ID   YHG7_SCHPO              Reviewed;         442 AA.
AC   Q9P6I3;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 2.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Putative mannan endo-1,6-alpha-mannosidase C1198.07c;
DE            EC=3.2.1.101;
DE   AltName: Full=Endo-alpha-1->6-D-mannanase C1198.07c;
DE   Flags: Precursor;
GN   ORFNames=SPBC1198.07c;
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]
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]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in
CC         unbranched (1->6)-mannans.; EC=3.2.1.101;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 76 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB91182.2; -; Genomic_DNA.
DR   RefSeq; NP_595076.2; NM_001020982.2.
DR   AlphaFoldDB; Q9P6I3; -.
DR   SMR; Q9P6I3; -.
DR   STRING; 284812.Q9P6I3; -.
DR   CAZy; GH76; Glycoside Hydrolase Family 76.
DR   iPTMnet; Q9P6I3; -.
DR   MaxQB; Q9P6I3; -.
DR   PaxDb; 4896-SPBC1198-07c-1; -.
DR   EnsemblFungi; SPBC1198.07c.1; SPBC1198.07c.1:pep; SPBC1198.07c.
DR   GeneID; 2539836; -.
DR   KEGG; spo:SPBC1198.07c; -.
DR   PomBase; SPBC1198.07c; -.
DR   VEuPathDB; FungiDB:SPBC1198.07c; -.
DR   eggNOG; ENOG502QSWP; Eukaryota.
DR   HOGENOM; CLU_025694_1_2_1; -.
DR   InParanoid; Q9P6I3; -.
DR   OMA; WFWWLSG; -.
DR   PRO; PR:Q9P6I3; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:PomBase.
DR   GO; GO:0008496; F:mannan endo-1,6-alpha-mannosidase activity; ISM:PomBase.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IBA:GO_Central.
DR   Gene3D; 1.50.10.20; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR005198; Glyco_hydro_76.
DR   InterPro; IPR014480; Mannan-1_6-alpha_mannosidase.
DR   PANTHER; PTHR12145:SF40; MANNAN ENDO-1,6-ALPHA-MANNOSIDASE C1198.07C-RELATED; 1.
DR   PANTHER; PTHR12145; UNCHARACTERIZED; 1.
DR   Pfam; PF03663; Glyco_hydro_76; 1.
DR   PIRSF; PIRSF016302; Man_a_manosd; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..442
FT                   /note="Putative mannan endo-1,6-alpha-mannosidase
FT                   C1198.07c"
FT                   /id="PRO_0000012130"
FT   TOPO_DOM        20..421
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
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        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   442 AA;  48877 MW;  E5D2F9EEAFCF749A CRC64;
     MRYLSFFFEF FFLFSFAFAF DFDVTSDDSI NSALTTVTDG MLNYYQSTSH TFTAYWWMTG
     AGLNSMTDTY AATGNTTHLD MLISALVANK GDNNDYAPNS EKFDLGNDDQ GIWGLSAMSA
     AEVNMTTGDS SASFTELAQA VFNEIMSRWD TSSCGGGVRW QIYSFNNGYS YKNSISNGIL
     FQLAARLARY TNNDTYVDLA QKVWDWSTTV GFVDLDDYTV YDGASVTSNC SSITNEQWSY
     NVGVYLAGTA FLYNYTNGSS VWQTHMEGLM NKALDYYFTS DKIIYEPSCE PTESCNSDQT
     AFKGMLARFL GYTMQLAPYT VETILPYIQS SAEAAALACS GGSDGVTCGY MWYWNNGTWD
     DHYGLGEQIS AVETFQALLA QQSATILTLD TGASSESNPD AGTDDGDTVT ITPATKSDKG
     WAGFLTFAFS FVFLLFSIWL YF
//