Full text data of ATP11B
ATP11B
(ATPIF, ATPIR, KIAA0956)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Probable phospholipid-transporting ATPase IF; 3.6.3.1 (ATPase IR; ATPase class VI type 11B)
Probable phospholipid-transporting ATPase IF; 3.6.3.1 (ATPase IR; ATPase class VI type 11B)
UniProt
Q9Y2G3
ID AT11B_HUMAN Reviewed; 1177 AA.
AC Q9Y2G3; Q96FN1; Q9UKK7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-APR-2003, sequence version 2.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Probable phospholipid-transporting ATPase IF;
DE EC=3.6.3.1;
DE AltName: Full=ATPase IR;
DE AltName: Full=ATPase class VI type 11B;
GN Name=ATP11B; Synonyms=ATPIF, ATPIR, KIAA0956;
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] OF 1-248.
RC TISSUE=Colon;
RX PubMed=11015572;
RA Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P.,
RA Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D.,
RA Williamson P.L., Schlegel R.A.;
RT "Differential expression of putative transbilayer amphipath
RT transporters.";
RL Physiol. Genomics 1:139-150(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-195 AND 540-1177.
RC TISSUE=Colon, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 111-450.
RX PubMed=11790799; DOI=10.1074/jbc.M200240200;
RA Halleck M.S., Schlegel R.A., Williamson P.L.;
RT "Reanalysis of ATP11B, a Type IV P-type ATPase.";
RL J. Biol. Chem. 277:9736-9740(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-1111.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 688-1111.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1154, AND MASS
RP SPECTROMETRY.
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 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).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
CC phosphate + phospholipid(Side 2).
CC -!- SUBUNIT: Interacts with TMEM30A.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Multi-pass
CC membrane protein. Early endosome. Endoplasmic reticulum. Note=Exit
CC from the endoplasmic reticulum requires the presence of TMEM30A,
CC but not TMEM30B. In the presence of TMEM30A, mainly located in
CC recycling endosomes.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC (TC 3.A.3) family. Type IV subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10630.1; Type=Frameshift; Positions=884;
CC Sequence=AAH42180.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF156548; AAF09446.1; -; mRNA.
DR EMBL; AC069431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042180; AAH42180.1; ALT_SEQ; mRNA.
DR EMBL; BC010630; AAH10630.1; ALT_FRAME; mRNA.
DR EMBL; AB023173; BAA76800.1; -; mRNA.
DR EMBL; AL133061; CAB61385.1; -; mRNA.
DR PIR; T42662; T42662.
DR RefSeq; NP_055431.1; NM_014616.2.
DR UniGene; Hs.478429; -.
DR ProteinModelPortal; Q9Y2G3; -.
DR SMR; Q9Y2G3; 396-895.
DR STRING; 9606.ENSP00000321195; -.
DR TCDB; 3.A.3.8.12; the p-type atpase (p-atpase) superfamily.
DR PhosphoSite; Q9Y2G3; -.
DR DMDM; 30316395; -.
DR PaxDb; Q9Y2G3; -.
DR PRIDE; Q9Y2G3; -.
DR DNASU; 23200; -.
DR Ensembl; ENST00000323116; ENSP00000321195; ENSG00000058063.
DR Ensembl; ENST00000493826; ENSP00000419032; ENSG00000058063.
DR GeneID; 23200; -.
DR KEGG; hsa:23200; -.
DR UCSC; uc003flb.3; human.
DR CTD; 23200; -.
DR GeneCards; GC03P182511; -.
DR HGNC; HGNC:13553; ATP11B.
DR HPA; HPA036237; -.
DR HPA; HPA036238; -.
DR MIM; 605869; gene.
DR neXtProt; NX_Q9Y2G3; -.
DR PharmGKB; PA25102; -.
DR eggNOG; COG0474; -.
DR HOGENOM; HOG000202528; -.
DR HOVERGEN; HBG050601; -.
DR InParanoid; Q9Y2G3; -.
DR KO; K01530; -.
DR OMA; PHVLQSK; -.
DR OrthoDB; EOG7HHWRB; -.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP11B; human.
DR GeneWiki; ATP11B; -.
