Full text data of ATP11C
ATP11C
(ATPIG, ATPIQ)
[Confidence: high (present in two of the MS resources)]
Probable phospholipid-transporting ATPase IG; 3.6.3.1 (ATPase IQ; ATPase class VI type 11C)
Probable phospholipid-transporting ATPase IG; 3.6.3.1 (ATPase IQ; ATPase class VI type 11C)
Comments
Isoform Q8NB49-2 was detected.
Isoform Q8NB49-2 was detected.
UniProt
Q8NB49
ID AT11C_HUMAN Reviewed; 1132 AA.
AC Q8NB49; Q5JT69; Q5JT70; Q5JT71; Q5JT72; Q5JT73; Q6ZND5; Q6ZU50;
read moreAC Q6ZUP7; Q70IJ9; Q70IK0; Q8WX24;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Probable phospholipid-transporting ATPase IG;
DE EC=3.6.3.1;
DE AltName: Full=ATPase IQ;
DE AltName: Full=ATPase class VI type 11C;
GN Name=ATP11C; Synonyms=ATPIG, ATPIQ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP VARIANT TRP-114.
RC TISSUE=Liver;
RX PubMed=15533723; DOI=10.1016/j.ygeno.2004.08.003;
RA Andrew-Nesbit M., Bowl M.R., Harding B., Schlessinger D., Whyte M.P.,
RA Thakker R.V.;
RT "X-linked hypoparathyroidism region on Xq27 is evolutionarily
RT conserved with regions on 3q26 and 13q34 and contains a novel P-type
RT ATPase.";
RL Genomics 84:1060-1070(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-1132 (ISOFORM 4),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 543-1132 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 777-1132 (ISOFORM 2).
RC TISSUE=Brain, Fetal brain, Testis, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1108, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP INTERACTION WITH TMEM30A, AND SUBCELLULAR LOCATION.
RX PubMed=21914794; DOI=10.1074/jbc.M111.281006;
RA Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M.,
RA Nakayama K., Shin H.W.;
RT "ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
RT localizes to the trans-Golgi network in a CDC50 protein-independent
RT manner.";
RL J. Biol. Chem. 286:38159-38167(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-157 AND PRO-931.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
CC phosphate + phospholipid(Side 2).
CC -!- SUBUNIT: Interacts with TMEM30A, but not with TMEM30B.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane. Note=Efficient exit from the
CC endoplasmic reticulum requires the presence of TMEM30A. Some cell
CC membrane localization observed in the presence of TMEM30B.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8NB49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NB49-2; Sequence=VSP_007309;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8NB49-3; Sequence=VSP_013373;
CC Name=4;
CC IsoId=Q8NB49-4; Sequence=VSP_013374;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC (TC 3.A.3) family. Type IV subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03692.1; Type=Erroneous initiation;
CC Sequence=BAC86172.1; Type=Erroneous initiation;
CC Sequence=BAC86377.1; Type=Erroneous initiation;
CC Sequence=BAD18440.1; Type=Erroneous initiation;
CC Sequence=CAI39713.1; Type=Erroneous gene model prediction;
CC Sequence=CAI39714.1; Type=Erroneous gene model prediction;
CC Sequence=CAI39716.1; Type=Erroneous gene model prediction;
CC Sequence=CAI40418.1; Type=Erroneous gene model prediction;
CC Sequence=CAI41444.1; Type=Erroneous gene model prediction;
CC Sequence=CAI41445.1; Type=Erroneous gene model prediction;
CC Sequence=CAI41446.1; Type=Erroneous gene model prediction;
CC Sequence=CAI41447.1; Type=Erroneous gene model prediction;
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DR EMBL; AJ580093; CAE30472.1; -; mRNA.
DR EMBL; AJ580094; CAE30473.1; -; mRNA.
DR EMBL; AL161777; CAI39713.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL356785; CAI39713.1; JOINED; Genomic_DNA.
DR EMBL; AL161777; CAI39714.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL356785; CAI39714.1; JOINED; Genomic_DNA.
DR EMBL; AL161777; CAI39716.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL356785; CAI39716.1; JOINED; Genomic_DNA.
DR EMBL; AL590077; CAI39716.1; JOINED; Genomic_DNA.
DR EMBL; AL356785; CAI41444.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161777; CAI41444.1; JOINED; Genomic_DNA.
