ID   MRP8_HUMAN              Reviewed;        1382 AA.
AC   Q96J66; Q8TDJ0; Q96JA6; Q9BX80;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   28-JUN-2023, entry version 172.
DE   RecName: Full=ATP-binding cassette sub-family C member 11 {ECO:0000303|PubMed:11483364};
DE            EC=7.6.2.2 {ECO:0000269|PubMed:12764137, ECO:0000269|PubMed:15537867, ECO:0000269|PubMed:25896536};
DE            EC=7.6.2.3 {ECO:0000269|PubMed:15537867};
DE   AltName: Full=Multidrug resistance-associated protein 8 {ECO:0000303|PubMed:11591886};
GN   Name=ABCC11 {ECO:0000312|HGNC:HGNC:14639}; Synonyms=MRP8;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=11483364; DOI=10.1016/s0378-1119(01)00572-8;
RA   Tammur J., Prades C., Arnould I., Rzhetsky A., Hutchinson A., Adachi M.,
RA   Schuetz J.D., Swoboda K.J., Ptacek L.J., Rosier M., Dean M., Allikmets R.;
RT   "Two new genes from the human ATP-binding cassette transporter superfamily,
RT   ABCC11 and ABCC12, tandemly duplicated on chromosome 16q12.";
RL   Gene 273:89-96(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Liver;
RX   PubMed=11688999; DOI=10.1006/bbrc.2001.5865;
RA   Yabuuchi H., Shimizu H., Takayanagi S., Ishikawa T.;
RT   "Multiple splicing variants of two new human ATP-binding cassette
RT   transporters, ABCC11 and ABCC12.";
RL   Biochem. Biophys. Res. Commun. 288:933-939(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP   GLU-317 AND ARG-1344.
RC   TISSUE=Mammary gland;
RX   PubMed=11591886; DOI=10.1007/bf03401856;
RA   Bera T.K., Lee S., Salvatore G., Lee B.K., Pastan I.H.;
RT   "MRP8, a new member of ABC transporter superfamily, identified by EST
RT   database mining and gene prediction program, is highly expressed in breast
RT   cancer.";
RL   Mol. Med. 7:509-516(2001).
RN   [4]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=12764137; DOI=10.1074/jbc.m304059200;
RA   Guo Y., Kotova E., Chen Z.S., Lee K., Hopper-Borge E., Belinsky M.G.,
RA   Kruh G.D.;
RT   "MRP8, ATP-binding cassette C11 (ABCC11), is a cyclic nucleotide efflux
RT   pump and a resistance factor for fluoropyrimidines 2',3'-dideoxycytidine
RT   and 9'-(2'-phosphonylmethoxyethyl)adenine.";
RL   J. Biol. Chem. 278:29509-29514(2003).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15537867; DOI=10.1124/mol.104.007138;
RA   Chen Z.S., Guo Y., Belinsky M.G., Kotova E., Kruh G.D.;
RT   "Transport of bile acids, sulfated steroids, estradiol 17-beta-D-
RT   glucuronide, and leukotriene C4 by human multidrug resistance protein 8
RT   (ABCC11).";
RL   Mol. Pharmacol. 67:545-557(2005).
RN   [6]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16359813; DOI=10.1016/j.neuroscience.2005.10.025;
RA   Bortfeld M., Rius M., Koenig J., Herold-Mende C., Nies A.T., Keppler D.;
RT   "Human multidrug resistance protein 8 (MRP8/ABCC11), an apical efflux pump
RT   for steroid sulfates, is an axonal protein of the CNS and peripheral
RT   nervous system.";
RL   Neuroscience 137:1247-1257(2006).
RN   [7]
RP   POLYMORPHISM, VARIANT ARG-180, CHARACTERIZATION OF VARIANT ARG-180, AND
RP   FUNCTION IN SECRETION OF EARWAX.