DR GenomeRNAi; 23200; -.
DR NextBio; 44715; -.
DR PRO; PR:Q9Y2G3; -.
DR ArrayExpress; Q9Y2G3; -.
DR Bgee; Q9Y2G3; -.
DR CleanEx; HS_ATP11B; -.
DR Genevestigator; Q9Y2G3; -.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0015075; F:ion transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004012; F:phospholipid-translocating ATPase activity; TAS:UniProtKB.
DR GO; GO:0015917; P:aminophospholipid transport; TAS:UniProtKB.
DR Gene3D; 2.70.150.10; -; 2.
DR Gene3D; 3.40.1110.10; -; 2.
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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SUPFAM; SSF56784; SSF56784; 3.
DR SUPFAM; SSF81660; SSF81660; 2.
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 ATP-binding; Complete proteome; Endoplasmic reticulum; Endosome;
KW Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 1177 Probable phospholipid-transporting ATPase
FT IF.
FT /FTId=PRO_0000046371.
FT TOPO_DOM 1 55 Cytoplasmic (Potential).
FT TRANSMEM 56 77 Helical; (Potential).
FT TOPO_DOM 78 82 Extracellular (Potential).
FT TRANSMEM 83 104 Helical; (Potential).
FT TOPO_DOM 105 289 Cytoplasmic (Potential).
FT TRANSMEM 290 311 Helical; (Potential).
FT TOPO_DOM 312 341 Extracellular (Potential).
FT TRANSMEM 342 359 Helical; (Potential).
FT TOPO_DOM 360 876 Cytoplasmic (Potential).
FT TRANSMEM 877 898 Helical; (Potential).
FT TOPO_DOM 899 910 Extracellular (Potential).
FT TRANSMEM 911 930 Helical; (Potential).
FT TOPO_DOM 931 960 Cytoplasmic (Potential).
FT TRANSMEM 961 982 Helical; (Potential).
FT TOPO_DOM 983 997 Extracellular (Potential).
FT TRANSMEM 998 1020 Helical; (Potential).
FT TOPO_DOM 1021 1025 Cytoplasmic (Potential).
FT TRANSMEM 1026 1047 Helical; (Potential).
FT TOPO_DOM 1048 1065 Extracellular (Potential).
FT TRANSMEM 1066 1090 Helical; (Potential).
FT TOPO_DOM 1091 1177 Cytoplasmic (Potential).
FT ACT_SITE 407 407 4-aspartylphosphate intermediate (By
FT similarity).
FT METAL 821 821 Magnesium (By similarity).
FT METAL 825 825 Magnesium (By similarity).
FT MOD_RES 1154 1154 Phosphoserine.
SQ SEQUENCE 1177 AA; 134190 MW; 665110145457B220 CRC64;
MWRWIRQQLG FDPPHQSDTR TIYVANRFPQ NGLYTPQKFI DNRIISSKYT VWNFVPKNLF
EQFRRVANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV TAIKQGYEDW LRHNSDNEVN
GAPVYVVRSG GLVKTRSKNI RVGDIVRIAK DEIFPADLVL LSSDRLDGSC HVTTASLDGE
TNLKTHVAVP ETALLQTVAN LDTLVAVIEC QQPEADLYRF MGRMIITQQM EEIVRPLGPE
SLLLRGARLK NTKEIFGVAV YTGMETKMAL NYKSKSQKRS AVEKSMNTFL IIYLVILISE
AVISTILKYT WQAEEKWDEP WYNQKTEHQR NSSKILRFIS DFLAFLVLYN FIIPISLYVT
VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMQFR
ECSINGMKYQ EINGRLVPEG PTPDSSEGNL SYLSSLSHLN NLSHLTTSSS FRTSPENETE
LIKEHDLFFK AVSLCHTVQI SNVQTDCTGD GPWQSNLAPS QLEYYASSPD EKALVEAAAR
IGIVFIGNSE ETMEVKTLGK LERYKLLHIL EFDSDRRRMS VIVQAPSGEK LLFAKGAESS
ILPKCIGGEI EKTRIHVDEF ALKGLRTLCI AYRKFTSKEY EEIDKRIFEA RTALQQREEK
LAAVFQFIEK DLILLGATAV EDRLQDKVRE TIEALRMAGI KVWVLTGDKH ETAVSVSLSC
GHFHRTMNIL ELINQKSDSE CAEQLRQLAR RITEDHVIQH GLVVDGTSLS LALREHEKLF
MEVCRNCSAV LCCRMAPLQK AKVIRLIKIS PEKPITLAVG DGANDVSMIQ EAHVGIGIMG
KEGRQAARNS DYAIARFKFL SKLLFVHGHF YYIRIATLVQ YFFYKNVCFI TPQFLYQFYC
LFSQQTLYDS VYLTLYNICF TSLPILIYSL LEQHVDPHVL QNKPTLYRDI SKNRLLSIKT
FLYWTILGFS HAFIFFFGSY LLIGKDTSLL GNGQMFGNWT FGTLVFTVMV ITVTVKMALE
THFWTWINHL VTWGSIIFYF VFSLFYGGIL WPFLGSQNMY FVFIQLLSSG SAWFAIILMV
VTCLFLDIIK KVFDRHLHPT STEKAQLTET NAGIKCLDSM CCFPEGEAAC ASVGRMLERV
IGRCSPTHIS RSWSASDPFY TNDRSILTLS TMDSSTC
//
ID AT11B_HUMAN Reviewed; 1177 AA.
AC Q9Y2G3; Q96FN1; Q9UKK7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-APR-2003, sequence version 2.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Probable phospholipid-transporting ATPase IF;
DE EC=3.6.3.1;
DE AltName: Full=ATPase IR;
DE AltName: Full=ATPase class VI type 11B;
GN Name=ATP11B; Synonyms=ATPIF, ATPIR, KIAA0956;
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] OF 1-248.
RC TISSUE=Colon;
RX PubMed=11015572;
RA Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P.,
RA Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D.,
RA Williamson P.L., Schlegel R.A.;
RT "Differential expression of putative transbilayer amphipath
RT transporters.";
RL Physiol. Genomics 1:139-150(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-195 AND 540-1177.
RC TISSUE=Colon, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 111-450.
RX PubMed=11790799; DOI=10.1074/jbc.M200240200;
RA Halleck M.S., Schlegel R.A., Williamson P.L.;
RT "Reanalysis of ATP11B, a Type IV P-type ATPase.";
RL J. Biol. Chem. 277:9736-9740(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-1111.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 688-1111.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1154, AND MASS
RP SPECTROMETRY.
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 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).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
CC phosphate + phospholipid(Side 2).
CC -!- SUBUNIT: Interacts with TMEM30A.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Multi-pass
CC membrane protein. Early endosome. Endoplasmic reticulum. Note=Exit
CC from the endoplasmic reticulum requires the presence of TMEM30A,
CC but not TMEM30B. In the presence of TMEM30A, mainly located in
CC recycling endosomes.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC (TC 3.A.3) family. Type IV subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10630.1; Type=Frameshift; Positions=884;
CC Sequence=AAH42180.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF156548; AAF09446.1; -; mRNA.
DR EMBL; AC069431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042180; AAH42180.1; ALT_SEQ; mRNA.
DR EMBL; BC010630; AAH10630.1; ALT_FRAME; mRNA.
DR EMBL; AB023173; BAA76800.1; -; mRNA.
DR EMBL; AL133061; CAB61385.1; -; mRNA.
DR PIR; T42662; T42662.
DR RefSeq; NP_055431.1; NM_014616.2.
DR UniGene; Hs.478429; -.
DR ProteinModelPortal; Q9Y2G3; -.
DR SMR; Q9Y2G3; 396-895.
DR STRING; 9606.ENSP00000321195; -.
DR TCDB; 3.A.3.8.12; the p-type atpase (p-atpase) superfamily.
DR PhosphoSite; Q9Y2G3; -.
DR DMDM; 30316395; -.
DR PaxDb; Q9Y2G3; -.
DR PRIDE; Q9Y2G3; -.
DR DNASU; 23200; -.
DR Ensembl; ENST00000323116; ENSP00000321195; ENSG00000058063.
DR Ensembl; ENST00000493826; ENSP00000419032; ENSG00000058063.
DR GeneID; 23200; -.
DR KEGG; hsa:23200; -.
DR UCSC; uc003flb.3; human.
DR CTD; 23200; -.
DR GeneCards; GC03P182511; -.
DR HGNC; HGNC:13553; ATP11B.
DR HPA; HPA036237; -.
DR HPA; HPA036238; -.
DR MIM; 605869; gene.
DR neXtProt; NX_Q9Y2G3; -.
DR PharmGKB; PA25102; -.
DR eggNOG; COG0474; -.
DR HOGENOM; HOG000202528; -.
DR HOVERGEN; HBG050601; -.
DR InParanoid; Q9Y2G3; -.
DR KO; K01530; -.
DR OMA; PHVLQSK; -.
DR OrthoDB; EOG7HHWRB; -.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP11B; human.
DR GeneWiki; ATP11B; -.
DR GenomeRNAi; 23200; -.
DR NextBio; 44715; -.
DR PRO; PR:Q9Y2G3; -.
DR ArrayExpress; Q9Y2G3; -.
DR Bgee; Q9Y2G3; -.
DR CleanEx; HS_ATP11B; -.
DR Genevestigator; Q9Y2G3; -.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0015075; F:ion transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004012; F:phospholipid-translocating ATPase activity; TAS:UniProtKB.
DR GO; GO:0015917; P:aminophospholipid transport; TAS:UniProtKB.
DR Gene3D; 2.70.150.10; -; 2.
DR Gene3D; 3.40.1110.10; -; 2.
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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SUPFAM; SSF56784; SSF56784; 3.
DR SUPFAM; SSF81660; SSF81660; 2.
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 ATP-binding; Complete proteome; Endoplasmic reticulum; Endosome;
KW Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 1177 Probable phospholipid-transporting ATPase
FT IF.
FT /FTId=PRO_0000046371.
FT TOPO_DOM 1 55 Cytoplasmic (Potential).
FT TRANSMEM 56 77 Helical; (Potential).
FT TOPO_DOM 78 82 Extracellular (Potential).
FT TRANSMEM 83 104 Helical; (Potential).
FT TOPO_DOM 105 289 Cytoplasmic (Potential).
FT TRANSMEM 290 311 Helical; (Potential).
FT TOPO_DOM 312 341 Extracellular (Potential).
FT TRANSMEM 342 359 Helical; (Potential).
FT TOPO_DOM 360 876 Cytoplasmic (Potential).
FT TRANSMEM 877 898 Helical; (Potential).
FT TOPO_DOM 899 910 Extracellular (Potential).
FT TRANSMEM 911 930 Helical; (Potential).
FT TOPO_DOM 931 960 Cytoplasmic (Potential).
FT TRANSMEM 961 982 Helical; (Potential).
FT TOPO_DOM 983 997 Extracellular (Potential).
FT TRANSMEM 998 1020 Helical; (Potential).
FT TOPO_DOM 1021 1025 Cytoplasmic (Potential).
FT TRANSMEM 1026 1047 Helical; (Potential).
FT TOPO_DOM 1048 1065 Extracellular (Potential).
FT TRANSMEM 1066 1090 Helical; (Potential).
FT TOPO_DOM 1091 1177 Cytoplasmic (Potential).
FT ACT_SITE 407 407 4-aspartylphosphate intermediate (By
FT similarity).
FT METAL 821 821 Magnesium (By similarity).
FT METAL 825 825 Magnesium (By similarity).
FT MOD_RES 1154 1154 Phosphoserine.
