ANP1_YEAST
ID ANP1_YEAST Reviewed; 500 AA.
AC P32629; D3DLL3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Mannan polymerase II complex ANP1 subunit;
DE Short=M-Pol II subunit ANP1;
DE AltName: Full=Aminonitrophenyl propanediol resistance protein;
GN Name=ANP1; Synonyms=GEM3; OrderedLocusNames=YEL036C; ORFNames=SYGP-ORF28;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B-6441;
RX PubMed=8411151; DOI=10.1006/jmbi.1993.1518;
RA Melnick L., Sherman F.;
RT "The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of
RT Saccharomyces cerevisiae share a common ancestry.";
RL J. Mol. Biol. 233:372-388(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 1-10, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9434768; DOI=10.1006/bbrc.1997.7888;
RA Hashimoto H., Yoda K.;
RT "Novel membrane protein complexes for protein glycosylation in the yeast
RT Golgi apparatus.";
RL Biochem. Biophys. Res. Commun. 241:682-686(1997).
RN [5]
RP PROTEIN SEQUENCE OF 1-5, AND SUBCELLULAR LOCATION.
RX PubMed=10713261; DOI=10.1016/s0014-5793(00)01268-0;
RA Cho J.-H., Noda Y., Yoda K.;
RT "Proteins in the early Golgi compartment of Saccharomyces cerevisiae
RT immunoisolated by Sed5p.";
RL FEBS Lett. 469:151-154(2000).
RN [6]
RP CHARACTERIZATION.
RX PubMed=7957057; DOI=10.1002/j.1460-2075.1994.tb06817.x;
RA Chapman R.E., Munro S.;
RT "The functioning of the yeast Golgi apparatus requires an ER protein
RT encoded by ANP1, a member of a new family of genes affecting the secretory
RT pathway.";
RL EMBO J. 13:4896-4907(1994).
RN [7]
RP ACTIVITY OF M-POL II COMPLEX, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9430634; DOI=10.1093/emboj/17.2.423;
RA Jungmann J., Munro S.;
RT "Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with
RT alpha-1,6-mannosyltransferase activity.";
RL EMBO J. 17:423-434(1998).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11095735; DOI=10.1073/pnas.250472397;
RA Todorow Z., Spang A., Carmack E., Yates J., Schekman R.;
RT "Active recycling of yeast Golgi mannosyltransferase complexes through the
RT endoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13643-13648(2000).
CC -!- FUNCTION: Involved in the organization of the secretory pathway.
CC Required to maintain a functional Golgi apparatus.
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 -!- SUBUNIT: Component of the M-Pol II complex composed of ANP1, MNN9,
CC MNN10, MNN11 and HOC1. {ECO:0000269|PubMed:9430634,
CC ECO:0000269|PubMed:9434768}.
CC -!- INTERACTION:
CC P32629; P47124: HOC1; NbExp=2; IntAct=EBI-2595, EBI-8430;
CC P32629; P50108: MNN10; NbExp=3; IntAct=EBI-2595, EBI-11043;
CC P32629; P46985: MNN11; NbExp=3; IntAct=EBI-2595, EBI-11052;
CC P32629; P39107: MNN9; NbExp=6; IntAct=EBI-2595, EBI-11082;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11095735}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:9434768}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:10713261, ECO:0000269|PubMed:9430634,
CC ECO:0000269|PubMed:9434768}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:9434768}. Note=Cis-Golgi (PubMed:9430634). Recycles
CC between endoplasmic reticulum and Golgi (PubMed:11095735).
CC {ECO:0000269|PubMed:11095735, ECO:0000269|PubMed:9430634}.
CC -!- SIMILARITY: Belongs to the ANP1/MMN9/VAN1 family. {ECO:0000305}.
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DR EMBL; S65964; AAD13971.1; -; Genomic_DNA.
DR EMBL; L22171; AAA34426.1; -; Genomic_DNA.
DR EMBL; S66114; AAB28440.1; -; mRNA.
DR EMBL; L22173; AAA34937.1; -; Genomic_DNA.
DR EMBL; U18779; AAB65006.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07617.1; -; Genomic_DNA.
DR PIR; S50508; S50508.
DR RefSeq; NP_010878.1; NM_001178851.1.
DR AlphaFoldDB; P32629; -.
DR SMR; P32629; -.
DR BioGRID; 36693; 670.
DR ComplexPortal; CPX-1839; alpha-1,6-mannosyltransferase complex, M-Pol II variant.
DR DIP; DIP-845N; -.
DR IntAct; P32629; 21.
DR MINT; P32629; -.
DR STRING; 4932.YEL036C; -.
DR CAZy; GT62; Glycosyltransferase Family 62.
DR MaxQB; P32629; -.
DR PaxDb; P32629; -.
DR PRIDE; P32629; -.
DR EnsemblFungi; YEL036C_mRNA; YEL036C; YEL036C.
DR GeneID; 856675; -.
DR KEGG; sce:YEL036C; -.
DR SGD; S000000762; ANP1.
DR VEuPathDB; FungiDB:YEL036C; -.
DR eggNOG; ENOG502QVDT; Eukaryota.
DR GeneTree; ENSGT00940000176370; -.
DR HOGENOM; CLU_017872_0_0_1; -.
DR InParanoid; P32629; -.
DR OMA; NVQGTAR; -.
DR BioCyc; MetaCyc:YEL036C-MON; -.
DR BioCyc; YEAST:YEL036C-MON; -.
DR PRO; PR:P32629; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32629; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:SGD.
DR GO; GO:0000136; C:mannan polymerase complex; IDA:SGD.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:SGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..500
FT /note="Mannan polymerase II complex ANP1 subunit"
FT /id="PRO_0000193668"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 28..500
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 424..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 220..224
FT /note="HHDKD -> QSGQGN (in Ref. 1; AAD13971/AAA34426)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="F -> L (in Ref. 1; AAD13971/AAA34426/AAB28440/
FT AAA34937)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..500
FT /note="PQGKPLDDNDKNKKKHPKEVPLDFDPDRN -> RRGNLLMTTTRTRKNILKK
FT FH (in Ref. 1; AAD13971/AAA34426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 58182 MW; 845B395CE548CD14 CRC64;
MKYNNRKLSF NPTTVSIAGT LLTVFFLTRL VLSFFSISLF QLVTFQGIFK PYVPDFKNTP
SVEFYDLRNY QGNKDGWQQG DRILFCVPLR DASEHLPMFF NHLNTMTYPH NLIDLSFLVS
DSSDNTMGVL LSNLQMAQSQ QDKSKRFGNI EIYEKDFGQI IGQSFSDRHG FGAQGPRRKL
MARARNWLGS VALKPYHSWV YWRDVDVETI PTTIMEDLMH HDKDVIVPNV WRPLPDWLGN
IQPYDLNSWK ESEGGLQLAD SLDEDAVIVE GYPEYATWRP HLAYMRDPNG NPEDEMELDG
IGGVSILAKA KVFRTGSHFP AFSFEKHAET EAFGRLSRRM NYNVIGLPHY VIWHIYEPSS
DDLKHMAWMA EEEKRKLEEE RIREFYNKIW EIGFEDVRDQ WNEERDSILK NIDSTLNNKV
TVDWSEEGDG SELVDSKGDF VSPNNQQQQQ QQQQQQQQQQ QQQQQQQLDG NPQGKPLDDN
DKNKKKHPKE VPLDFDPDRN
