O75185 (AT2C2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calcium-transporting ATPase type 2C member 2
Short name=ATPase 2C2
EC=3.6.3.8

Alternative name(s):
Secretory pathway Ca(2+)-ATPase 2

Gene names

Name:	ATP2C2
Synonyms:	KIAA0703, SPCA2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	946 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium By similarity.
Catalytic activity	ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. [View classification]
Sequence caution	The sequence BAA31678.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ion transmembrane transport Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome 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: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ORAI1	Q96D31	10	EBI-2939806,EBI-2291476

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75185-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O75185-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: MVEGRVSEFL...QKEDLARAFC → MLHFHLLKFK...SELVPDLSFQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 946	946	Calcium-transporting ATPase type 2C member 2		PRO_0000046207
Regions
	Topological domain	1 – 106	106	Cytoplasmic Potential
	Transmembrane	107 – 127	21	Helical; Name=1; Potential
	Topological domain	128 – 129	2	Extracellular Potential
	Transmembrane	130 – 150	21	Helical; Name=2; Potential
	Topological domain	151 – 231	81	Cytoplasmic Potential
	Transmembrane	232 – 252	21	Helical; Name=3; Potential
	Topological domain	253 – 293	41	Extracellular Potential
	Transmembrane	294 – 314	21	Helical; Name=4; Potential
	Topological domain	315 – 331	17	Cytoplasmic Potential
	Transmembrane	332 – 352	21	Helical; Name=5; Potential
	Topological domain	353 – 750	398	Extracellular Potential
	Transmembrane	751 – 771	21	Helical; Name=6; Potential
	Topological domain	772 – 804	33	Cytoplasmic Potential
	Transmembrane	805 – 825	21	Helical; Name=7; Potential
	Topological domain	826 – 837	12	Extracellular Potential
	Transmembrane	838 – 855	18	Helical; Name=8; Potential
	Topological domain	856 – 874	19	Cytoplasmic Potential
	Transmembrane	875 – 895	21	Helical; Name=9; Potential
	Topological domain	896 – 905	10	Extracellular Potential
	Transmembrane	906 – 926	21	Helical; Name=10; Potential
	Topological domain	927 – 946	20	Cytoplasmic Potential
	Compositional bias	114 – 119	6	Poly-Leu
Sites
	Active site	379	1	4-aspartylphosphate intermediate By similarity
	Metal binding	332	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	333	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	335	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	337	1	Calcium 2 By similarity
	Metal binding	674	1	Magnesium By similarity
	Metal binding	678	1	Magnesium By similarity
	Metal binding	768	1	Calcium 2 By similarity
	Metal binding	772	1	Calcium 2 By similarity
Amino acid modifications
	Modified residue	264	1	Phosphothreonine Ref.6
	Modified residue	267	1	Phosphoserine Ref.6
	Modified residue	268	1	Phosphoserine Ref.6
Natural variations
	Alternative sequence	1 – 70	70	MVEGR…ARAFC → MLHFHLLKFKTRVVFSAVII MVTGLCLFLLSLPHLHGVFE QVPAPWWTSLCPWPIMEAAA FQSGSLYPVASFLAAPMSEL VPDLSFQ in isoform 2.		VSP_035989