DR EMBL; AL356785; CAI41445.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161777; CAI41445.1; JOINED; Genomic_DNA.
DR EMBL; AL356785; CAI41446.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161777; CAI41446.1; JOINED; Genomic_DNA.
DR EMBL; AL590077; CAI41446.1; JOINED; Genomic_DNA.
DR EMBL; AL356785; CAI41447.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL590077; CAI40418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL356785; CAI40418.1; JOINED; Genomic_DNA.
DR EMBL; AL161777; CAI40418.1; JOINED; Genomic_DNA.
DR EMBL; AK091552; BAC03692.1; ALT_INIT; mRNA.
DR EMBL; AK125474; BAC86172.1; ALT_INIT; mRNA.
DR EMBL; AK125986; BAC86377.1; ALT_INIT; mRNA.
DR EMBL; AK131262; BAD18440.1; ALT_INIT; mRNA.
DR RefSeq; NP_001010986.1; NM_001010986.2.
DR RefSeq; NP_775965.2; NM_173694.4.
DR UniGene; Hs.88252; -.
DR ProteinModelPortal; Q8NB49; -.
DR SMR; Q8NB49; 390-702.
DR PhosphoSite; Q8NB49; -.
DR DMDM; 62512178; -.
DR PaxDb; Q8NB49; -.
DR PRIDE; Q8NB49; -.
DR DNASU; 286410; -.
DR Ensembl; ENST00000327569; ENSP00000332756; ENSG00000101974.
DR Ensembl; ENST00000359686; ENSP00000352715; ENSG00000101974.
DR Ensembl; ENST00000361648; ENSP00000355165; ENSG00000101974.
DR Ensembl; ENST00000370543; ENSP00000359574; ENSG00000101974.
DR GeneID; 286410; -.
DR KEGG; hsa:286410; -.
DR UCSC; uc004faz.3; human.
DR CTD; 286410; -.
DR GeneCards; GC0XM138808; -.
DR HGNC; HGNC:13554; ATP11C.
DR HPA; HPA030830; -.
DR MIM; 300516; gene.
DR neXtProt; NX_Q8NB49; -.
DR PharmGKB; PA25103; -.
DR eggNOG; COG0474; -.
DR HOVERGEN; HBG050601; -.
DR InParanoid; Q8NB49; -.
DR KO; K01530; -.
DR OMA; PRLYMKI; -.
DR OrthoDB; EOG7HHWRB; -.
DR PhylomeDB; Q8NB49; -.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GenomeRNAi; 286410; -.
DR NextBio; 96190; -.
DR PRO; PR:Q8NB49; -.
DR Bgee; Q8NB49; -.
DR Genevestigator; Q8NB49; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0045332; P:phospholipid translocation; NAS:UniProtKB.
DR Gene3D; 2.70.150.10; -; 2.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR006539; ATPase_P-typ_Plipid-transp.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
DR InterPro; IPR001757; Cation_transp_P_typ_ATPase.
DR InterPro; IPR023214; HAD-like_dom.
DR PANTHER; PTHR24092; PTHR24092; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR SUPFAM; SSF56784; SSF56784; 3.
DR SUPFAM; SSF81660; SSF81660; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
KW Endoplasmic reticulum; Hydrolase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 1132 Probable phospholipid-transporting ATPase
FT IG.
FT /FTId=PRO_0000046373.
FT TOPO_DOM 1 66 Cytoplasmic (Potential).
FT TRANSMEM 67 85 Helical; (Potential).
FT TOPO_DOM 86 86 Extracellular (Potential).
FT TRANSMEM 87 107 Helical; (Potential).
FT TOPO_DOM 108 290 Cytoplasmic (Potential).
FT TRANSMEM 291 311 Helical; (Potential).
FT TOPO_DOM 312 346 Extracellular (Potential).
FT TRANSMEM 347 367 Helical; (Potential).
FT TOPO_DOM 368 879 Cytoplasmic (Potential).
FT TRANSMEM 880 900 Helical; (Potential).
FT TOPO_DOM 901 908 Extracellular (Potential).
FT TRANSMEM 909 929 Helical; (Potential).
FT TOPO_DOM 930 955 Cytoplasmic (Potential).
FT TRANSMEM 956 976 Helical; (Potential).
FT TOPO_DOM 977 995 Extracellular (Potential).
