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SP65_DICDI
ID   SP65_DICDI              Reviewed;         464 AA.
AC   Q9NAX4; Q54YL6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Spore coat protein SP65;
DE            Short=Spore coat protein E;
DE   Flags: Precursor;
GN   Name=cotE; Synonyms=SP65; ORFNames=DDB_G0277903;
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], SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, AND INTERACTION WITH SP85.
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).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 18-47 AND 166-180, AND INTERACTION WITH SP85.
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).
CC   -!- FUNCTION: Forms a triad with cellulose and pspB that is essential for
CC       spore outer layer formation.
CC   -!- SUBUNIT: Binds to the C-terminal region of pspB.
CC   -!- INTERACTION:
CC       Q9NAX4; P54704: pspB; NbExp=2; IntAct=EBI-1808756, EBI-1808765;
CC   -!- SUBCELLULAR LOCATION: Spore wall {ECO:0000269|PubMed:17416892}.
CC       Note=Depends on pspB for incorporation into the coat. Accumulates
CC       initially in vesicles distinct from prespore vesicles (PSVs).
CC   -!- DEVELOPMENTAL STAGE: Expressed at or just prior to spore coat
CC       formation, at 20 to 22 hours of development of the fruiting bodies.
CC       Secreted to the cell surface before cellulose is deposited.
CC       {ECO:0000269|PubMed:17416892}.
CC   -!- DOMAIN: The N-terminal part (18-235) contains the information required
CC       for insertion into the coat.
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DR   EMBL; AF279135; AAF82380.1; -; Genomic_DNA.
DR   EMBL; AAFI02000023; EAL68124.1; -; Genomic_DNA.
DR   RefSeq; XP_642186.1; XM_637094.1.
DR   AlphaFoldDB; Q9NAX4; -.
DR   IntAct; Q9NAX4; 1.
DR   STRING; 44689.DDB0214991; -.
DR   PaxDb; Q9NAX4; -.
DR   EnsemblProtists; EAL68124; EAL68124; DDB_G0277903.
DR   GeneID; 8621393; -.
DR   KEGG; ddi:DDB_G0277903; -.
DR   dictyBase; DDB_G0277903; cotE.
DR   HOGENOM; CLU_589780_0_0_1; -.
DR   InParanoid; Q9NAX4; -.
DR   OMA; INTRSCC; -.
DR   PRO; PR:Q9NAX4; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:dictyBase.
DR   GO; GO:0031160; C:spore wall; IDA:dictyBase.
DR   GO; GO:0005199; F:structural constituent of 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; 3.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Reference proteome; Repeat;
KW   Signal; Sporulation.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:10564654"
FT   CHAIN           18..464
FT                   /note="Spore coat protein SP65"
FT                   /id="PRO_0000327782"
FT   DOMAIN          21..43
FT                   /note="Follistatin-like 1"
FT   DOMAIN          121..143
FT                   /note="Follistatin-like 2"
FT   DOMAIN          151..173
FT                   /note="Follistatin-like 3"
FT   REGION          250..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        44
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   464 AA;  47250 MW;  E97723B13144C445 CRC64;
     MKVLLLLVCL VFAYVNASYD ACYNVVCPSN YQCRAEGDQA YCVPEHHEYG CDRHSCGRGY
     ECVERWDSFC CKPIHHRPHP HPRPPHPHPR PTNCDYTSCP REFDCHVINR NVTACLPDNH
     VCRDFQCPVG THCFNGERGP HCVSDTHYPN LCRVTKCSYD FTCKMVRGNP TCLRNHDGIS
     THSPTHTPTH SPTTSPTHCP SCTELAPFCH SAGLVCRTIL NPSCVSAVRG IINTRSCCTY
     IAVCASNSTS TTGATTGATT PTSTTGAATT AAATTTTATS TTGAATTAPA TTTTTSTTGA
     ATTAPATTTT STTGAATTAP ATTTTTATTI VGVTTANSVG GLTTTRATTV AGVTTANSVG
     GLTTAGITTV AGATTGNSVG GLTTARATTV ADVTTANSVG GLTTAGVTTV AGATTGNSVG
     GLTTARATTV ADVTTANSVG GLTTSRATTI AGATTANSIG GLTN
 
 
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