOI=10.1128/ec.00329-06;
RA Metcalf T., van der Wel H., Escalante R., Sastre L., West C.M.;
RT "Role of SP65 in assembly of the Dictyostelium discoideum spore coat.";
RL Eukaryot. Cell 6:1137-1149(2007).
CC -!- FUNCTION: Required for incorporation of cotE into the spore coat and
CC for the formation of the outer layer. Has a cross-bridging function
CC between cellulose and other coat proteins.
CC {ECO:0000269|PubMed:12624193}.
CC -!- SUBUNIT: Binds to cotE.
CC -!- INTERACTION:
CC P54704; Q9NAX4: cotE; NbExp=2; IntAct=EBI-1808765, EBI-1808756;
CC -!- SUBCELLULAR LOCATION: Spore wall {ECO:0000269|PubMed:17416892}.
CC Note=Accumulates in prespore vesicles coordinately with other coat
CC proteins.
CC -!- DEVELOPMENTAL STAGE: Expressed from 17.5 hours of development of the
CC fruiting bodies. {ECO:0000269|PubMed:17416892}.
CC -!- DOMAIN: The N-terminal part (1-200) directs accumulation in prespore
CC vesicles.
CC -!- DOMAIN: The C-terminal part (333-532) binds cellulose and cotE
CC simultaneously and specifies incorporation into the coat.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:14551185}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC60506.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S72639; AAC60506.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF066071; AAC19123.1; -; Genomic_DNA.
DR EMBL; AF066072; AAC19124.1; -; Genomic_DNA.
DR EMBL; AF066073; AAC19125.1; -; Genomic_DNA.
DR EMBL; AAFI02000019; EAL68971.1; -; Genomic_DNA.
DR RefSeq; XP_642916.1; XM_637824.1.
DR AlphaFoldDB; P54704; -.
DR IntAct; P54704; 1.
DR STRING; 44689.DDB0185060; -.
DR PaxDb; P54704; -.
DR EnsemblProtists; EAL68971; EAL68971; DDB_G0276939.
DR GeneID; 8620782; -.
DR KEGG; ddi:DDB_G0276939; -.
DR dictyBase; DDB_G0276939; pspB.
DR eggNOG; ENOG502RFIS; Eukaryota.
DR HOGENOM; CLU_512347_0_0_1; -.
DR InParanoid; P54704; -.
DR OMA; DNKWEND; -.
DR PRO; PR:P54704; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0090665; C:glycoprotein complex; IDA:dictyBase.
DR GO; GO:0031160; C:spore wall; IDA:dictyBase.
DR GO; GO:0030248; F:cellulose binding; IDA:dictyBase.
DR GO; GO:0005199; F:structural constituent of cell wall; IMP:dictyBase.
DR GO; GO:0099614; P:protein localization to spore cell wall; IMP:dictyBase.
DR GO; GO:0042244; P:spore wall assembly; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR InterPro; IPR003645; Fol_N.
DR SMART; SM00274; FOLN; 4.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Reference proteome; Repeat;
KW Signal; Sporulation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..532
FT /note="Spore coat protein SP85"
FT /id="PRO_0000032668"
FT DOMAIN 267..289
FT /note="Follistatin-like 1"
FT DOMAIN 335..359
FT /note="Follistatin-like 2"
FT DOMAIN 400..423
FT /note="Follistatin-like 3"
FT DOMAIN 430..452
FT /note="Follistatin-like 4"
FT REGION 197..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 222..229
FT /note="Missing (in strain: WS576 and WS380B)"
FT VARIANT 233
FT /note="T -> S (in strain: WS576 and WS380B)"
FT VARIANT 237
FT /note="T -> S (in strain: WS576 and WS380B)"
FT VARIANT 252..258
FT /note="PTYPPTQ -> RSYPQTP (in strain: WS380B)"
FT VARIANT 253..254
FT /note="TY -> SC (in strain: WS576)"
FT VARIANT 255..258
FT /note="Missing (in strain: WS576)"
FT VARIANT 261
FT /note="T -> S (in strain: WS380B)"
FT VARIANT 315
FT /note="P -> S (in strain: WS576)"
FT MUTAGEN 352..354
FT /note="WEN->SKH: In ANC1(B); no effect on cellulose
FT binding. Loss of cellulose binding; when associated with
FT 390-SGE-392, 417-QGE-419 and 445-SAAQ-448."
FT /evidence="ECO:0000269|PubMed:12624193"
FT MUTAGEN 390..392
FT /note="RGK->SGE: In ANC1(C); no effect on cellulose
FT binding. Loss of cellulose binding; when associated with
FT 352-SKH-354, 417-QGE-419 and 445-SAAQ-448."
FT /evidence="ECO:0000269|PubMed:12624193"
FT MUTAGEN 417..419
FT /note="KGQ->QGE: In ANC1(D); no effect on cellulose
FT binding. Loss of cellulose binding; when associated with
FT 352-SKH-354, 390-SGE-392 and 445-SAAQ-448."
FT /evidence="ECO:0000269|PubMed:12624193"
FT MUTAGEN 445..448
FT /note="RRGE->SAAQ: In ANC1(E); no effect on cellulose
FT binding. Loss of cellulose binding; when associated with
FT 352-SKH-354, 390-SGE-392 and 417-QGE-419."
FT /evidence="ECO:0000269|PubMed:12624193"
FT CONFLICT 215..326
FT /note="Missing (in Ref. 1; AAC60506)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="T -> S (in Ref. 2; AAC19123)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="R -> S (in Ref. 1; AAC60506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 59506 MW; DED65EBE1D4E7671 CRC64;
MRLLSVLLIG FLCLAGTYAQ KYQLSPAYND PYLTDDKTGT HDFWVQNASL PVFYGFHDWN
FQDNSGIMEI NGDEMHITGK IYPTVNMGDC HRYNVDLVFK KDKSGNVMPK KELRESAYVP
HGPIDPATWK YYTFVQGKWT GFGCDPQNVV FSGAEGGMPL QLGYGANGKN GDNGISVWLI
YGYTIVDINC NIRPIITQSP TQPPTQPPTY PPTQPPTQPP TQPPTYPPTY PPTYPPTYPP
TYPPTHPPTY PPTYPPTQPP TQPPVQDCST LECPEGFHCE IVNNRRTCVC DTTVPPTHPP
TQSPTYPPTQ PPTQPPTYPP TYPPTYPPTQ PPRASCDNVR CPRGYHCECN HWENVARCVR
NEEPTHRPKP PHHGCRPDSC ARGEKCICVR GKIYCIPKTT CDQVRCPRKH HCECNRKGQV
FCVPDCPKLT CKQVGCPENH ECVSRRGELH CVYVRPPTGR WGDDLSDLGY NQASVEAAID
AYEAQRGQRP HNNIPSNNLH QENNDNLGDG FYDGVEIGFA DGGFDVNDLN GF