	Natural variant	165	1	M → L. Ref.3 Ref.4 Corresponds to variant rs247818 [ dbSNP | Ensembl ].		VAR_059137
	Natural variant	411	1	G → S. Corresponds to variant rs2303853 [ dbSNP | Ensembl ].		VAR_047935
	Natural variant	466	1	M → L. Ref.3 Corresponds to variant rs247897 [ dbSNP | Ensembl ].		VAR_047936
	Natural variant	907	1	L → P. Corresponds to variant rs16973859 [ dbSNP | Ensembl ].		VAR_047937
Experimental info
Isoform 2:
	Sequence conflict	12	1	R → I in BAA31678. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: AEB061210ED09D1C	FASTA	946	103,187
	10 20 30 40 50 60 MVEGRVSEFL KKLGFSGGGR QYQALEKDEE EALIDEQSEL KAIEKEKKVT ALPPKEACKC 70 80 90 100 110 120 QKEDLARAFC VDLHTGLSEF SVTQRRLAHG WNEFVADNSE PVWKKYLDQF KNPLILLLLG 130 140 150 160 170 180 SALVSVLTKE YEDAVSIATA VLVVVTVAFI QEYRSEKSLE ELTKMVPPEC NCLREGKLQH 190 200 210 220 230 240 LLARELVPGD VVSLSIGDRI PADIRLTEVT DLLVDESSFT GEAEPCSKTD SPLTGGGDLT 250 260 270 280 290 300 TLSNIVFMGT LVQYGRGQGV VIGTGESSQF GEVFKMMQAE ETPKTPLQKS MDRLGKQLTL 310 320 330 340 350 360 FSFGIIGLIM LIGWSQGKQL LSMFTIGVSL AVAAIPEGLP IVVMVTLVLG VLRMAKKRVI 370 380 390 400 410 420 VKKLPIVETL GCCSVLCSDK TGTLTANEMT VTQLVTSDGL RAEVSGVGYD GQGTVCLLPS 430 440 450 460 470 480 KEVIKEFSNV SVGKLVEAGC VANNAVIRKN AVMGQPTEGA LMALAMKMDL SDIKNSYIRK 490 500 510 520 530 540 KEIPFSSEQK WMAVKCSLKT EDQEDIYFMK GALEEVIRYC TMYNNGGIPL PLTPQQRSFC 550 560 570 580 590 600 LQEEKRMGSL GLRVLALASG PELGRLTFLG LVGIIDPPRV GVKEAVQVLS ESGVSVKMIT 610 620 630 640 650 660 GDALETALAI GRNIGLCNGK LQAMSGEEVD SVEKGELADR VGKVSVFFRT SPKHKLKIIK 670 680 690 700 710 720 ALQESGAIVA MTGDGVNDAV ALKSADIGIA MGQTGTDVSK EAANMILVDD DFSAIMNAVE 730 740 750 760 770 780 EGKGIFYNIK NFVRFQLSTS ISALSLITLS TVFNLPSPLN AMQILWINII MDGPPAQSLG 790 800 810 820 830 840 VEPVDKDAFR QPPRSVRDTI LSRALILKIL MSAAIIISGT LFIFWKEMPE DRASTPRTTT 850 860 870 880 890 900 MTFTCFVFFD LFNALTCRSQ TKLIFEIGFL RNHMFLYSVL GSILGQLAVI YIPPLQRVFQ 910 920 930 940 TENLGALDLL FLTGLASSVF ILSELLKLCE KYCCSPKRVQ MHPEDV
	Isoform 2 [UniParc]. Checksum: A82EA87032866F4D	FASTA	963	105,041
	10 20 30 40 50 60 MLHFHLLKFK TRVVFSAVII MVTGLCLFLL SLPHLHGVFE QVPAPWWTSL CPWPIMEAAA 70 80 90 100 110 120 FQSGSLYPVA SFLAAPMSEL VPDLSFQVDL HTGLSEFSVT QRRLAHGWNE FVADNSEPVW 130 140 150 160 170 180 KKYLDQFKNP LILLLLGSAL VSVLTKEYED AVSIATAVLV VVTVAFIQEY RSEKSLEELT 190 200 210 220 230 240 KMVPPECNCL REGKLQHLLA RELVPGDVVS LSIGDRIPAD IRLTEVTDLL VDESSFTGEA 250 260 270 280 290 300 EPCSKTDSPL TGGGDLTTLS NIVFMGTLVQ YGRGQGVVIG TGESSQFGEV FKMMQAEETP 310 320 330 340 350 360 KTPLQKSMDR LGKQLTLFSF GIIGLIMLIG WSQGKQLLSM FTIGVSLAVA AIPEGLPIVV 370 380 390 400 410 420 MVTLVLGVLR MAKKRVIVKK LPIVETLGCC SVLCSDKTGT LTANEMTVTQ LVTSDGLRAE 430 440 450 460 470 480 VSGVGYDGQG TVCLLPSKEV IKEFSNVSVG KLVEAGCVAN NAVIRKNAVM GQPTEGALMA 490 500 510 520 530 540 LAMKMDLSDI KNSYIRKKEI PFSSEQKWMA VKCSLKTEDQ EDIYFMKGAL EEVIRYCTMY 550 560 570 580 590 600 NNGGIPLPLT PQQRSFCLQE EKRMGSLGLR VLALASGPEL GRLTFLGLVG IIDPPRVGVK 610 620 630 640 650 660 EAVQVLSESG VSVKMITGDA LETALAIGRN IGLCNGKLQA MSGEEVDSVE KGELADRVGK 670 680 690 700 710 720 VSVFFRTSPK HKLKIIKALQ ESGAIVAMTG DGVNDAVALK SADIGIAMGQ TGTDVSKEAA 730 740 750 760 770 