FT TRANSMEM 996 1016 Helical; (Potential).
FT TOPO_DOM 1017 1026 Cytoplasmic (Potential).
FT TRANSMEM 1027 1047 Helical; (Potential).
FT TOPO_DOM 1048 1069 Extracellular (Potential).
FT TRANSMEM 1070 1090 Helical; (Potential).
FT TOPO_DOM 1091 1132 Cytoplasmic (Potential).
FT ACT_SITE 412 412 4-aspartylphosphate intermediate (By
FT similarity).
FT METAL 819 819 Magnesium (By similarity).
FT METAL 823 823 Magnesium (By similarity).
FT MOD_RES 445 445 Phosphoserine.
FT MOD_RES 1108 1108 Phosphoserine.
FT VAR_SEQ 1100 1132 RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> VHHL
FT ISSSA (in isoform 2).
FT /FTId=VSP_007309.
FT VAR_SEQ 1100 1132 RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> NPNL
FT ELPMLLSYKHTDSGYS (in isoform 3).
FT /FTId=VSP_013373.
FT VAR_SEQ 1100 1132 RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> VTKR
FT LPSSGTSAIFMLSQTSSNHSFSWSE (in isoform 4).
FT /FTId=VSP_013374.
FT VARIANT 114 114 C -> W (in dbSNP:rs2491014).
FT /FTId=VAR_021827.
FT VARIANT 157 157 T -> I (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036501.
FT VARIANT 522 522 Y -> C (in dbSNP:rs17281983).
FT /FTId=VAR_055546.
FT VARIANT 931 931 Q -> P (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036502.
FT VARIANT 972 972 V -> M (in dbSNP:rs55724992).
FT /FTId=VAR_061036.
FT CONFLICT 537 537 L -> P (in Ref. 3; BAC86377).
FT CONFLICT 873 873 I -> V (in Ref. 3; BAC86377).
SQ SEQUENCE 1132 AA; 129477 MW; 74B63B20A5C6E49D CRC64;
MQMVPSLPPA SECAGEEKRV GTRTVFVGNH PVSETEAYIA QRFCDNRIVS SKYTLWNFLP
KNLFEQFRRI ANFYFLIIFL VQVTVDTPTS PVTSGLPLFF VITVTAIKQG YEDCLRHRAD
NEVNKSTVYI IENAKRVRKE SEKIKVGDVV EVQADETFPC DLILLSSCTT DGTCYVTTAS
LDGESNCKTH YAVRDTIALC TAESIDTLRA AIECEQPQPD LYKFVGRINI YSNSLEAVAR
SLGPENLLLK GATLKNTEKI YGVAVYTGME TKMALNYQGK SQKRSAVEKS INAFLIVYLF
ILLTKAAVCT TLKYVWQSTP YNDEPWYNQK TQKERETLKV LKMFTDFLSF MVLFNFIIPV
SMYVTVEMQK FLGSFFISWD KDFYDEEINE GALVNTSDLN EELGQVDYVF TDKTGTLTEN
SMEFIECCID GHKYKGVTQE VDGLSQTDGT LTYFDKVDKN REELFLRALC LCHTVEIKTN
DAVDGATESA ELTYISSSPD EIALVKGAKR YGFTFLGNRN GYMRVENQRK EIEEYELLHT
LNFDAVRRRM SVIVKTQEGD ILLFCKGADS AVFPRVQNHE IELTKVHVER NAMDGYRTLC
VAFKEIAPDD YERINRQLIE AKMALQDREE KMEKVFDDIE TNMNLIGATA VEDKLQDQAA
ETIEALHAAG LKVWVLTGDK METAKSTCYA CRLFQTNTEL LELTTKTIEE SERKEDRLHE
LLIEYRKKLL HEFPKSTRSF KKAWTEHQEY GLIIDGSTLS LILNSSQDSS SNNYKSIFLQ
ICMKCTAVLC CRMAPLQKAQ IVRMVKNLKG SPITLSIGDG ANDVSMILES HVGIGIKGKE
GRQAARNSDY SVPKFKHLKK LLLAHGHLYY VRIAHLVQYF FYKNLCFILP QFLYQFFCGF
SQQPLYDAAY LTMYNICFTS LPILAYSLLE QHINIDTLTS DPRLYMKISG NAMLQLGPFL
YWTFLAAFEG TVFFFGTYFL FQTASLEENG KVYGNWTFGT IVFTVLVFTV TLKLALDTRF
WTWINHFVIW GSLAFYVFFS FFWGGIIWPF LKQQRMYFVF AQMLSSVSTW LAIILLIFIS
LFPEILLIVL KNVRRRSARR NLSCRRASDS LSARPSVRPL LLRTFSDESN VL
//
ID AT11C_HUMAN Reviewed; 1132 AA.
