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Multidrug resistance-associated protein 7 (ATP-binding cassette sub-family C member 10)

 MRP7_HUMAN              Reviewed;        1492 AA.
Q5T3U5; Q8NHX7; Q9H7N2; Q9NXY3; Q9UF48;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Multidrug resistance-associated protein 7;
AltName: Full=ATP-binding cassette sub-family C member 10;
Name=ABCC10; Synonyms=MRP7, SIMRP7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
TISSUE=Small intestine;
PubMed=12566991; DOI=10.1007/BF02256002;
Kao H.-H., Chang M.-S., Cheng J.-F., Huang J.-D.;
"Genomic structure, gene expression, and promoter analysis of human
multidrug resistance-associated protein 7.";
J. Biomed. Sci. 10:98-110(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Spleen;
PubMed=11214971; DOI=10.1093/dnares/7.6.357;
Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
"Characterization of long cDNA clones from human adult spleen.";
DNA Res. 7:357-366(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 793-1492 (ISOFORMS 1/2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12527806; DOI=10.1124/mol.63.2.351;
Chen Z.-S., Hopper-Borge E., Belinsky M.G., Shchaveleva I., Kotova E.,
Kruh G.D.;
"Characterization of the transport properties of human multidrug
resistance protein 7 (MRP7, ABCC10).";
Mol. Pharmacol. 63:351-358(2003).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15256465; DOI=10.1158/0008-5472.CAN-03-3111;
Hopper-Borge E., Chen Z.-S., Shchaveleva I., Belinsky M.G., Kruh G.D.;
"Analysis of the drug resistance profile of multidrug resistance
protein 7 (ABCC10): resistance to docetaxel.";
Cancer Res. 64:4927-4930(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463 AND SER-467, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
-!- FUNCTION: ATP-dependent transporter probably involved in cellular
detoxification through lipophilic anion extrusion.
{ECO:0000269|PubMed:12527806, ECO:0000269|PubMed:15256465}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=57.8 uM for 17-beta-estradiol 17-(beta-D-glucuronide) (at 37
degrees Celsius) {ECO:0000269|PubMed:12527806};
Vmax=20 pmol/min/mg enzyme toward 17-beta-estradiol 17-(beta-D-
glucuronide) (at 37 degrees Celsius)
{ECO:0000269|PubMed:12527806};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12566991,
ECO:0000269|PubMed:15256465}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00441,
ECO:0000269|PubMed:12566991, ECO:0000269|PubMed:15256465}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Mrp7;
IsoId=Q5T3U5-1; Sequence=Displayed;
Name=2; Synonyms=Mrp7A;
IsoId=Q5T3U5-2; Sequence=VSP_021078, VSP_021079, VSP_021080;
-!- TISSUE SPECIFICITY: Isoform 1 is specifically expressed in spleen.
Isoform 2 is more widely expressed. {ECO:0000269|PubMed:12566991}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA92227.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB15736.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q5T3U5";
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EMBL; AY032599; AAK39642.1; -; mRNA.
EMBL; AK000002; BAA92227.1; ALT_INIT; mRNA.
EMBL; AK024446; BAB15736.1; ALT_SEQ; mRNA.
EMBL; AL359813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133613; CAB63742.1; -; mRNA.
CCDS; CCDS4896.1; -. [Q5T3U5-2]
CCDS; CCDS56430.1; -. [Q5T3U5-1]
PIR; T43469; T43469.
RefSeq; NP_001185863.1; NM_001198934.1. [Q5T3U5-1]
RefSeq; NP_258261.2; NM_033450.2. [Q5T3U5-2]
UniGene; Hs.55879; -.
ProteinModelPortal; Q5T3U5; -.
SMR; Q5T3U5; -.
BioGrid; 124617; 12.
STRING; 9606.ENSP00000361608; -.
ChEMBL; CHEMBL2073687; -.
DrugBank; DB00091; Cyclosporine.
DrugBank; DB00987; Cytarabine.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB01248; Docetaxel.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB00783; Estradiol.
DrugBank; DB00773; Etoposide.
DrugBank; DB00441; Gemcitabine.
DrugBank; DB00563; Methotrexate.
DrugBank; DB01229; Paclitaxel.
DrugBank; DB00203; Sildenafil.
