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YEOB_SCHPO
ID   YEOB_SCHPO              Reviewed;         636 AA.
AC   O13789;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Uncharacterized beta-glucan synthesis-associated protein C17G6.11c;
GN   ORFNames=SPAC17G6.11c;
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:CAB16222.1}
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; CAB16222.1; -; Genomic_DNA.
DR   PIR; T37843; T37843.
DR   RefSeq; NP_594258.1; NM_001019681.2.
DR   AlphaFoldDB; O13789; -.
DR   BioGRID; 278646; 1.
DR   STRING; 4896.SPAC17G6.11c.1; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   iPTMnet; O13789; -.
DR   MaxQB; O13789; -.
DR   PaxDb; O13789; -.
DR   PRIDE; O13789; -.
DR   EnsemblFungi; SPAC17G6.11c.1; SPAC17G6.11c.1:pep; SPAC17G6.11c.
DR   GeneID; 2542171; -.
DR   KEGG; spo:SPAC17G6.11c; -.
DR   PomBase; SPAC17G6.11c; -.
DR   VEuPathDB; FungiDB:SPAC17G6.11c; -.
DR   eggNOG; ENOG502QR13; Eukaryota.
DR   HOGENOM; CLU_010811_4_2_1; -.
DR   InParanoid; O13789; -.
DR   OMA; YITWINE; -.
DR   PhylomeDB; O13789; -.
DR   PRO; PR:O13789; -.
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; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; ISO:PomBase.
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..636
FT                   /note="Uncharacterized beta-glucan synthesis-associated
FT                   protein C17G6.11c"
FT                   /id="PRO_0000317219"
FT   TOPO_DOM        1..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P32486, ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..636
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P32486, ECO:0000255"
FT   DOMAIN          218..587
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        616
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   636 AA;  70008 MW;  B30861820641323B CRC64;
     MYNVRGDLNR KTPSDGNVNE IGSMYASRDT STSSFTNPTD SSTRLLYNNA SNATFSSAAL
     AAGVGGTRAS GYTHRFSIRP SSQTYNRYPN GGNSAGSDMY STSPQNNSIV DDIENINKLE
     AVAFAGPTAG ESDFSLSRED KEIDDFLHYP LPAKDAKKLS YFVGGEGLMQ LLFLLFLAAG
     TGMLFIGLPI LTYTGHNSLA STRVTGITNH QFRILRLLRY GSLIDPDTPE SAYTFDSQDL
     GTLDLVFSDE FNYPGRAFYD GDDQFWLATD LHYAATTDYE YYDADTPTTA NGTLRLRMDA
     FYNHDLNFRS GMVTTWNKLC FKGGRIEVSA SLGGSPYIPG FWPGIWTIGN LVRPGYLATS
     DGVWPYSYNS CDAGITPNQS DPSGISYLGG QRLNQCVCKG EDHPNVGTGR GGPEIDALEG
     TFGSGIPYNG SIYLETMPVV SQSAQYAPFD LYMYPNYDFV TIYNQSVSAM NGWAGGVYQQ
     ALSCASQLNN SWLSGNAYQK YGFDYKPGSG PDALISWFVG DEYTWTMRQP AVGQNGNIAS
     RPVSEEPMIV VLNFGISPTW IYFYWYELTF PQTMYVDYVR IYQDSSDSSS VLGCDPEGFP
     TTEYIANHPK AYLNYNATSW SEAGYVRPKN SLMDGC
 
 
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