RX   PubMed=16444273; DOI=10.1038/ng1733;
RA   Yoshiura K., Kinoshita A., Ishida T., Ninokata A., Ishikawa T., Kaname T.,
RA   Bannai M., Tokunaga K., Sonoda S., Komaki R., Ihara M., Saenko V.A.,
RA   Alipov G.K., Sekine I., Komatsu K., Takahashi H., Nakashima M.,
RA   Sosonkina N., Mapendano C.K., Ghadami M., Nomura M., Liang D.-S., Miwa N.,
RA   Kim D.-K., Garidkhuu A., Natsume N., Ohta T., Tomita H., Kaneko A.,
RA   Kikuchi M., Russomando G., Hirayama K., Ishibashi M., Takahashi A.,
RA   Saitou N., Murray J.C., Saito S., Nakamura Y., Niikawa N.;
RT   "A SNP in the ABCC11 gene is the determinant of human earwax type.";
RL   Nat. Genet. 38:324-330(2006).
RN   [8]
RP   VARIANT ARG-180, CHARACTERIZATION OF VARIANTS HIS-19; ARG-180; GLU-317;
RP   MET-546; TRP-630; ILE-648; ILE-687; ARG-735; VAL-970 AND ARG-1344,
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION AT
RP   ASN-838 AND ASN-844, POLYMORPHISM, AND MUTAGENESIS OF GLY-180; ASN-838 AND
RP   ASN-844.
RX   PubMed=19383836; DOI=10.1096/fj.09-129098;
RA   Toyoda Y., Sakurai A., Mitani Y., Nakashima M., Yoshiura K., Nakagawa H.,
RA   Sakai Y., Ota I., Lezhava A., Hayashizaki Y., Niikawa N., Ishikawa T.;
RT   "Earwax, osmidrosis, and breast cancer: why does one SNP (538G>A) in the
RT   human ABC transporter ABCC11 gene determine earwax type?";
RL   FASEB J. 23:2001-2013(2009).
RN   [9]
RP   VARIANT ARG-180, CHARACTERIZATION OF VARIANT ARG-180, FUNCTION, TISSUE
RP   SPECIFICITY, AND POLYMORPHISM.
RX   PubMed=19710689; DOI=10.1038/jid.2009.254;
RA   Martin A., Saathoff M., Kuhn F., Max H., Terstegen L., Natsch A.;
RT   "A functional ABCC11 allele is essential in the biochemical formation of
RT   human axillary odor.";
RL   J. Invest. Dermatol. 130:529-540(2010).
RN   [10]
RP   CHARACTERIZATION OF VARIANTS HIS-19; ARG-180; GLU-317; MET-546; ILE-648 AND
RP   ARG-1344, FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX   PubMed=25896536; DOI=10.1038/tpj.2015.27;
RA   Arlanov R., Lang T., Jedlitschky G., Schaeffeler E., Ishikawa T.,
RA   Schwab M., Nies A.T.;
RT   "Functional characterization of common protein variants in the efflux
RT   transporter ABCC11 and identification of T546M as functionally damaging
RT   variant.";
RL   Pharmacogenomics J. 16:193-201(2016).
CC   -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC       family that actively extrudes physiological compounds, and xenobiotics
CC       from cells. Participates in physiological processes involving bile
CC       acids, conjugated steroids and cyclic nucleotides (PubMed:12764137,
CC       PubMed:15537867). Stimulates the ATP-dependent uptake of a range of
CC       physiological lipophilic anions, including the glutathione S-conjugates
CC       leukotriene C4 and dinitrophenyl S-glutathione, steroid sulfates such
CC       as dehydroepiandrosterone 3-sulfate (DHEAS) and estrone 3-sulfate,
CC       glucuronides such as estradiol 17-beta-D-glucuronide (E(2)17betaG), the
CC       monoanionic bile acids glycocholate and taurocholate, and methotrexate
CC       (PubMed:15537867, PubMed:25896536). Enhances also the cellular
CC       extrusion of cAMP and cGMP (PubMed:12764137, PubMed:15537867). Confers
CC       resistance to anticancer drugs, such as 5-fluorouracil (5-FU) and
CC       methotrexate (PubMed:25896536, PubMed:15537867, PubMed:12764137).
CC       Probably functions to secrete earwax (PubMed:16444273,
CC       PubMed:19383836). Required for the secretion of components contributing
CC       to axillary odor formation (PubMed:19710689, PubMed:12764137,
CC       PubMed:15537867, PubMed:16444273, PubMed:19383836, PubMed:25896536).