AC Q8NB49; Q5JT69; Q5JT70; Q5JT71; Q5JT72; Q5JT73; Q6ZND5; Q6ZU50;
read moreAC Q6ZUP7; Q70IJ9; Q70IK0; Q8WX24;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Probable phospholipid-transporting ATPase IG;
DE EC=3.6.3.1;
DE AltName: Full=ATPase IQ;
DE AltName: Full=ATPase class VI type 11C;
GN Name=ATP11C; Synonyms=ATPIG, ATPIQ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP VARIANT TRP-114.
RC TISSUE=Liver;
RX PubMed=15533723; DOI=10.1016/j.ygeno.2004.08.003;
RA Andrew-Nesbit M., Bowl M.R., Harding B., Schlessinger D., Whyte M.P.,
RA Thakker R.V.;
RT "X-linked hypoparathyroidism region on Xq27 is evolutionarily
RT conserved with regions on 3q26 and 13q34 and contains a novel P-type
RT ATPase.";
RL Genomics 84:1060-1070(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-1132 (ISOFORM 4),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 543-1132 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 777-1132 (ISOFORM 2).
RC TISSUE=Brain, Fetal brain, Testis, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1108, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP INTERACTION WITH TMEM30A, AND SUBCELLULAR LOCATION.
RX PubMed=21914794; DOI=10.1074/jbc.M111.281006;
RA Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M.,
RA Nakayama K., Shin H.W.;
RT "ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
RT localizes to the trans-Golgi network in a CDC50 protein-independent
RT manner.";
RL J. Biol. Chem. 286:38159-38167(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-157 AND PRO-931.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
CC phosphate + phospholipid(Side 2).
CC -!- SUBUNIT: Interacts with TMEM30A, but not with TMEM30B.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane. Note=Efficient exit from the
CC endoplasmic reticulum requires the presence of TMEM30A. Some cell
CC membrane localization observed in the presence of TMEM30B.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8NB49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NB49-2; Sequence=VSP_007309;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8NB49-3; Sequence=VSP_013373;
CC Name=4;
CC IsoId=Q8NB49-4; Sequence=VSP_013374;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC (TC 3.A.3) family. Type IV subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03692.1; Type=Erroneous initiation;
CC Sequence=BAC86172.1; Type=Erroneous initiation;
CC Sequence=BAC86377.1; Type=Erroneous initiation;
CC Sequence=BAD18440.1; Type=Erroneous initiation;
CC Sequence=CAI39713.1; Type=Erroneous gene model prediction;
CC Sequence=CAI39714.1; Type=Erroneous gene model prediction;
CC Sequence=CAI39716.1; Type=Erroneous gene model prediction;
CC Sequence=CAI40418.1; Type=Erroneous gene model prediction;
CC Sequence=CAI41444.1; Type=Erroneous gene model prediction;
CC Sequence=CAI41445.1; Type=Erroneous gene model prediction;
CC Sequence=CAI41446.1; Type=Erroneous gene model prediction;
CC Sequence=CAI41447.1; Type=Erroneous gene model prediction;
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DR EMBL; AJ580093; CAE30472.1; -; mRNA.
DR EMBL; AJ580094; CAE30473.1; -; mRNA.
DR EMBL; AL161777; CAI39713.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL356785; CAI39713.1; JOINED; Genomic_DNA.
DR EMBL; AL161777; CAI39714.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL356785; CAI39714.1; JOINED; Genomic_DNA.
DR EMBL; AL161777; CAI39716.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL356785; CAI39716.1; JOINED; Genomic_DNA.
DR EMBL; AL590077; CAI39716.1; JOINED; Genomic_DNA.
DR EMBL; AL356785; CAI41444.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161777; CAI41444.1; JOINED; Genomic_DNA.
DR EMBL; AL356785; CAI41445.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161777; CAI41445.1; JOINED; Genomic_DNA.
DR EMBL; AL356785; CAI41446.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161777; CAI41446.1; JOINED; Genomic_DNA.
DR EMBL; AL590077; CAI41446.1; JOINED; Genomic_DNA.
DR EMBL; AL356785; CAI41447.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL590077; CAI40418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL356785; CAI40418.1; JOINED; Genomic_DNA.
DR EMBL; AL161777; CAI40418.1; JOINED; Genomic_DNA.
DR EMBL; AK091552; BAC03692.1; ALT_INIT; mRNA.
DR EMBL; AK125474; BAC86172.1; ALT_INIT; mRNA.
DR EMBL; AK125986; BAC86377.1; ALT_INIT; mRNA.
DR EMBL; AK131262; BAD18440.1; ALT_INIT; mRNA.
DR RefSeq; NP_001010986.1; NM_001010986.2.
DR RefSeq; NP_775965.2; NM_173694.4.
DR UniGene; Hs.88252; -.
DR ProteinModelPortal; Q8NB49; -.
DR SMR; Q8NB49; 390-702.
DR PhosphoSite; Q8NB49; -.
DR DMDM; 62512178; -.
DR PaxDb; Q8NB49; -.
DR PRIDE; Q8NB49; -.
DR DNASU; 286410; -.
DR Ensembl; ENST00000327569; ENSP00000332756; ENSG00000101974.
DR Ensembl; ENST00000359686; ENSP00000352715; ENSG00000101974.
DR Ensembl; ENST00000361648; ENSP00000355165; ENSG00000101974.
DR Ensembl; ENST00000370543; ENSP00000359574; ENSG00000101974.
DR GeneID; 286410; -.
DR KEGG; hsa:286410; -.
DR UCSC; uc004faz.3; human.
DR CTD; 286410; -.
DR GeneCards; GC0XM138808; -.
DR HGNC; HGNC:13554; ATP11C.
DR HPA; HPA030830; -.
DR MIM; 300516; gene.
DR neXtProt; NX_Q8NB49; -.
DR PharmGKB; PA25103; -.
DR eggNOG; COG0474; -.
DR HOVERGEN; HBG050601; -.
DR InParanoid; Q8NB49; -.
DR KO; K01530; -.
DR OMA; PRLYMKI; -.
DR OrthoDB; EOG7HHWRB; -.
DR PhylomeDB; Q8NB49; -.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GenomeRNAi; 286410; -.
DR NextBio; 96190; -.
DR PRO; PR:Q8NB49; -.
DR Bgee; Q8NB49; -.
DR Genevestigator; Q8NB49; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0045332; P:phospholipid translocation; NAS:UniProtKB.
DR Gene3D; 2.70.150.10; -; 2.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR006539; ATPase_P-typ_Plipid-transp.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
DR InterPro; IPR001757; Cation_transp_P_typ_ATPase.
DR InterPro; IPR023214; HAD-like_dom.
DR PANTHER; PTHR24092; PTHR24092; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR SUPFAM; SSF56784; SSF56784; 3.
DR SUPFAM; SSF81660; SSF81660; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
KW Endoplasmic reticulum; Hydrolase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 1132 Probable phospholipid-transporting ATPase
FT IG.
FT /FTId=PRO_0000046373.
FT TOPO_DOM 1 66 Cytoplasmic (Potential).
FT TRANSMEM 67 85 Helical; (Potential).
FT TOPO_DOM 86 86 Extracellular (Potential).
FT TRANSMEM 87 107 Helical; (Potential).
FT TOPO_DOM 108 290 Cytoplasmic (Potential).
FT TRANSMEM 291 311 Helical; (Potential).
FT TOPO_DOM 312 346 Extracellular (Potential).
FT TRANSMEM 347 367 Helical; (Potential).
FT TOPO_DOM 368 879 Cytoplasmic (Potential).
FT TRANSMEM 880 900 Helical; (Potential).
FT TOPO_DOM 901 908 Extracellular (Potential).
FT TRANSMEM 909 929 Helical; (Potential).
FT TOPO_DOM 930 955 Cytoplasmic (Potential).
FT TRANSMEM 956 976 Helical; (Potential).
FT TOPO_DOM 977 995 Extracellular (Potential).
FT TRANSMEM 996 1016 Helical; (Potential).