DrugBank; DB04348; Taurocholic Acid.
DrugBank; DB00300; Tenofovir.
DrugBank; DB00661; Verapamil.
DrugBank; DB00541; Vincristine.
TCDB; 3.A.1.208.31; the atp-binding cassette (abc) superfamily.
iPTMnet; Q5T3U5; -.
PhosphoSitePlus; Q5T3U5; -.
BioMuta; ABCC10; -.
DMDM; 74756298; -.
MaxQB; Q5T3U5; -.
PaxDb; Q5T3U5; -.
PeptideAtlas; Q5T3U5; -.
PRIDE; Q5T3U5; -.
DNASU; 89845; -.
Ensembl; ENST00000244533; ENSP00000244533; ENSG00000124574. [Q5T3U5-2]
Ensembl; ENST00000372530; ENSP00000361608; ENSG00000124574. [Q5T3U5-1]
GeneID; 89845; -.
KEGG; hsa:89845; -.
UCSC; uc003ouy.2; human. [Q5T3U5-1]
CTD; 89845; -.
DisGeNET; 89845; -.
EuPathDB; HostDB:ENSG00000124574.14; -.
GeneCards; ABCC10; -.
HGNC; HGNC:52; ABCC10.
HPA; HPA041607; -.
HPA; HPA045464; -.
MIM; 612509; gene.
neXtProt; NX_Q5T3U5; -.
OpenTargets; ENSG00000124574; -.
PharmGKB; PA24392; -.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00880000137856; -.
HOVERGEN; HBG107141; -.
InParanoid; Q5T3U5; -.
KO; K05674; -.
OMA; CRLPHRL; -.
OrthoDB; EOG091G00IN; -.
PhylomeDB; Q5T3U5; -.
TreeFam; TF105203; -.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
ChiTaRS; ABCC10; human.
GeneWiki; ABCC10; -.
GenomeRNAi; 89845; -.
PRO; PR:Q5T3U5; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124574; -.
CleanEx; HS_ABCC10; -.
ExpressionAtlas; Q5T3U5; baseline and differential.
Genevisible; Q5T3U5; HS.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0043225; F:ATPase-coupled anion transmembrane transporter activity; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1492 Multidrug resistance-associated protein
7.
/FTId=PRO_0000253576.
TRANSMEM 32 52 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 70 90 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 102 122 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 133 153 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 172 192 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 293 313 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 320 340 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 391 411 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 414 434 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 507 527 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 538 558 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 875 895 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 933 953 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 974 994 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 1051 1071 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 1153 1173 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 1182 1202 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
DOMAIN 285 563 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 598 824 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 885 1210 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1246 1479 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 633 640 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1280 1287 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 463 463 Phosphothreonine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:18220336}.
VAR_SEQ 1 43 Missing (in isoform 2).
{ECO:0000303|PubMed:12566991}.
/FTId=VSP_021078.
VAR_SEQ 44 52 VLSACYLGT -> MCLLVFPLV (in isoform 2).
{ECO:0000303|PubMed:12566991}.
/FTId=VSP_021079.
VAR_SEQ 588 588 P -> PDCGRLGAQIKWLLCS (in isoform 2).
{ECO:0000303|PubMed:12566991}.
/FTId=VSP_021080.
VARIANT 948 948 I -> T (in dbSNP:rs2125739).
/FTId=VAR_028391.
CONFLICT 208 208 D -> E (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 220 220 Missing (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 631 631 I -> T (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 764 764 L -> P (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 809 809 S -> P (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 888 888 I -> T (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 1030 1030 S -> F (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 1134 1134 L -> F (in Ref. 2; BAB15736).
{ECO:0000305}.
CONFLICT 1276 1276 L -> V (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 1455 1455 G -> E (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 1481 1481 S -> C (in Ref. 1; AAK39642).
{ECO:0000305}.
CONFLICT 1490 1490 G -> R (in Ref. 1; AAK39642).
{ECO:0000305}.