CC       {ECO:0000269|PubMed:12764137, ECO:0000269|PubMed:15537867,
CC       ECO:0000269|PubMed:16444273, ECO:0000269|PubMed:19383836,
CC       ECO:0000269|PubMed:19710689, ECO:0000269|PubMed:25896536}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:12764137,
CC         ECO:0000269|PubMed:15537867, ECO:0000269|PubMed:25896536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC         substituted glutathione(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC         ChEBI:CHEBI:456216; EC=7.6.2.3;
CC         Evidence={ECO:0000269|PubMed:15537867};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC         Evidence={ECO:0000305|PubMed:15537867};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC         C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:15537867};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC         Evidence={ECO:0000305|PubMed:15537867};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP +
CC         dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15537867,
CC         ECO:0000269|PubMed:16359813, ECO:0000269|PubMed:25896536};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365;
CC         Evidence={ECO:0000305|PubMed:15537867};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-
CC         sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61348,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:60050, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:16359813, ECO:0000269|PubMed:25896536};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61349;
CC         Evidence={ECO:0000305|PubMed:25896536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate +
CC         taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:15537867};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053;
CC         Evidence={ECO:0000305|PubMed:15537867};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+)
CC         + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:15537867};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057;
CC         Evidence={ECO:0000305|PubMed:15537867};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O =
CC         17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:82961, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:15537867};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC         Evidence={ECO:0000305|PubMed:15537867};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP(in) + ATP + H2O = 3',5'-cyclic AMP(out) + ADP
CC         + H(+) + phosphate; Xref=Rhea:RHEA:66184, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58165, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:12764137, ECO:0000269|PubMed:15537867};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66185;
CC         Evidence={ECO:0000305|PubMed:12764137};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP(in) + ATP + H2O = 3',5'-cyclic GMP(out) + ADP
CC         + H(+) + phosphate; Xref=Rhea:RHEA:66188, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57746, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:12764137, ECO:0000269|PubMed:15537867};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66189;
CC         Evidence={ECO:0000305|PubMed:12764137};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,4-dinitrophenyl-S-glutathione(in) + ATP + H2O = 2,4-
CC         dinitrophenyl-S-glutathione(out) + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:61380, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:133977,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15537867};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61381;
CC         Evidence={ECO:0000305|PubMed:15537867};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13 uM for DHEAS transport {ECO:0000269|PubMed:15537867};
CC         KM=21 uM for DHEAS transport {ECO:0000269|PubMed:16359813};
CC         KM=62.9 uM for E(2)17betaG transport {ECO:0000269|PubMed:15537867};
CC         KM=957 uM for methotrexate transport {ECO:0000269|PubMed:15537867};
CC         Vmax=0.74 pmol/min/mg enzyme for cAMP transport
CC         {ECO:0000269|PubMed:15537867};
CC         Vmax=0.59 pmol/min/mg enzyme for cGMP transport
CC         {ECO:0000269|PubMed:15537867};
CC         Vmax=370 pmol/min/mg enzyme for DHEAS transport
CC         {ECO:0000269|PubMed:16359813};
CC         Vmax=34.9 pmol/min/mg enzyme for DHEAS transport
CC         {ECO:0000269|PubMed:15537867};
CC         Vmax=62 pmol/min/mg enzyme E(2)17betaG transport
CC         {ECO:0000269|PubMed:15537867};
CC         Vmax=317 pmol/min/mg enzyme methotrexate
CC         {ECO:0000269|PubMed:15537867};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19383836,
CC       ECO:0000269|PubMed:25896536}; Multi-pass membrane protein
CC       {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:19383836}.
CC       Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25896536}. Apical cell
CC       membrane {ECO:0000269|PubMed:16359813}; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96J66-1; Sequence=Displayed;
CC       Name=2; Synonyms=Isoform A;
CC         IsoId=Q96J66-2; Sequence=VSP_017351;
CC   -!- TISSUE SPECIFICITY: Expressed in ceruminous apocrine gland (at protein
CC       level) (PubMed:19383836, PubMed:19710689). Expressed in many tissues.
CC       Not expressed in kidney, spleen and colon. Highly expressed in breast
CC       cancer. Expressed at moderate levels in normal breast and testis and at
CC       very low levels in liver, brain and placenta (PubMed:11483364,
CC       PubMed:11591886, PubMed:19383836, PubMed:19710689). Localizes to axons
CC       of the CNS and peripheral nervous system (at protein level)
CC       (PubMed:16359813). {ECO:0000269|PubMed:11483364,
CC       ECO:0000269|PubMed:11591886, ECO:0000269|PubMed:16359813,
CC       ECO:0000269|PubMed:19383836, ECO:0000269|PubMed:19710689}.