SQ SEQUENCE 1177 AA; 134190 MW; 665110145457B220 CRC64;
MWRWIRQQLG FDPPHQSDTR TIYVANRFPQ NGLYTPQKFI DNRIISSKYT VWNFVPKNLF
EQFRRVANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV TAIKQGYEDW LRHNSDNEVN
GAPVYVVRSG GLVKTRSKNI RVGDIVRIAK DEIFPADLVL LSSDRLDGSC HVTTASLDGE
TNLKTHVAVP ETALLQTVAN LDTLVAVIEC QQPEADLYRF MGRMIITQQM EEIVRPLGPE
SLLLRGARLK NTKEIFGVAV YTGMETKMAL NYKSKSQKRS AVEKSMNTFL IIYLVILISE
AVISTILKYT WQAEEKWDEP WYNQKTEHQR NSSKILRFIS DFLAFLVLYN FIIPISLYVT
VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMQFR
ECSINGMKYQ EINGRLVPEG PTPDSSEGNL SYLSSLSHLN NLSHLTTSSS FRTSPENETE
LIKEHDLFFK AVSLCHTVQI SNVQTDCTGD GPWQSNLAPS QLEYYASSPD EKALVEAAAR
IGIVFIGNSE ETMEVKTLGK LERYKLLHIL EFDSDRRRMS VIVQAPSGEK LLFAKGAESS
ILPKCIGGEI EKTRIHVDEF ALKGLRTLCI AYRKFTSKEY EEIDKRIFEA RTALQQREEK
LAAVFQFIEK DLILLGATAV EDRLQDKVRE TIEALRMAGI KVWVLTGDKH ETAVSVSLSC
GHFHRTMNIL ELINQKSDSE CAEQLRQLAR RITEDHVIQH GLVVDGTSLS LALREHEKLF
MEVCRNCSAV LCCRMAPLQK AKVIRLIKIS PEKPITLAVG DGANDVSMIQ EAHVGIGIMG
KEGRQAARNS DYAIARFKFL SKLLFVHGHF YYIRIATLVQ YFFYKNVCFI TPQFLYQFYC
LFSQQTLYDS VYLTLYNICF TSLPILIYSL LEQHVDPHVL QNKPTLYRDI SKNRLLSIKT
FLYWTILGFS HAFIFFFGSY LLIGKDTSLL GNGQMFGNWT FGTLVFTVMV ITVTVKMALE
THFWTWINHL VTWGSIIFYF VFSLFYGGIL WPFLGSQNMY FVFIQLLSSG SAWFAIILMV
VTCLFLDIIK KVFDRHLHPT STEKAQLTET NAGIKCLDSM CCFPEGEAAC ASVGRMLERV
IGRCSPTHIS RSWSASDPFY TNDRSILTLS TMDSSTC
//
MIM
605869
*RECORD*
*FIELD* NO
605869
*FIELD* TI
*605869 ATPase, CLASS VI, TYPE 11B; ATP11B
;;ATPIR
*FIELD* TX
DESCRIPTION
P-type ATPases, such as ATP11B, are phosphorylated in their intermediate
read morestate and drive uphill transport of ions across membranes. Several
subfamilies of P-type ATPases have been identified. One subfamily
transports heavy metal ions, such as Cu(2+) or Cd(2+). Another subfamily
transports non-heavy metal ions, such as H(+), Na(+), K(+), or Ca(+). A
third subfamily transports amphipaths, such as phosphatidylserine.
CLONING
Nagase et al. (1999) isolated a partial cDNA encoding ATP11B, which they
called KIAA0956, from a brain cDNA library. Based on homology analysis,
they predicted that the KIAA0956 protein is a chromaffin granule ATPase.
RT-PCR analysis detected wide expression, with highest levels in kidney,
followed by ovary, corpus callosum, and testis.
RUSH proteins are SWI/SNF-related transcription factors with uteroglobin
promoter-binding RING finger signatures near their C termini (see
603257). Mansharamani et al. (2001) isolated a nearly full-length rabbit
cDNA encoding Rfbp, a RUSH-binding protein that shares 93% amino acid
identity with KIAA0956.
Nesbit et al. (2004) reported that the ATP11B protein contains 10
transmembrane domains and the conserved DKTGTLT sequence found in P-type
ATPases.
GENE STRUCTURE
Nesbit et al. (2004) determined that the ATP11B gene contains at least
30 exons.
MAPPING
Nagase et al. (1999) stated that the ATP11B gene, or KIAA0956, maps to
chromosome 3. By genomic sequence analysis, Halleck et al. (1999)
confirmed that the ATP11B gene, or ATP1R, maps to chromosome 3.
