ID   YEPB_SCHPO              Reviewed;         629 AA.
AC   O13941;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Uncharacterized beta-glucan synthesis-associated protein C23H3.11c;
GN   ORFNames=SPAC23H3.11c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAB16237.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Required for synthesis of the major beta-glucans of the yeast
CC       cell wall. {ECO:0000250|UniProtKB:P33336}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SKN1/KRE6 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16237.1; -; Genomic_DNA.
DR   PIR; T38304; T38304.
DR   RefSeq; NP_593801.1; NM_001019230.2.
DR   AlphaFoldDB; O13941; -.
DR   BioGRID; 278356; 7.
DR   STRING; 4896.SPAC23H3.11c.1; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   PaxDb; O13941; -.
DR   EnsemblFungi; SPAC23H3.11c.1; SPAC23H3.11c.1:pep; SPAC23H3.11c.
DR   GeneID; 2541866; -.
DR   KEGG; spo:SPAC23H3.11c; -.
DR   PomBase; SPAC23H3.11c; -.
DR   VEuPathDB; FungiDB:SPAC23H3.11c; -.
DR   eggNOG; ENOG502QR13; Eukaryota.
DR   HOGENOM; CLU_010811_4_3_1; -.
DR   InParanoid; O13941; -.
DR   OMA; RGWINSV; -.
DR   PhylomeDB; O13941; -.
DR   PRO; PR:O13941; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015926; F:glucosidase activity; IBA:GO_Central.
DR   GO; GO:0006078; P:(1->6)-beta-D-glucan biosynthetic process; ISO:PomBase.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   CDD; cd02180; GH16_fungal_KRE6_glucanase; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR005629; Skn1/Kre6/Sbg1.
DR   PANTHER; PTHR31361; PTHR31361; 1.
DR   Pfam; PF03935; SKN1_KRE6_Sbg1; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..629
FT                   /note="Uncharacterized beta-glucan synthesis-associated
FT                   protein C23H3.11c"
FT                   /id="PRO_0000317220"
FT   TOPO_DOM        1..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P33336, ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..629
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P33336, ECO:0000255"
FT   DOMAIN          231..578
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   629 AA;  70785 MW;  7D80C31D3D679696 CRC64;
     MEKGHSDLPR QPERVAQNPF LTFDQDSFPS SYGSSLNVSE QTSGSSSTSP LPQISCLLRK
     DDVPLANKEL SRSLIHVQEL SRYPPFYNQD HQHLGVPRSR VGSDVWKMRE KSFLSPSQFS
     SIDLSWVYRS KEEDDDFHDP KSSVVSLMGE EDYLGWSRFC DLFFLFVLSL GIGLLFIVFP
     ALTFTGNITP SKEKFDAIMA NQITDHLFAH MRVPRTNLID KDTPSTAYHR TGYNGRKYNL
     VFSDEFNKEG RSFYSGNDQF WEAVNIHYAA TNDLDWYDPD AITTVNGTLA IQLDAFWNRD
     LNFRSGMLQS WNKLCLKGGI IEVSASLAGS GEHAGLWPGI WTLGNLARPG YMATTDGVWP
     YAYSQCDVGI TPNQSSYDGI SYLPGQKLPN CVCLNEDHPS PGVGRGAPEI DILEGSTEKL
     HPDDELDIGV VSQSGQFAPF DFFWLPNYDY LAVYNDSITH MNSYVGGPFQ QALSGITTLN
     NTWYGGNAFQ IYGFDYKPGE GTNGYVSWFV GPNYTWSMLG SAVGQNGNVG PRQISEEPMS
     IIFNLGISNN WAYYYFRDLS FPAVMYIDYI RIYQDPDDTN SHIGCDPPGY PTTKYIEEHP
     LAYKNPNATT WEMAGYTWPK NSLMHKCNT