CC   -!- POLYMORPHISM: Polymorphism in ABCC11 is associated with variation in
CC       apocrine gland secretion [MIM:117800]. This determines different ear
CC       wax phenotypes, presence or absence of axillary odor, and variation in
CC       colostrum secretion. Characteristic of earwax and strength of axillary
CC       odor are most likely interconnected. Human earwax is a Mendelian trait
CC       consisting of wet and dry types. The wet earwax is brownish and sticky,
CC       whereas the dry type lacks cerumen. The wet cerumen phenotype is
CC       completely dominant. The dry type is seen frequently (80-95%) among
CC       East Asians, but uncommon (0-3%) in populations of European and African
CC       origins. Intermediate frequencies (30-50%) of the dry type are seen in
CC       populations of Southern Asia, the Pacific Islands, Central Asia and
CC       Asia Minor, as well as among the Native North American and Inuit of
CC       Asian ancestry. The allele with Arg-180 is responsible for the dry
CC       earwax phenotype and lack of axillary odor.
CC       {ECO:0000269|PubMed:16444273, ECO:0000269|PubMed:19383836,
CC       ECO:0000269|PubMed:19710689}.
CC   -!- MISCELLANEOUS: This protein has no ortholog in rodents. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Of earwax and migration
CC       - Issue 67 of February 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/067";
CC   -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC       URL="http://abcm2.hegelab.org/search";
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DR   EMBL; AY040219; AAK76739.1; -; mRNA.
DR   EMBL; AF367202; AAK58869.1; -; mRNA.
DR   EMBL; AF411579; AAL99902.1; -; mRNA.
DR   EMBL; AF352582; AAK19755.1; -; mRNA.
DR   CCDS; CCDS10732.1; -. [Q96J66-1]
DR   CCDS; CCDS10733.1; -. [Q96J66-2]
DR   RefSeq; NP_115972.2; NM_032583.3. [Q96J66-1]
DR   RefSeq; NP_149163.2; NM_033151.3. [Q96J66-1]
DR   RefSeq; NP_660187.1; NM_145186.2. [Q96J66-2]
DR   RefSeq; XP_016879284.1; XM_017023795.1.
DR   RefSeq; XP_016879285.1; XM_017023796.1.
DR   RefSeq; XP_016879286.1; XM_017023797.1. [Q96J66-1]
DR   RefSeq; XP_016879287.1; XM_017023798.1. [Q96J66-1]
DR   RefSeq; XP_016879288.1; XM_017023799.1. [Q96J66-1]
DR   RefSeq; XP_016879289.1; XM_017023800.1. [Q96J66-1]
DR   AlphaFoldDB; Q96J66; -.
DR   SMR; Q96J66; -.
DR   BioGRID; 124474; 3.
DR   IntAct; Q96J66; 1.
DR   STRING; 9606.ENSP00000378230; -.
DR   ChEMBL; CHEMBL2073702; -.
DR   DrugBank; DB00286; Conjugated estrogens.
DR   DrugBank; DB02527; Cyclic adenosine monophosphate.
DR   DrugBank; DB00158; Folic acid.
DR   DrugBank; DB00328; Indomethacin.
DR   DrugBank; DB00563; Methotrexate.
DR   DrugBank; DB01032; Probenecid.
DR   DrugBank; DB04348; Taurocholic acid.
DR   DrugCentral; Q96J66; -.
DR   TCDB; 3.A.1.208.13; the atp-binding cassette (abc) superfamily.
DR   GlyCosmos; Q96J66; 3 sites, No reported glycans.
DR   GlyGen; Q96J66; 3 sites.
DR   iPTMnet; Q96J66; -.
DR   PhosphoSitePlus; Q96J66; -.
DR   BioMuta; ABCC11; -.
DR   DMDM; 74762666; -.
DR   jPOST; Q96J66; -.
DR   MassIVE; Q96J66; -.
DR   MaxQB; Q96J66; -.
DR   PaxDb; Q96J66; -.
DR   PeptideAtlas; Q96J66; -.