780 NMILVDDDFS AIMNAVEEGK GIFYNIKNFV RFQLSTSISA LSLITLSTVF NLPSPLNAMQ 790 800 810 820 830 840 ILWINIIMDG PPAQSLGVEP VDKDAFRQPP RSVRDTILSR ALILKILMSA AIIISGTLFI 850 860 870 880 890 900 FWKEMPEDRA STPRTTTMTF TCFVFFDLFN ALTCRSQTKL IFEIGFLRNH MFLYSVLGSI 910 920 930 940 950 960 LGQLAVIYIP PLQRVFQTEN LGALDLLFLT GLASSVFILS ELLKLCEKYC CSPKRVQMHP EDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The secretory pathway Ca2+/Mn2+-ATPase 2 is a Golgi-localized pump with high affinity for Ca2+ ions." Vanoevelen J., Dode L., Van Baelen K., Fairclough R.J., Missiaen L., Raeymaekers L., Wuytack F. J. Biol. Chem. 280:22800-22808(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS LEU-165 AND LEU-466. Tissue: Prostate.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-165. Tissue: Small intestine.
[5]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-264; SER-267 AND SER-268, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY791884 mRNA. Translation: AAV54193.1. AB014603 mRNA. Translation: BAA31678.2. Different initiation. AK300526 mRNA. Translation: BAG62238.1. CR749829 mRNA. Translation: CAH18686.1. AC010551 Genomic DNA. No translation available. AC022165 Genomic DNA. No translation available.
IPI	IPI00006653. IPI00915432.
RefSeq	NP_055676.2. NM_014861.2.
UniGene	Hs.6168.
3D structure databases
ProteinModelPortal	O75185.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75185. 1 interaction.
STRING	9606.ENSP00000262429.
Protein family/group databases
TCDB	3.A.3.2.9. P-type ATPase (P-ATPase) superfamily.
PTM databases
PhosphoSite	O75185.
Proteomic databases
PaxDb	O75185.
PRIDE	O75185.
Protocols and materials databases
DNASU	9914.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262429; ENSP00000262429; ENSG00000064270.
GeneID	9914.
KEGG	hsa:9914.
UCSC	uc002fhx.3. human. uc002fhy.3. human.
Organism-specific databases
CTD	9914.
GeneCards	GC16P084402.
H-InvDB	HIX0013295. HIX0013296.
HGNC	HGNC:29103. ATP2C2.
HPA	HPA052262.
MIM	613082. gene.
neXtProt	NX_O75185.
PharmGKB	PA162377204.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0474.
HOGENOM	HOG000265621.
HOVERGEN	HBG106478.
InParanoid	O75185.
KO	K01537.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	O75185.
Bgee	O75185.
CleanEx	HS_ATP2C2.
Genevestigator	O75185.
GermOnline	ENSG00000064270. Homo sapiens.
Family and domain databases
Gene3D	1.20.1110.10. 3 hits.
InterPro	IPR006413. ATPase_P-typ_Ca-transp_PMR1. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023299. ATPase_P-typ_cyto_domN. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR008250. ATPase_P-typ_transduc_dom_A. IPR001757. Cation_transp_P_typ_ATPase. IPR023214. HAD-like_dom. [Graphical view]
PANTHER	PTHR24093. PTHR24093. 1 hit.
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	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01522. ATPase-IIA2_Ca. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP2C2. human.
GenomeRNAi	9914.
NextBio	37400.
SOURCE	Search...

Entry information

Entry name

AT2C2_HUMAN

Accession

Primary (citable) accession number: O75185
Secondary accession number(s): B4DU76, Q5S053, Q68CQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.