ANP1_SCHPO
ID ANP1_SCHPO Reviewed; 430 AA.
AC O74745; Q9US67;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Mannan polymerase II complex anp1 subunit;
DE Short=M-Pol II subunit anp1;
GN Name=anp1; ORFNames=SPBC1734.04;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 214-414, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=18184749; DOI=10.1091/mbc.e07-07-0663;
RA Vjestica A., Tang X.Z., Oliferenko S.;
RT "The actomyosin ring recruits early secretory compartments to the division
RT site in fission yeast.";
RL Mol. Biol. Cell 19:1125-1138(2008).
CC -!- FUNCTION: The M-Pol II complex possesses alpha-1,6-mannosyltransferase
CC activity and is probably involved in the elongation of the mannan
CC backbone of N-linked glycans on cell wall and periplasmic proteins.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the M-Pol II complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P32629}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P32629}. Note=Cis-Golgi (PubMed:18184749).
CC Recycles between endoplasmic reticulum and Golgi (By similarity).
CC {ECO:0000250|UniProtKB:P32629, ECO:0000269|PubMed:18184749}.
CC -!- SIMILARITY: Belongs to the ANP1/MMN9/VAN1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21290.1; -; Genomic_DNA.
DR EMBL; AB028011; BAA87315.1; -; Genomic_DNA.
DR PIR; T39651; T39651.
DR RefSeq; NP_595421.2; NM_001021328.3.
DR AlphaFoldDB; O74745; -.
DR SMR; O74745; -.
DR BioGRID; 276240; 2.
DR STRING; 4896.SPBC1734.04.1; -.
DR CAZy; GT62; Glycosyltransferase Family 62.
DR iPTMnet; O74745; -.
DR MaxQB; O74745; -.
DR PaxDb; O74745; -.
DR PRIDE; O74745; -.
DR EnsemblFungi; SPBC1734.04.1; SPBC1734.04.1:pep; SPBC1734.04.
DR GeneID; 2539685; -.
DR KEGG; spo:SPBC1734.04; -.
DR PomBase; SPBC1734.04; anp1.
DR VEuPathDB; FungiDB:SPBC1734.04; -.
DR eggNOG; ENOG502QVDT; Eukaryota.
DR HOGENOM; CLU_017872_0_0_1; -.
DR InParanoid; O74745; -.
DR OMA; EEGPLAH; -.
DR PhylomeDB; O74745; -.
DR PRO; PR:O74745; -.
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:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:PomBase.
DR GO; GO:0000136; C:mannan polymerase complex; IPI:PomBase.
DR GO; GO:0140497; C:mannan polymerase II complex; ISO:PomBase.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:PomBase.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:PomBase.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..430
FT /note="Mannan polymerase II complex anp1 subunit"
FT /id="PRO_0000193673"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..57
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..430
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 430 AA; 48991 MW; 48A48634005F6C66 CRC64;
MKANRDFGRD GGPFSITPNR FQPKSSGNPI FRQKTIRTVG IIALTLVLFL FFHRSFFSSF
GEFPSFSSTA NAPNSDVQEY DLRKVMNAKF TGDYSPKEKV LICAPLRNAA EHLNMFFGHM
NNLTYPHELI DLAFLISDTD DNTLEVLKQH LDAIQNDEDE SKHFNNVLIM LKDFGAIFGQ
EFSDRHGFAA QGPRRKLMAR ARNWLLSAAI QPYHSWVYWR DVDVETAPNT ILEDLMRHDK
DIIVPNVYRP LPDWLGNEQP YDLNSWAESE TALQLADTLG EDDVIVEGYA EYATWRPHLA
YLRDPNGDPS VEMPLDGIGG VSIMSKAKVH LEGCEFPAFS FEKHAETEGF GKMAKRMGFS
VYGLPHYVIW HIYEPSDDDK RIMAEMERER KEREAAELEE AKKYQTAGFT QPDDQGAEEG
PLAHADDHVD
