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Canalicular multispecific organic anion transporter 1 (ATP-binding cassette sub-family C member 2)

 MRP2_MOUSE              Reviewed;        1543 AA.
Q8VI47; Q8VI46;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 2.
12-SEP-2018, entry version 125.
RecName: Full=Canalicular multispecific organic anion transporter 1;
AltName: Full=ATP-binding cassette sub-family C member 2;
Name=Abcc2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=AKR/J, and C57L/J;
Bouchard G., Chao H., Lammert F., Carey M.C., Paigen B.;
"Murine cholesterol cholelithiasis is linked to a mutation in the
Abcc2 gene.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-876, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Mediates hepatobiliary excretion of numerous organic
anions. May function as a cellular cisplatin transporter (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-
pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
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EMBL; AF282772; AAL36985.1; -; mRNA.
EMBL; AF282773; AAL36986.1; -; mRNA.
CCDS; CCDS29838.1; -.
RefSeq; NP_038834.2; NM_013806.2.
UniGene; Mm.39054; -.
ProteinModelPortal; Q8VI47; -.
SMR; Q8VI47; -.
STRING; 10090.ENSMUSP00000026208; -.
ChEMBL; CHEMBL2073681; -.
iPTMnet; Q8VI47; -.
PhosphoSitePlus; Q8VI47; -.
SwissPalm; Q8VI47; -.
MaxQB; Q8VI47; -.
PaxDb; Q8VI47; -.
PeptideAtlas; Q8VI47; -.
PRIDE; Q8VI47; -.
Ensembl; ENSMUST00000026208; ENSMUSP00000026208; ENSMUSG00000025194.
GeneID; 12780; -.
KEGG; mmu:12780; -.
UCSC; uc008how.1; mouse.
CTD; 1244; -.
MGI; MGI:1352447; Abcc2.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00880000137856; -.
HOVERGEN; HBG108314; -.
InParanoid; Q8VI47; -.
KO; K05666; -.
OMA; DLPLCFE; -.
OrthoDB; EOG091G00IN; -.
TreeFam; TF105199; -.
Reactome; R-MMU-382556; ABC-family proteins mediated transport.
ChiTaRS; Abcc2; mouse.
PRO; PR:Q8VI47; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000025194; Expressed in 51 organ(s), highest expression level in ileum.
ExpressionAtlas; Q8VI47; baseline and differential.
Genevisible; Q8VI47; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0031526; C:brush border membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
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:0008514; F:organic anion transmembrane transporter activity; IEA:InterPro.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0016999; P:antibiotic metabolic process; ISO:MGI.
GO; GO:1901086; P:benzylpenicillin metabolic process; ISO:MGI.
GO; GO:0015722; P:canalicular bile acid transport; ISO:MGI.
GO; GO:0030644; P:cellular chloride ion homeostasis; ISO:MGI.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0006855; P:drug transmembrane transport; ISO:MGI.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0015694; P:mercury ion transport; ISO:MGI.
GO; GO:0015732; P:prostaglandin transport; ISO:MGI.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
GO; GO:0042493; P:response to drug; ISO:MGI.
GO; GO:0043627; P:response to estrogen; ISO:MGI.
GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
GO; GO:0009408; P:response to heat; IEA:Ensembl.
GO; GO:0031427; P:response to methotrexate; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0070327; P:thyroid hormone transport; ISO:MGI.
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; IPR030247; ABCC2.
InterPro; IPR005292; Multidrug-R_assoc.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24223:SF176; PTHR24223:SF176; 1.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Glycoprotein; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1543 Canalicular multispecific organic anion
transporter 1.
/FTId=PRO_0000093357.
TOPO_DOM 1 26 Extracellular. {ECO:0000250}.
TRANSMEM 27 47 Helical; Name=1. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 48 67 Cytoplasmic. {ECO:0000250}.
TRANSMEM 68 88 Helical; Name=2. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 89 92 Extracellular. {ECO:0000250}.
TRANSMEM 93 113 Helical; Name=3. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 114 125 Cytoplasmic. {ECO:0000250}.
TRANSMEM 126 146 Helical; Name=4. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 147 164 Extracellular. {ECO:0000250}.
TRANSMEM 165 185 Helical; Name=5. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 186 311 Cytoplasmic. {ECO:0000250}.
TRANSMEM 312 332 Helical; Name=6. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 333 358 Extracellular. {ECO:0000250}.
TRANSMEM 359 379 Helical; Name=7. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 380 435 Cytoplasmic. {ECO:0000250}.
TRANSMEM 436 456 Helical; Name=8. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 457 459 Extracellular. {ECO:0000250}.
TRANSMEM 460 480 Helical; Name=9. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 481 542 Cytoplasmic. {ECO:0000250}.
TRANSMEM 543 563 Helical; Name=10. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 564 585 Extracellular. {ECO:0000250}.
TRANSMEM 586 606 Helical; Name=11. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 607 969 Cytoplasmic. {ECO:0000250}.
TRANSMEM 970 990 Helical; Name=12. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 991 1031 Extracellular. {ECO:0000250}.