FT TOPO_DOM 1017 1026 Cytoplasmic (Potential).
FT TRANSMEM 1027 1047 Helical; (Potential).
FT TOPO_DOM 1048 1069 Extracellular (Potential).
FT TRANSMEM 1070 1090 Helical; (Potential).
FT TOPO_DOM 1091 1132 Cytoplasmic (Potential).
FT ACT_SITE 412 412 4-aspartylphosphate intermediate (By
FT similarity).
FT METAL 819 819 Magnesium (By similarity).
FT METAL 823 823 Magnesium (By similarity).
FT MOD_RES 445 445 Phosphoserine.
FT MOD_RES 1108 1108 Phosphoserine.
FT VAR_SEQ 1100 1132 RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> VHHL
FT ISSSA (in isoform 2).
FT /FTId=VSP_007309.
FT VAR_SEQ 1100 1132 RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> NPNL
FT ELPMLLSYKHTDSGYS (in isoform 3).
FT /FTId=VSP_013373.
FT VAR_SEQ 1100 1132 RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> VTKR
FT LPSSGTSAIFMLSQTSSNHSFSWSE (in isoform 4).
FT /FTId=VSP_013374.
FT VARIANT 114 114 C -> W (in dbSNP:rs2491014).
FT /FTId=VAR_021827.
FT VARIANT 157 157 T -> I (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036501.
FT VARIANT 522 522 Y -> C (in dbSNP:rs17281983).
FT /FTId=VAR_055546.
FT VARIANT 931 931 Q -> P (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036502.
FT VARIANT 972 972 V -> M (in dbSNP:rs55724992).
FT /FTId=VAR_061036.
FT CONFLICT 537 537 L -> P (in Ref. 3; BAC86377).
FT CONFLICT 873 873 I -> V (in Ref. 3; BAC86377).
SQ SEQUENCE 1132 AA; 129477 MW; 74B63B20A5C6E49D CRC64;
MQMVPSLPPA SECAGEEKRV GTRTVFVGNH PVSETEAYIA QRFCDNRIVS SKYTLWNFLP
KNLFEQFRRI ANFYFLIIFL VQVTVDTPTS PVTSGLPLFF VITVTAIKQG YEDCLRHRAD
NEVNKSTVYI IENAKRVRKE SEKIKVGDVV EVQADETFPC DLILLSSCTT DGTCYVTTAS
LDGESNCKTH YAVRDTIALC TAESIDTLRA AIECEQPQPD LYKFVGRINI YSNSLEAVAR
SLGPENLLLK GATLKNTEKI YGVAVYTGME TKMALNYQGK SQKRSAVEKS INAFLIVYLF
ILLTKAAVCT TLKYVWQSTP YNDEPWYNQK TQKERETLKV LKMFTDFLSF MVLFNFIIPV
SMYVTVEMQK FLGSFFISWD KDFYDEEINE GALVNTSDLN EELGQVDYVF TDKTGTLTEN
SMEFIECCID GHKYKGVTQE VDGLSQTDGT LTYFDKVDKN REELFLRALC LCHTVEIKTN
DAVDGATESA ELTYISSSPD EIALVKGAKR YGFTFLGNRN GYMRVENQRK EIEEYELLHT
LNFDAVRRRM SVIVKTQEGD ILLFCKGADS AVFPRVQNHE IELTKVHVER NAMDGYRTLC
VAFKEIAPDD YERINRQLIE AKMALQDREE KMEKVFDDIE TNMNLIGATA VEDKLQDQAA
ETIEALHAAG LKVWVLTGDK METAKSTCYA CRLFQTNTEL LELTTKTIEE SERKEDRLHE
LLIEYRKKLL HEFPKSTRSF KKAWTEHQEY GLIIDGSTLS LILNSSQDSS SNNYKSIFLQ
ICMKCTAVLC CRMAPLQKAQ IVRMVKNLKG SPITLSIGDG ANDVSMILES HVGIGIKGKE
GRQAARNSDY SVPKFKHLKK LLLAHGHLYY VRIAHLVQYF FYKNLCFILP QFLYQFFCGF
SQQPLYDAAY LTMYNICFTS LPILAYSLLE QHINIDTLTS DPRLYMKISG NAMLQLGPFL
YWTFLAAFEG TVFFFGTYFL FQTASLEENG KVYGNWTFGT IVFTVLVFTV TLKLALDTRF
WTWINHFVIW GSLAFYVFFS FFWGGIIWPF LKQQRMYFVF AQMLSSVSTW LAIILLIFIS
LFPEILLIVL KNVRRRSARR NLSCRRASDS LSARPSVRPL LLRTFSDESN VL
//
MIM
300516
*RECORD*
*FIELD* NO
300516
*FIELD* TI
*300516 ATPase, CLASS VI, TYPE 11C; ATP11C
;;ATPase IQ; ATPIQ;;
ATPase IG; ATPIG
*FIELD* TX
read more
CLONING
By searching for genes near the X-linked hypoparathyroidism locus (HYPX;
307700), followed by cDNA library screening, EST database analysis, and
5-prime RACE, Nesbit et al. (2004) cloned ATP11C. The deduced