SEQUENCE 1492 AA; 161629 MW; 6FBC260DEFB3DF30 CRC64;
MERLLAQLCG SSAAWPLPLW EGDTTGHCFT QLVLSALPHA LLAVLSACYL GTPRSPDYIL
PCSPGWRLRL AASFLLSVFP LLDLLPVALP PGAGPGPIGL EVLAGCVAAV AWISHSLALW
VLAHSPHGHS RGPLALALVA LLPAPALVLT VLWHCQRGTL LPPLLPGPMA RLCLLILQLA
ALLAYALGWA APGGPREPWA QEPLLPEDQE PEVAEDGESW LSRFSYAWLA PLLARGACGE
LRQPQDICRL PHRLQPTYLA RVFQAHWQEG ARLWRALYGA FGRCYLALGL LKLVGTMLGF
SGPLLLSLLV GFLEEGQEPL SHGLLYALGL AGGAVLGAVL QNQYGYEVYK VTLQARGAVL
NILYCKALQL GPSRPPTGEA LNLLGTDSER LLNFAGSFHE AWGLPLQLAI TLYLLYQQVG
VAFVGGLILA LLLVPVNKVI ATRIMASNQE MLQHKDARVK LVTELLSGIR VIKFCGWEQA
LGARVEACRA RELGRLRVIK YLDAACVYLW AALPVVISIV IFITYVLMGH QLTATKVFTA
LALVRMLILP LNNFPWVING LLEAKVSLDR IQLFLDLPNH NPQAYYSPDP PAEPSTVLEL
HGALFSWDPV GTSLETFISH LEVKKGMLVG IVGKVGCGKS SLLAAIAGEL HRLRGHVAVR
GLSKGFGLAT QEPWIQFATI RDNILFGKTF DAQLYKEVLE ACALNDDLSI LPAGDQTEVG
EKGVTLSGGQ RARIALARAV YQEKELYLLD DPLAAVDADV ANHLLHRCIL GMLSYTTRLL
CTHRTEYLER ADAVLLMEAG RLIRAGPPSE ILPLVQAVPK AWAENGQESD SATAQSVQNP
EKTKEGLEEE QSTSGRLLQE ESKKEGAVAL HVYQAYWKAV GQGLALAILF SLLLMQATRN
AADWWLSHWI SQLKAENSSQ EAQPSTSPAS MGLFSPQLLL FSPGNLYIPV FPLPKAAPNG
SSDIRFYLTV YATIAGVNSL CTLLRAVLFA AGTLQAAATL HRRLLHRVLM APVTFFNATP
TGRILNRFSS DVACADDSLP FILNILLANA AGLLGLLAVL GSGLPWLLLL LPPLSIMYYH
VQRHYRASSR ELRRLGSLTL SPLYSHLADT LAGLSVLRAT GATYRFEEEN LRLLELNQRC
QFATSATMQW LDIRLQLMGA AVVSAIAGIA LVQHQQGLAN PGLVGLSLSY ALSLTGLLSG
LVSSFTQTEA MLVSVERLEE YTCDLPQEPQ GQPLQLGTGW LTQGGVEFQD VVLAYRPGLP
NALDGVTFCV QPGEKLGIVG RTGSGKSSLL LVLFRLLEPS SGRVLLDGVD TSQLELAQLR
SQLAIIPQEP FLFSGTVREN LDPQGLHKDR ALWQALKQCH LSEVITSMGG LDGELGEGGR
SLSLGQRQLL CLARALLTDA KILCIDEATA SVDQKTDQLL QQTICKRFAN KTVLTIAHRL
NTILNSDRVL VLQAGRVVEL DSPATLRNQP HSLFQQLLQS SQQGVPASLG GP


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E1068r ELISA Abcc1,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mrp1,Multidrug resistance-associated protein 1,Rat,Rattus norvegicus 96T
U1068r CLIA Abcc1,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mrp1,Multidrug resistance-associated protein 1,Rat,Rattus norvegicus 96T
U1068b CLIA ABCC1,ATP-binding cassette sub-family C member 1,Bos taurus,Bovine,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
EIAAB25435 ABCC5,ATP-binding cassette sub-family C member 5,Homo sapiens,Human,MOAT-C,MRP5,Multidrug resistance-associated protein 5,Multi-specific organic anion transporter C,pABC11,SMRP
U1068h CLIA ABCC1,ATP-binding cassette sub-family C member 1,Homo sapiens,Human,Leukotriene C(4) transporter,LTC4 transporter,MRP,MRP1,Multidrug resistance-associated protein 1 96T


 

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