DR   ProteomicsDB; 76891; -. [Q96J66-1]
DR   ProteomicsDB; 76892; -. [Q96J66-2]
DR   Antibodypedia; 28152; 352 antibodies from 34 providers.
DR   DNASU; 85320; -.
DR   Ensembl; ENST00000353782.9; ENSP00000311326.6; ENSG00000121270.16. [Q96J66-2]
DR   Ensembl; ENST00000356608.7; ENSP00000349017.2; ENSG00000121270.16. [Q96J66-1]
DR   Ensembl; ENST00000394747.5; ENSP00000378230.1; ENSG00000121270.16. [Q96J66-1]
DR   Ensembl; ENST00000394748.5; ENSP00000378231.1; ENSG00000121270.16. [Q96J66-1]
DR   GeneID; 85320; -.
DR   KEGG; hsa:85320; -.
DR   MANE-Select; ENST00000356608.7; ENSP00000349017.2; NM_001370497.1; NP_001357426.1.
DR   UCSC; uc002eff.1; human. [Q96J66-1]
DR   AGR; HGNC:14639; -.
DR   CTD; 85320; -.
DR   DisGeNET; 85320; -.
DR   GeneCards; ABCC11; -.
DR   HGNC; HGNC:14639; ABCC11.
DR   HPA; ENSG00000121270; Tissue enriched (breast).
DR   MalaCards; ABCC11; -.
DR   MIM; 117800; phenotype.
DR   MIM; 607040; gene.
DR   neXtProt; NX_Q96J66; -.
DR   OpenTargets; ENSG00000121270; -.
DR   PharmGKB; PA24393; -.
DR   VEuPathDB; HostDB:ENSG00000121270; -.
DR   eggNOG; KOG0054; Eukaryota.
DR   GeneTree; ENSGT00940000162968; -.
DR   HOGENOM; CLU_000604_27_1_1; -.
DR   InParanoid; Q96J66; -.
DR   OMA; VYHYYIQ; -.
DR   OrthoDB; 3384185at2759; -.
DR   PhylomeDB; Q96J66; -.
DR   TreeFam; TF352085; -.
DR   PathwayCommons; Q96J66; -.
DR   Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR   SABIO-RK; Q96J66; -.
DR   SignaLink; Q96J66; -.
DR   BioGRID-ORCS; 85320; 14 hits in 1143 CRISPR screens.
DR   ChiTaRS; ABCC11; human.
DR   GeneWiki; ABCC11; -.
DR   GenomeRNAi; 85320; -.
DR   Pharos; Q96J66; Tbio.
DR   PRO; PR:Q96J66; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q96J66; protein.
DR   Bgee; ENSG00000121270; Expressed in right lobe of liver and 86 other tissues.
DR   ExpressionAtlas; Q96J66; baseline and differential.
DR   Genevisible; Q96J66; HS.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015432; F:ABC-type bile acid transporter activity; IDA:UniProtKB.
DR   GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IDA:UniProtKB.
DR   GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0043225; F:ATPase-coupled inorganic anion transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015216; F:purine nucleotide transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015721; P:bile acid and bile salt transport; IDA:UniProtKB.
DR   GO; GO:0071716; P:leukotriene transport; IDA:UniProtKB.
DR   GO; GO:0015711; P:organic anion transport; IDA:UniProtKB.
DR   GO; GO:0015865; P:purine nucleotide transport; IDA:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:0042908; P:xenobiotic transport; IDA:UniProtKB.
DR   CDD; cd18592; ABC_6TM_MRP5_8_9_D1; 1.
DR   CDD; cd18599; ABC_6TM_MRP5_8_9_D2; 1.
DR   CDD; cd03250; ABCC_MRP_domain1; 1.
DR   CDD; cd03244; ABCC_MRP_domain2; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR   PANTHER; PTHR24223:SF168; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 11; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Cytoplasmic vesicle;
KW   Glycoprotein; Lipid transport; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..1382
FT                   /note="ATP-binding cassette sub-family C member 11"
FT                   /id="PRO_0000225594"
FT   TOPO_DOM        1..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        439..806
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        807..827
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        864..884
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        931..951
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1050..1070
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        1071..1382
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          163..443
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          508..732
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          806..1105
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1141..1375
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          504..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         544..551
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1175..1182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        838
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:19383836"
FT   CARBOHYD        844
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:19383836"
FT   CARBOHYD        992
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1261..1298
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11688999"
FT                   /id="VSP_017351"
FT   VARIANT         19
FT                   /note="R -> H (no effect on glycosylation; no effect on
FT                   transport activity; no effect on plasma membrane
FT                   localization; dbSNP:rs16945988)"
FT                   /evidence="ECO:0000269|PubMed:19383836,
FT                   ECO:0000269|PubMed:25896536"
FT                   /id="VAR_025437"
FT   VARIANT         180
FT                   /note="G -> R (in dry earwax and lack of axillary odor
FT                   phenotype; loss of N-glycosylation; strongly reduced plasma
FT                   membrane localization; no DHEAS transport and largely
FT                   reduced estrone 3-sulfate transport; decreased protein
FT                   concentration in axillary sweat; dbSNP:rs17822931)"
FT                   /evidence="ECO:0000269|PubMed:16444273,
FT                   ECO:0000269|PubMed:19383836, ECO:0000269|PubMed:19710689,
FT                   ECO:0000269|PubMed:25896536"
FT                   /id="VAR_025438"
FT   VARIANT         317
FT                   /note="A -> E (no effect on glycosylation; no effect on
FT                   transport activity; no effect on plasma membrane
FT                   localization; dbSNP:rs11863236)"
FT                   /evidence="ECO:0000269|PubMed:11591886,
FT                   ECO:0000269|PubMed:19383836, ECO:0000269|PubMed:25896536"
FT                   /id="VAR_048144"
FT   VARIANT         546
FT                   /note="T -> M (significantly decreased transport activity
FT                   of DHEAS and estrone 3-sulfate; no effect on glycosylation;
FT                   reduced ATP-dependent 5-FdUMP transport; no effect on
FT                   plasma membrane localization; dbSNP:rs17822471)"
FT                   /evidence="ECO:0000269|PubMed:19383836,
FT                   ECO:0000269|PubMed:25896536"
FT                   /id="VAR_048145"
FT   VARIANT         630
FT                   /note="R -> W (no effect on glycosylation;
FT                   dbSNP:rs41282045)"
FT                   /evidence="ECO:0000269|PubMed:19383836"
FT                   /id="VAR_077575"
FT   VARIANT         648
FT                   /note="V -> I (no effect on glycosylation; no effect on
FT                   transport activity; no effect on plasma membrane
FT                   localization; dbSNP:rs16945930)"
FT                   /evidence="ECO:0000269|PubMed:19383836,
FT                   ECO:0000269|PubMed:25896536"
FT                   /id="VAR_048146"
FT   VARIANT         687
FT                   /note="V -> I (no effect on glycosylation;
FT                   dbSNP:rs16945928)"
FT                   /evidence="ECO:0000269|PubMed:19383836"
FT                   /id="VAR_048147"
FT   VARIANT         735
FT                   /note="K -> R (no effect on glycosylation;
FT                   dbSNP:rs16945926)"
FT                   /evidence="ECO:0000269|PubMed:19383836"
FT                   /id="VAR_048148"
FT   VARIANT         970
FT                   /note="M -> V (no effect on glycosylation;
FT                   dbSNP:rs41280943)"
FT                   /evidence="ECO:0000269|PubMed:19383836"
FT                   /id="VAR_077576"
FT   VARIANT         1344
FT                   /note="H -> R (no effect on glycosylation; no effect on
FT                   transport activity; no effect on plasma membrane
FT                   localization; dbSNP:rs16945916)"
FT                   /evidence="ECO:0000269|PubMed:11591886,
FT                   ECO:0000269|PubMed:19383836, ECO:0000269|PubMed:25896536"
FT                   /id="VAR_048149"
FT   MUTAGEN         180
FT                   /note="G->A,P: Does not affect N-glycosylation."
FT                   /evidence="ECO:0000269|PubMed:19383836"
FT   MUTAGEN         180
FT                   /note="G->L,H,D,E: Loss of N-glycosylation."
FT                   /evidence="ECO:0000269|PubMed:19383836"
FT   MUTAGEN         838
FT                   /note="N->Q: Loss of N-glycosylation."
