Calcium-transporting ATPase 1 - Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Calcium-transporting ATPase 1
EC=3.6.3.8

Alternative name(s):
P-type calcium ATPase

Gene names

Name:	PMR1
Synonyms:	SCA1
Ordered Locus Names:	YALI0E09471g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	928 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Has a role in the secretory pathway.
Catalytic activity	ATP + H₂O + Ca²⁺[side 1] = ADP + phosphate + Ca²⁺[side 2].
Subcellular location	Golgi apparatus membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. [View classification]

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Golgi apparatus Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Magnesium Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-transporting ATPase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 928

928

Calcium-transporting ATPase 1

PRO_0000046230

Regions

Transmembrane

81 – 101

21

Helical; Potential

Transmembrane

105 – 125

21

Helical; Potential

Transmembrane

271 – 291

21

Helical; Potential

Transmembrane

306 – 326

21

Helical; Potential

Transmembrane

718 – 738

21

Helical; Potential

Transmembrane

750 – 770

21

Helical; Potential

Transmembrane

799 – 819

21

Helical; Potential

Transmembrane

860 – 880

21

Helical; Potential

Transmembrane

887 – 907

21

Helical; Potential

Sites

Active site

353

1

4-aspartylphosphate intermediate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O43108 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: CBA53B0DD075EBE7
Show »

FASTA

928

100,051

        10         20         30         40         50         60 
MDSHTSTEGV PLSETNNRSH ATPSAQYCQM TVEETCSKLQ TNPETGLTSS QEAMHRRDIH 

        70         80         90        100        110        120 
GSNEFAQEEE DSLIKKFFEQ FSENPLLLLL IGAAAVSFFM GNHDDAISIT LAILIVTTVG 

       130        140        150        160        170        180 
FVQEYRSEKS LEALNKLVPP EAHLIRAGNS QTVLASTLVP GDLVEFSVGD RIPADCRIVK 

       190        200        210        220        230        240 
AVHLSIDESN LTGETTPVTK DTNPVTGTPP IGLADRTNTA YMGTLVRDGN GTGIVVGTGS 

       250        260        270        280        290        300 
HTAFGAVYDM VSEISTPKTP LQASMDNLGK DLSLVSFGVI GVICLIGMFQ GRDWLEMFTI 

       310        320        330        340        350        360 
GVSLAVAAIP EGLPIIVTVT LALGVLRMSR QKAIVRKLPS VETLGSVNVI CSDKTGTLTR 

       370        380        390        400        410        420 
NHMSCTTCWT VDMGDLANAV TLKPGQSHTE ADPKAVAALK NSVSLANMLK VGNLCNNSKF 

       430        440        450        460        470        480 
NREAGHLVGN ATDIALIEVL DYFGLEDTRE TRKRVAEVPF SSSRKWMLTS TTTGDSSTPM 

       490        500        510        520        530        540 
ISVKGAGEVI APFCEYYCKK DGKTAPFNDD MRKKVTEIAS EMSNDGLRII AFAYKQGKYE 

       550        560        570        580        590        600 
EGSEEAPEGL VFAGLMGLYD PPRPDVPRAI RRLTTGGVRV VMITGDSAAT ALSIGRRIGM 

       610        620        630        640        650        660 
PLMPGTQSVV EGSKLATMSD QALDECLQTA SIFARTSPED KMKIVKGFQR RGDVVAMTGD 

       670        680        690        700        710        720 
GVNDAPALKL ADIGIAMGQG GTDVAKEAAD MILTDDDFAT ILSAIEEGKG IFNNIRNFIT 

       730        740        750        760        770        780 
FQLSTSMAAL SIVAVATIMG LENPLNPMQI LWINILMDGP PAQSLGVEPV DPDVMNKPPR 

       790        800        810        820        830        840 
PRNEKVMTPD LVKKCVEAAV IILVGTMLVY VTQMQDGVID KRDTTMTFTC FVFYDMFNAL 

       850        860        870        880        890        900 
ACRSATKSVF EIGFFSNKMF LYACGASIIG QLAVVYVPFL QSVFQTEALS VKDLLSLVLI 

       910        920 
SSSVWILDEA KKYFLKSRST NNYTNSVV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of YlPMR1, a S. cerevisiae PMR1 homologue encoding a novel P-type secretory pathway Ca2+ ATPase, in the yeast Yarrowia lipolytica." Park C.S., Kim J.-Y., Crispino C., Chang C.C., Ryu D.D.Y. Gene 206:107-116(1998) [PubMed: 9461422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U75447 Genomic DNA. Translation: AAC03419.1. CR382131 Genomic DNA. Translation: CAG79326.1.
RefSeq	XP_503736.1. XM_503736.1.
3D structure databases
ProteinModelPortal	O43108.
ModBase	Search...
Protein-protein interaction databases
STRING	O43108.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2911589.
GenomeReviews	Gene locus YALI0E09471g in contig CR382131_GR.
KEGG	yli:YALI0E09471g.
Phylogenomic databases
eggNOG	fuNOG04517.
HOGENOM	HBG456486.
OMA	VYTHEML.
OrthoDB	EOG498Z7V.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR006413. ATPase_P-typ_Ca-transp_PMR1. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits.
KO	K01537.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01522. ATPase-IIA2_Ca. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATC1_YARLI

Accession

Primary (citable) accession number: O43108

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents