Reviewed, UniProtKB/Swiss-Prot P32629 (ANP1_YEAST)

Names and origin

Protein names

Recommended name:
    Mannan polymerase II complex ANP1 subunit
      Short name=M-Pol II subunit ANP1
Alternative name(s):
    Aminonitrophenyl propanediol resistance protein

Gene names

Name:	ANP1
Synonyms:	GEM3
Ordered Locus Names:	YEL036C
ORF Names:	SYGP-ORF28

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the organization of the secretory pathway. Required to maintain a functional Golgi apparatus. The M-Pol II complex possesses alpha-1,6-mannosyltransferase activity and is probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins.
Subunit structure	Component of the M-Pol II complex composed of ANP1, MNN9, MNN10, MNN11 and HOC1. Ref.3 Ref.6
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Note: Cis-Golgi. Recycles between endoplasmic reticulum and Golgi. Ref.3 Ref.6 Ref.4 Ref.7
Sequence similarities	Belongs to the ANP1/MMN9/VAN1 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall mannoprotein biosynthetic process Ref.6 Traceable author statement. Source: UniProtKB protein amino acid N-linked glycosylation Ref.6 Inferred from direct assay. Source: SGD
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell alpha-1,6-mannosyltransferase complex Ref.3 Ref.6 Traceable author statement. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-1,6-mannosyltransferase activity Ref.6 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 500	500	Mannan polymerase II complex ANP1 subunit		PRO_0000193668
Regions
	Topological domain	1 – 15	15	Cytoplasmic Potential
	Transmembrane	16 – 27	12	Signal-anchor for type II membrane protein
	Topological domain	28 – 500	473	Lumenal Potential
	Compositional bias	446 – 473	28	Gln-rich
Experimental info
	Sequence conflict	220 – 224	5	HHDKD → QSGQGN in AAD13971. Ref.1
	Sequence conflict	220 – 224	5	HHDKD → QSGQGN in AAA34426. Ref.1
	Sequence conflict	313	1	F → L in AAD13971. Ref.1
	Sequence conflict	313	1	F → L in AAA34426. Ref.1
	Sequence conflict	313	1	F → L in AAB28440. Ref.1
	Sequence conflict	313	1	F → L in AAA34937. Ref.1
	Sequence conflict	472 – 500	29	PQGKP…DPDRN → RRGNLLMTTTRTRKNILKKF H in AAD13971. Ref.1
	Sequence conflict	472 – 500	29	PQGKP…DPDRN → RRGNLLMTTTRTRKNILKKF H in AAA34426. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32629-1 [UniParc]. Last modified February 1, 1995. Version 3. Checksum: 845B395CE548CD14	FASTA	500	58,182
	10 20 30 40 50 60 MKYNNRKLSF NPTTVSIAGT LLTVFFLTRL VLSFFSISLF QLVTFQGIFK PYVPDFKNTP 70 80 90 100 110 120 SVEFYDLRNY QGNKDGWQQG DRILFCVPLR DASEHLPMFF NHLNTMTYPH NLIDLSFLVS 130 140 150 160 170 180 DSSDNTMGVL LSNLQMAQSQ QDKSKRFGNI EIYEKDFGQI IGQSFSDRHG FGAQGPRRKL 190 200 210 220 230 240 MARARNWLGS VALKPYHSWV YWRDVDVETI PTTIMEDLMH HDKDVIVPNV WRPLPDWLGN 250 260 270 280 290 300 IQPYDLNSWK ESEGGLQLAD SLDEDAVIVE GYPEYATWRP HLAYMRDPNG NPEDEMELDG 310 320 330 340 350 360 IGGVSILAKA KVFRTGSHFP AFSFEKHAET EAFGRLSRRM NYNVIGLPHY VIWHIYEPSS 370 380 390 400 410 420 DDLKHMAWMA EEEKRKLEEE RIREFYNKIW EIGFEDVRDQ WNEERDSILK NIDSTLNNKV 430 440 450 460 470 480 TVDWSEEGDG SELVDSKGDF VSPNNQQQQQ QQQQQQQQQQ QQQQQQQLDG NPQGKPLDDN 490 500 DKNKKKHPKE VPLDFDPDRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of Saccharomyces cerevisiae share a common ancestry." Melnick L., Sherman F. J. Mol. Biol. 233:372-388(1993) [PubMed: 8411151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B-6441.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Novel membrane protein complexes for protein glycosylation in the yeast Golgi apparatus." Hashimoto H., Yoda K. Biochem. Biophys. Res. Commun. 241:682-686(1997) [PubMed: 9434768] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, SUBCELLULAR LOCATION, SUBUNIT.
[4]	"Proteins in the early Golgi compartment of Saccharomyces cerevisiae immunoisolated by Sed5p." Cho J.-H., Noda Y., Yoda K. FEBS Lett. 469:151-154(2000) [PubMed: 10713261] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-5, SUBCELLULAR LOCATION.
[5]	"The functioning of the yeast Golgi apparatus requires an ER protein encoded by ANP1, a member of a new family of genes affecting the secretory pathway." Chapman R.E., Munro S. EMBO J. 13:4896-4907(1994) [PubMed: 7957057] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity." Jungmann J., Munro S. EMBO J. 17:423-434(1998) [PubMed: 9430634] [Abstract] Cited for: ACTIVITY OF M-POL II COMPLEX, SUBUNIT, SUBCELLULAR LOCATION.
[7]	"Active recycling of yeast Golgi mannosyltransferase complexes through the endoplasmic reticulum." Todorow Z., Spang A., Carmack E., Yates J., Schekman R. Proc. Natl. Acad. Sci. U.S.A. 97:13643-13648(2000) [PubMed: 11095735] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S65964 Genomic DNA. Translation: AAD13971.1. L22171 Genomic DNA. Translation: AAA34426.1. S66114 mRNA. Translation: AAB28440.1. L22173 Genomic DNA. Translation: AAA34937.1. U18779 Genomic DNA. Translation: AAB65006.1.
PIR	S50508.
RefSeq	NP_010878.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:845N.
IntAct	P32629. 23 interactions.
Protein family/group databases
CAZy	GT62. Glycosyltransferase Family 62.
Proteomic databases
PRIDE	P32629.
Genome annotation databases
Ensembl	YEL036C. Saccharomyces cerevisiae. [Contig view]
GeneID	856675.
GenomeReviews	Gene locus YEL036C in contig U00092_GR.
KEGG	sce:YEL036C.
NMPDR	fig|4932.3.peg.1929.
Organism-specific databases
CYGD	YEL036c.
SGD	S000000762. ANP1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P32629.
OMA	P32629. VVGLPHY.
Gene expression databases
GermOnline	YEL036C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005109. Anp1. [Graphical view]
Pfam	PF03452. Anp1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	982696.

Entry information

Entry name

ANP1_YEAST

Accession

Primary (citable) accession number: P32629

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)