ID   EXPL9_DICDI             Reviewed;         535 AA.
AC   Q54C78;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Expansin-like protein 9;
DE            Short=Ddexpl9;
DE   Flags: Precursor;
GN   Name=expl9; ORFNames=DDB_G0293148;
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).
CC   -!- FUNCTION: May serve to lubricate the movement of the cellulose
CC       microfibrils during cell growth and wall extension and/or may serve to
CC       maintain the fluid state of the slug cell wall. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the expansin family. Expansin A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000199; EAL60926.1; -; Genomic_DNA.
DR   RefSeq; XP_629341.1; XM_629339.1.
DR   AlphaFoldDB; Q54C78; -.
DR   SMR; Q54C78; -.
DR   STRING; 44689.DDB0304871; -.
DR   PaxDb; Q54C78; -.
DR   EnsemblProtists; EAL60926; EAL60926; DDB_G0293148.
DR   GeneID; 8629065; -.
DR   KEGG; ddi:DDB_G0293148; -.
DR   dictyBase; DDB_G0293148; expl9.
DR   eggNOG; ENOG502R9PZ; Eukaryota.
DR   HOGENOM; CLU_038219_0_0_1; -.
DR   InParanoid; Q54C78; -.
DR   OMA; NDENPKC; -.
DR   PhylomeDB; Q54C78; -.
DR   PRO; PR:Q54C78; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.40.10; -; 1.
DR   InterPro; IPR007112; Expansin/allergen_DPBB_dom.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   PROSITE; PS50842; EXPANSIN_EG45; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..535
FT                   /note="Expansin-like protein 9"
FT                   /id="PRO_0000383954"
FT   TOPO_DOM        26..514
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        515..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..144
FT                   /note="Expansin-like EG45"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT   REGION          459..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT   DISULFID        78..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
SQ   SEQUENCE   535 AA;  57794 MW;  1C7E34483B64414F CRC64;
     MKINKNNYFK IIIFIIYVII NLINASDNVK LSNCGQARAE PTFKQSENGG QCQLPPPSIG
     TAALSLSAFN GGARCGQCYE LTGPLGKTVV MVTDGCNSGE ACTQKDLFNF IISNKDFDKI
     GNSSSYVNIY SLGYQEVSCG FLGNIKIKFG GSLGHNGKVD YSYYFTVSFS NFNIGIKQVQ
     ILGTGMVSYM KLKRSLGGFT WNQESGGSKL QFPATLVLTG VDGQIISYKF RQPPANIAID
     MKKQFIPQVG LLSSKFNQSE ICGMGNVPEY IYEDSLTFGW IVSNSWRFNV FNLSSQDTDD
     NPTLGESVIK MDLAANGGLA FTREGGFQTK YLESLKVMIK VLPPTNSLQC FFGASGIYVI
     PGPLGGDWQE ISIPISVLKP QKVEYSLSFY NNQGQSITMW IDNIKWIFSP EAPPTPLIIT
     DPTVTPPPLP QSIVTAAAGV VGLNSIGITS NKGGVANLVD GSSNDDDGTG GTGGGASNKV
     GKRVDGEDGD NFMGGNNAFS YYNDDNSSNI LLFSFNITLT FLLLSLIINI LLLLF