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Reviewed, UniProtKB/Swiss-Prot Q8NB49 (AT11C_HUMAN)

Last modified July 22, 2008. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable phospholipid-transporting ATPase IG
    EC=3.6.3.1
Alternative name(s):
    ATPase class I type 11C
    ATPase IG
    ATPase IQ
    ATPase class VI type 11C
Gene names
Name: ATP11C
Synonyms: ATPIG, ATPIQ
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out).

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Widely expressed.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR.

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IV subfamily.

Sequence caution

CAI39713.1 sequence differs from that shown. Reason: Erroneous gene model prediction.

CAI39714.1 sequence differs from that shown. Reason: Erroneous gene model prediction.

CAI39716.1 sequence differs from that shown. Reason: Erroneous gene model prediction.

CAI40418.1 sequence differs from that shown. Reason: Erroneous gene model prediction.

CAI41444.1 sequence differs from that shown. Reason: Erroneous gene model prediction.

CAI41445.1 sequence differs from that shown. Reason: Erroneous gene model prediction.

CAI41446.1 sequence differs from that shown. Reason: Erroneous gene model prediction.

CAI41447.1 sequence differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords

   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein

Gene Ontology (GO)

None. [Check GOA]

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NB49-1)

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: Q8NB49-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1100-1132: RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL → VHHLISSSA
Notes: No experimental confirmation available.
Isoform 3 (identifier: Q8NB49-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1100-1132: RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL → NPNLELPMLLSYKHTDSGYS
Isoform 4 (identifier: Q8NB49-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1100-1132: RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL → VTKRLPSSGTSAIFMLSQTSSNHSFSWSE
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 11321132Probable phospholipid-transporting ATPase IG

Regions

Topological domain1 – 6666Cytoplasmic Potential
Transmembrane67 – 8519 Potential
Topological domain861Extracellular Potential
Transmembrane87 – 10721 Potential
Topological domain108 – 290183Cytoplasmic Potential
Transmembrane291 – 31121 Potential
Topological domain312 – 34635Extracellular Potential
Transmembrane347 – 36721 Potential
Topological domain368 – 879512Cytoplasmic Potential
Transmembrane880 – 90021 Potential
Topological domain901 – 9088Extracellular Potential
Transmembrane909 – 92921 Potential
Topological domain930 – 95526Cytoplasmic Potential
Transmembrane956 – 97621 Potential
Topological domain977 – 99519Extracellular Potential
Transmembrane996 – 101621 Potential
Topological domain1017 – 102610Cytoplasmic Potential
Transmembrane1027 – 104721 Potential
Topological domain1048 – 106922Extracellular Potential
Transmembrane1070 – 109021 Potential
Topological domain1091 – 113242Cytoplasmic Potential

Sites

Active site41214-aspartylphosphate intermediate By similarity
Metal binding8191Magnesium By similarity
Metal binding8231Magnesium By similarity

Amino acid modifications

Modified residue2611Phosphotyrosine
Modified residue4451Phosphoserine
Modified residue11081Phosphoserine By similarity

Natural variations

Alternative sequence1100 – 113233RNLSC…ESNVL → VHHLISSSA in isoform 2.
Alternative sequence1100 – 113233RNLSC…ESNVL → NPNLELPMLLSYKHTDSGYS in isoform 3.
Alternative sequence1100 – 113233RNLSC…ESNVL → VTKRLPSSGTSAIFMLSQTS SNHSFSWSE in isoform 4.
Natural variant1141C → W: dbSNP rs2491014.
Natural variant1571T → I in a colorectal cancer sample; somatic mutation.
Natural variant9311Q → P in a colorectal cancer sample; somatic mutation.