*FIELD* RF
1. Halleck, M. S.; Lawler, J. F., Jr.; Blackshaw, S.; Gao, L.; Nagarajan,
P.; Hacker, C.; Pyle, S.; Newman, J. T.; Nakanishi, Y.; Ando, H.;
Weinstock, D.; Williamson, P.; Schlegel, R. A.: Differential expression
of putative transbilayer amphipath transporters. Physiol. Genomics 1:
139-150, 1999.
2. Mansharamani, M.; Hewetson, A.; Chilton, B. S.: Cloning and characterization
of an atypical type IV P-type ATPase that binds to the RING motif
of RUSH transcription factors. J. Biol. Chem. 276: 3641-3649, 2001.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, M.;
Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction
of the coding sequences of unidentified human genes. XIII. The complete
sequences of 100 new cDNA clones from brain which code for large proteins
in vitro. DNA Res. 6: 63-70, 1999.
4. 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* CN
Patricia A. Hartz - updated: 12/21/2004
*FIELD* CD
Paul J. Converse: 4/23/2001
*FIELD* ED
mgross: 12/21/2004
terry: 12/21/2004
mgross: 4/23/2001
*RECORD*
*FIELD* NO
605869
*FIELD* TI
*605869 ATPase, CLASS VI, TYPE 11B; ATP11B
;;ATPIR
*FIELD* TX
DESCRIPTION
P-type ATPases, such as ATP11B, are phosphorylated in their intermediate
read morestate and drive uphill transport of ions across membranes. Several
subfamilies of P-type ATPases have been identified. One subfamily
transports heavy metal ions, such as Cu(2+) or Cd(2+). Another subfamily
transports non-heavy metal ions, such as H(+), Na(+), K(+), or Ca(+). A
third subfamily transports amphipaths, such as phosphatidylserine.
CLONING
Nagase et al. (1999) isolated a partial cDNA encoding ATP11B, which they
called KIAA0956, from a brain cDNA library. Based on homology analysis,
they predicted that the KIAA0956 protein is a chromaffin granule ATPase.
RT-PCR analysis detected wide expression, with highest levels in kidney,
followed by ovary, corpus callosum, and testis.
RUSH proteins are SWI/SNF-related transcription factors with uteroglobin
promoter-binding RING finger signatures near their C termini (see
603257). Mansharamani et al. (2001) isolated a nearly full-length rabbit
cDNA encoding Rfbp, a RUSH-binding protein that shares 93% amino acid
identity with KIAA0956.
Nesbit et al. (2004) reported that the ATP11B protein contains 10
transmembrane domains and the conserved DKTGTLT sequence found in P-type
ATPases.
GENE STRUCTURE
Nesbit et al. (2004) determined that the ATP11B gene contains at least
30 exons.
MAPPING
Nagase et al. (1999) stated that the ATP11B gene, or KIAA0956, maps to
chromosome 3. By genomic sequence analysis, Halleck et al. (1999)
confirmed that the ATP11B gene, or ATP1R, maps to chromosome 3.
*FIELD* RF
1. Halleck, M. S.; Lawler, J. F., Jr.; Blackshaw, S.; Gao, L.; Nagarajan,
P.; Hacker, C.; Pyle, S.; Newman, J. T.; Nakanishi, Y.; Ando, H.;
Weinstock, D.; Williamson, P.; Schlegel, R. A.: Differential expression
of putative transbilayer amphipath transporters. Physiol. Genomics 1:
139-150, 1999.
2. Mansharamani, M.; Hewetson, A.; Chilton, B. S.: Cloning and characterization
of an atypical type IV P-type ATPase that binds to the RING motif
of RUSH transcription factors. J. Biol. Chem. 276: 3641-3649, 2001.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, M.;
Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction
of the coding sequences of unidentified human genes. XIII. The complete
sequences of 100 new cDNA clones from brain which code for large proteins
in vitro. DNA Res. 6: 63-70, 1999.
4. 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* CN
Patricia A. Hartz - updated: 12/21/2004
*FIELD* CD
Paul J. Converse: 4/23/2001
*FIELD* ED
mgross: 12/21/2004
terry: 12/21/2004
mgross: 4/23/2001