1,132-amino acid protein has a calculated molecular mass of 130 kD. By
searching EST databases, Nesbit et al. (2004) identified mouse and human
ATP11C cDNAs with alternate first exons that encode deduced 1,128-amino
acid proteins with apparent molecular masses of 129 kD. The mouse and
human proteins share 94.8% amino acid identity. Using RT-PCR, Nesbit et
al. (2004) also identified mouse and human ATP11C variants in which
alternative splicing of exon 29 results in proteins with different C
termini. Northern blot analysis of several human tissues detected a
7.4-kb transcript that was expressed ubiquitously and a minor 7.3-kb
transcript that was expressed in some tissues, including liver and
pancreas.
GENE STRUCTURE
Nesbit et al. (2004) determined that the ATP11C gene contains 31 exons,
including the alternate first exons 1a and 1b, and spans more than 211
kb.
MAPPING
By genomic sequence analysis, Nesbit et al. (2004) mapped the ATP11C
gene to chromosome Xq27.
*FIELD* RF
1. Nesbit, M. A.; Bowl, M. R.; Harding, B.; Schlessinger, D.; Whyte,
M. P.; Thakker, R. V.: X-linked hypoparathyroidism region on Xq27
is evolutionarily conserved with regions on 3q26 and 13q34 and contains
a novel P-type ATPase. Genomics 84: 1060-1070, 2004.
*FIELD* CD
Patricia A. Hartz: 1/3/2005
*FIELD* ED
mgross: 01/03/2005
*RECORD*
*FIELD* NO
300516
*FIELD* TI
*300516 ATPase, CLASS VI, TYPE 11C; ATP11C
;;ATPase IQ; ATPIQ;;
ATPase IG; ATPIG
*FIELD* TX
read more
CLONING
By searching for genes near the X-linked hypoparathyroidism locus (HYPX;
307700), followed by cDNA library screening, EST database analysis, and
5-prime RACE, Nesbit et al. (2004) cloned ATP11C. The deduced
1,132-amino acid protein has a calculated molecular mass of 130 kD. By
searching EST databases, Nesbit et al. (2004) identified mouse and human
ATP11C cDNAs with alternate first exons that encode deduced 1,128-amino
acid proteins with apparent molecular masses of 129 kD. The mouse and
human proteins share 94.8% amino acid identity. Using RT-PCR, Nesbit et
al. (2004) also identified mouse and human ATP11C variants in which
alternative splicing of exon 29 results in proteins with different C
termini. Northern blot analysis of several human tissues detected a
7.4-kb transcript that was expressed ubiquitously and a minor 7.3-kb
transcript that was expressed in some tissues, including liver and
pancreas.
GENE STRUCTURE
Nesbit et al. (2004) determined that the ATP11C gene contains 31 exons,
including the alternate first exons 1a and 1b, and spans more than 211
kb.
MAPPING
By genomic sequence analysis, Nesbit et al. (2004) mapped the ATP11C
gene to chromosome Xq27.
*FIELD* RF
1. Nesbit, M. A.; Bowl, M. R.; Harding, B.; Schlessinger, D.; Whyte,
M. P.; Thakker, R. V.: X-linked hypoparathyroidism region on Xq27
is evolutionarily conserved with regions on 3q26 and 13q34 and contains
a novel P-type ATPase. Genomics 84: 1060-1070, 2004.
*FIELD* CD
Patricia A. Hartz: 1/3/2005
*FIELD* ED
mgross: 01/03/2005