Experimental info

Sequence conflict5371L → P in BAC86377. Ref.3
Sequence conflict8731I → V in BAC86377. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 12, 2005. Version 3.
Checksum: 74B63B20A5C6E49D

FASTA1,132129,477
        10         20         30         40         50         60 
MQMVPSLPPA SECAGEEKRV GTRTVFVGNH PVSETEAYIA QRFCDNRIVS SKYTLWNFLP 

        70         80         90        100        110        120 
KNLFEQFRRI ANFYFLIIFL VQVTVDTPTS PVTSGLPLFF VITVTAIKQG YEDCLRHRAD 

       130        140        150        160        170        180 
NEVNKSTVYI IENAKRVRKE SEKIKVGDVV EVQADETFPC DLILLSSCTT DGTCYVTTAS 

       190        200        210        220        230        240 
LDGESNCKTH YAVRDTIALC TAESIDTLRA AIECEQPQPD LYKFVGRINI YSNSLEAVAR 

       250        260        270        280        290        300 
SLGPENLLLK GATLKNTEKI YGVAVYTGME TKMALNYQGK SQKRSAVEKS INAFLIVYLF 

       310        320        330        340        350        360 
ILLTKAAVCT TLKYVWQSTP YNDEPWYNQK TQKERETLKV LKMFTDFLSF MVLFNFIIPV 

       370        380        390        400        410        420 
SMYVTVEMQK FLGSFFISWD KDFYDEEINE GALVNTSDLN EELGQVDYVF TDKTGTLTEN 

       430        440        450        460        470        480 
SMEFIECCID GHKYKGVTQE VDGLSQTDGT LTYFDKVDKN REELFLRALC LCHTVEIKTN 

       490        500        510        520        530        540 
DAVDGATESA ELTYISSSPD EIALVKGAKR YGFTFLGNRN GYMRVENQRK EIEEYELLHT 

       550        560        570        580        590        600 
LNFDAVRRRM SVIVKTQEGD ILLFCKGADS AVFPRVQNHE IELTKVHVER NAMDGYRTLC 

       610        620        630        640        650        660 
VAFKEIAPDD YERINRQLIE AKMALQDREE KMEKVFDDIE TNMNLIGATA VEDKLQDQAA 

       670        680        690        700        710        720 
ETIEALHAAG LKVWVLTGDK METAKSTCYA CRLFQTNTEL LELTTKTIEE SERKEDRLHE 

       730        740        750        760        770        780 
LLIEYRKKLL HEFPKSTRSF KKAWTEHQEY GLIIDGSTLS LILNSSQDSS SNNYKSIFLQ 

       790        800        810        820        830        840 
ICMKCTAVLC CRMAPLQKAQ IVRMVKNLKG SPITLSIGDG ANDVSMILES HVGIGIKGKE 

       850        860        870        880        890        900 
GRQAARNSDY SVPKFKHLKK LLLAHGHLYY VRIAHLVQYF FYKNLCFILP QFLYQFFCGF 

       910        920        930        940        950        960 
SQQPLYDAAY LTMYNICFTS LPILAYSLLE QHINIDTLTS DPRLYMKISG NAMLQLGPFL 

       970        980        990       1000       1010       1020 
YWTFLAAFEG TVFFFGTYFL FQTASLEENG KVYGNWTFGT IVFTVLVFTV TLKLALDTRF 

      1030       1040       1050       1060       1070       1080 
WTWINHFVIW GSLAFYVFFS FFWGGIIWPF LKQQRMYFVF AQMLSSVSTW LAIILLIFIS 

      1090       1100       1110       1120       1130 
LFPEILLIVL KNVRRRSARR NLSCRRASDS LSARPSVRPL LLRTFSDESN VL 

« Hide

Isoform 2 [UniParc].

Checksum: ADC1995E368B8C4E
Show »

1,108126,710
Isoform 3 [UniParc].

Checksum: 2F1EF15A73AB3947
Show »

1,119128,040
Isoform 4 [UniParc].

Checksum: 5928DF8ED2988A7C
Show »

1,128128,933

References

[1]"X-linked hypoparathyroidism region on Xq27 is evolutionarily conserved with regions on 3q26 and 13q34 and contains a novel P-type ATPase."
Andrew-Nesbit M., Bowl M.R., Harding B., Schlessinger D., Whyte M.P., Thakker R.V.
Genomics 84:1060-1070(2004) [PubMed: 15533723] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, VARIANT TRP-114.
Tissue: Liver.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. expand/collapse author list , 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.,