TRANSMEM 1032 1052 Helical; Name=13. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1053 1095 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1096 1116 Helical; Name=14. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1117 1117 Extracellular. {ECO:0000250}.
TRANSMEM 1118 1138 Helical; Name=15. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1139 1209 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1210 1230 Helical; Name=16. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1231 1232 Extracellular. {ECO:0000250}.
TRANSMEM 1233 1253 Helical; Name=17. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1254 1543 Cytoplasmic. {ECO:0000250}.
DOMAIN 320 603 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 635 859 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 977 1262 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1298 1532 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 669 676 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1332 1339 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000250|UniProtKB:Q63120}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000250|UniProtKB:Q92887}.
MOD_RES 876 876 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 924 924 Phosphoserine.
{ECO:0000250|UniProtKB:Q92887}.
MOD_RES 928 928 Phosphoserine.
{ECO:0000250|UniProtKB:Q92887}.
MOD_RES 1436 1436 Phosphoserine.
{ECO:0000250|UniProtKB:Q92887}.
CARBOHYD 6 6 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 11 11 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1009 1009 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 613 613 Q -> R (in Ref. 1; AAL36985).
{ECO:0000305}.
SEQUENCE 1543 AA; 173671 MW; 2D73F2881511FEC0 CRC64;
MDEFCNSTFW NLSLLKSPEA DLPLCFEQTV LVWIPLGFLW LLAPWQLYRI YRSRTKRFAI
TKFYLAKQVF VVCLLILAAI DLSLALTEDT GQATIPPVKY TNPILYLCTW LLVLVIQHCR
QCCIQKNSWF LSMFWILSLL CGIFQFQTLI RALLQDSKSN MTYSCLFFVS YGFQIVILIL
SAFSESSDST HAPSATASFL SSVTFSWYDS TVLKGYKHPL TIEDVWDIEE NLKAKSLTSK
FKTIMTKDLQ KARQALQRRL KKSQQSPEGT SHGLTKKQSQ SQDVLVLEDS KKKKKKSEAT
KDFPKSWLVK ALFKTFYVVI LKSFILKLAH DILLFLNPQL LKFLIGFVKD PDSYPWVGYI
YAILMFSVTL IQSFFLQCYF QFCFVLGMTV RTTIIASVYK KALTLSNLAR RQYTIGETVN
LMSVDSQKLM DVTNYIHLLW SSVLQIALSI FFLWRELGPS ILAGVGLMVL LVPVNGVLAT
KIRKIQVQNM KNKDKRLKIM NEILSGIKIL KYFAWEPSFK EQVNSIRKKE LRNLLRFSQL
QTILIFILHL TPTLVSVITF SVYVLVDSQN VLNAEKAFTS ITLFNILRFP LAMLPMVISS
VIQASVSVDR LEQYLGSDDL DLSAIRHVCH FDKAVQFSEA SFTWDRDLEA TIQDVNLDIK
PGQLVAVVGT VGSGKSSLIS AMLGEMENVH GHITIKGSIA YVPQQAWIQN GTIKDNILFG
SEYDEKKYQR VIEACALLPD LEMLPGGDMA EIGEKGINLS GGQKHRVSLA RATYQDADIY
ILDDPLSAVD THVGKHIFNK VVGPNGLLSG KTRILVTHGI HFLPQVDEIV VLGKGTILEK
GSYSDLMDKK GVFAKNWKTF MKHSGPEGEA TVDNDSEEED GDCGLIPTVE EIPDDAASLT
MRRENSLRRT LSRSSRSGSR RGKSLKSSLK IKSVNALNKK EEVVKGQKLI KKEFVETGKV
KFSIYLKYLQ AVGWWSLLFI VIFYVLNYVA FIGTNLWLSA WTSDSEKQNG TDNSPSQRDM
RIGVFGALGI AQGIFLLSSS LWSIYACRNA SKTLHRQLLT NILRAPMSFF DTTPTGRIVN
RFAGDISTVD DTLPQTLRSW LLCFFGIVST LVMICMATPI FIIIIIPLSI LYVSVQVFYV
ATSRQLRRLD SVTKSPIYSH FSETVSGLPV IRAFEHQQRF LANSEKQIDT NQKCVFSWIT
SNRWLAIRLE LVGNLIVFCS ALLLVIYKNS LTGDTVGFVL SNALNITQTL NWLVRMTSEV
ETNIVAVERI NEYINVDNEA PWVTDKKPPA DWPKKGEIQF NNYQVRYRPE LDLVLKGITC
NIKSTEKVGV VGRTGAGKSS LTNCLFRILE SAGGQIIIDG IDIASIGLHD LRGRLTIIPQ
DPILFSGNLR MNLDPFNKYS DEEIWRALEL AHLKSFVAGL QLGLLHEVTE GGDNLSIGQR
QLLCLGRAVL RKSKILVLDE ATAAVDLETD SLIQTTIRNE FSQCTVITIA HRLHTIMDSD
KIMVLDSGKI VEYGSPEELL SNMGPFYLMA KEAGIESVNH TEL


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