FT                   /evidence="ECO:0000269|PubMed:19383836"
FT   MUTAGEN         844
FT                   /note="N->Q: Loss of N-glycosylation."
FT                   /evidence="ECO:0000269|PubMed:19383836"
FT   CONFLICT        199
FT                   /note="V -> A (in Ref. 2; AAK58869/AAL99902)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311
FT                   /note="L -> P (in Ref. 3; AAK19755)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="K -> E (in Ref. 2; AAK58869/AAL99902)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="T -> A (in Ref. 3; AAK19755)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        632
FT                   /note="L -> P (in Ref. 3; AAK19755)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        688
FT                   /note="L -> Q (in Ref. 3; AAK19755)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        702
FT                   /note="I -> V (in Ref. 3; AAK19755)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        982
FT                   /note="K -> E (in Ref. 3; AAK19755)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1382 AA;  154301 MW;  0F3C17DC69AE97F4 CRC64;
     MTRKRTYWVP NSSGGLVNRG IDIGDDMVSG LIYKTYTLQD GPWSQQERNP EAPGRAAVPP
     WGKYDAALRT MIPFRPKPRF PAPQPLDNAG LFSYLTVSWL TPLMIQSLRS RLDENTIPPL
     SVHDASDKNV QRLHRLWEEE VSRRGIEKAS VLLVMLRFQR TRLIFDALLG ICFCIASVLG
     PILIIPKILE YSEEQLGNVV HGVGLCFALF LSECVKSLSF SSSWIINQRT AIRFRAAVSS
     FAFEKLIQFK SVIHITSGEA ISFFTGDVNY LFEGVCYGPL VLITCASLVI CSISSYFIIG
     YTAFIAILCY LLVFPLAVFM TRMAVKAQHH TSEVSDQRIR VTSEVLTCIK LIKMYTWEKP
     FAKIIEDLRR KERKLLEKCG LVQSLTSITL FIIPTVATAV WVLIHTSLKL KLTASMAFSM
     LASLNLLRLS VFFVPIAVKG LTNSKSAVMR FKKFFLQESP VFYVQTLQDP SKALVFEEAT
     LSWQQTCPGI VNGALELERN GHASEGMTRP RDALGPEEEG NSLGPELHKI NLVVSKGMML
     GVCGNTGSGK SSLLSAILEE MHLLEGSVGV QGSLAYVPQQ AWIVSGNIRE NILMGGAYDK
     ARYLQVLHCC SLNRDLELLP FGDMTEIGER GLNLSGGQKQ RISLARAVYS DRQIYLLDDP
     LSAVDAHVGK HIFEECIKKT LRGKTVVLVT HQLQYLEFCG QIILLENGKI CENGTHSELM
     QKKGKYAQLI QKMHKEATSD MLQDTAKIAE KPKVESQALA TSLEESLNGN AVPEHQLTQE
     EEMEEGSLSW RVYHHYIQAA GGYMVSCIIF FFVVLIVFLT IFSFWWLSYW LEQGSGTNSS
     RESNGTMADL GNIADNPQLS FYQLVYGLNA LLLICVGVCS SGIFTKVTRK ASTALHNKLF
     NKVFRCPMSF FDTIPIGRLL NCFAGDLEQL DQLLPIFSEQ FLVLSLMVIA VLLIVSVLSP
     YILLMGAIIM VICFIYYMMF KKAIGVFKRL ENYSRSPLFS HILNSLQGLS SIHVYGKTED
     FISQFKRLTD AQNNYLLLFL SSTRWMALRL EIMTNLVTLA VALFVAFGIS STPYSFKVMA
     VNIVLQLASS FQATARIGLE TEAQFTAVER ILQYMKMCVS EAPLHMEGTS CPQGWPQHGE
     IIFQDYHMKY RDNTPTVLHG INLTIRGHEV VGIVGRTGSG KSSLGMALFR LVEPMAGRIL
     IDGVDICSIG LEDLRSKLSV IPQDPVLLSG TIRFNLDPFD RHTDQQIWDA LERTFLTKAI
     SKFPKKLHTD VVENGGNFSV GERQLLCIAR AVLRNSKIIL IDEATASIDM ETDTLIQRTI
     REAFQGCTVL VIAHRVTTVL NCDHILVMGN GKVVEFDRPE VLRKKPGSLF AALMATATSS
     LR
//