ABCC3
entrez
8714
canonical
uniprot
O15438
canonical
ensembl
ENSG00000108846
resolver
ensp
ENSP00000285238
resolver
ensp
ENSP00000395160
resolver
genesymbol
ABCC3
resolver
genesymbol_syn
CMOAT2
resolver
genesymbol_syn
MLP2
resolver
genesymbol_syn
MRP3
resolver
hgnc
HGNC:54
resolver
uniprot
B2RPA9
resolver
uniprot
D3DTX9
resolver
uniprot
O60265
resolver
uniprot
O60922
resolver
uniprot
O75621
resolver
uniprot
O95078
resolver
uniprot
O95289
resolver
uniprot
O95290
resolver
uniprot
Q86VN9
resolver
uniprot
Q86X85
resolver
uniprot
Q9UN52
resolver
uniprot_entry
MRP3_HUMAN
resolver
uniprot_entry
Q86VN9_HUMAN
resolver
uniprot_sec
B2RPA9
resolver
uniprot_sec
D3DTX9
resolver
uniprot_sec
O60265
resolver
uniprot_sec
O60922
resolver
uniprot_sec
O75621
resolver
uniprot_sec
O95078
resolver
uniprot_sec
O95289
resolver
uniprot_sec
O95290
resolver
uniprot_sec
Q86X85
resolver
uniprot_sec
Q9UN52
resolver
amino_acid_sequence
MDALCGSGELGSKFWDSNLSVHTENPDLTPCFQNSLLAWVPCIYLWVALPCYLLYLRHHCRGYIILSHLSKLKMVLGVLLWCVSWADLFYSFHGLVHGRAPAPVFFVTPLVVGVTMLLATLLIQYERLQGVQSSGVLIIFWFLCVVCAIVPFRSKILLAKAEGEISDPFRFTTFYIHFALVLSALILACFREKPPFFSAKNVDPNPYPETSAGFLSRLFFWWFTKMAIYGYRHPLEEKDLWSLKEEDRSQMVVQQLLEAWRKQEKQTARHKASAAPGKNASGEDEVLLGARPRPRKPSFLKALLATFGSSFLISACFKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITLWVYVYVDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRIQQFLSQEELDPQSVERKTISPGYAITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFANFLCNYAPDEDQGHLEDSWTALEGAEDKEALLIEDTLSNHTDLTDNDPVTYVVQKQFMRQLSALSSDGEGQGRPVPRRHLGPSEKVQVTEAKADGALTQEEKAAIGTVELSVFWDYAKAVGLCTTLAICLLYVGQSAAAIGANVWLSAWTNDAMADSRQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVLFAALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEAPWVVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGMARDAGLA
uniprot
proteins
ec_number
7.6.2.-
uniprot
proteins
ec_number
7.6.2.2
uniprot
proteins
ec_number
7.6.2.3
uniprot
proteins
function
FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that hydrolyzes ATP to enable active transport of substrates conjugated with glucuronate, glutathione or sulfate. Operates at basolateral membranes of polarized cells such as hepatocytes and intestinal epithelial cells, where it mediates the efflux of conjugated substrates from intestine and liver into the bloodstream (PubMed:10359813, PubMed:11581266, PubMed:15083066, PubMed:29175180, PubMed:30959153, PubMed:31704245, PubMed:39993711, PubMed:37485728). Involved in enterohepatic recirculation of steroid glucuronates. Shares substrate specificity with MRP2, displaying higher affinity for both estrogen and androgen glucuronates such as 17beta-estradiol, estrone, testosterone and 5alpha-dihydrotestosterone glucuronates (PubMed:29175180, PubMed:30959153, PubMed:31704245, PubMed:37485728). Involved in sinusoidal efflux of mono- and bis-glucuronidated bilirubin from hepatocytes into the blood for renal uptake and excretion (PubMed:15083066). May selectively transport steroid sulfate conjugates. Has transporter activity toward androgen sulfates such as androsterone and dehydroepiandrosterone sulfates but is inactive toward estrone 3-sulfate (PubMed:29175180, PubMed:39993711). Can transport various bile acid conjugates such as taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate and taurolithocholate-3-sulfate. Does not contribute substantially to bile acids physiology, but provides an alternative route for the export of bile acids and glucuronate conjugates from cholestatic hepatocytes to avoid liver damage (By similarity). Can also transport glutathione conjugates such as leukotriene C4 (LTC4) (PubMed:11581266). Transports various xenobiotics. Confers resistance to anticancer drugs, methotrexate, tenoposide and etoposide, by decreasing accumulation of these drugs in cells (PubMed:10359813, PubMed:11581266). May contribute to the transport of organic compounds in testes across the blood-testis-barrier (Probable). {ECO:0000250|UniProtKB:B2RX12, ECO:0000250|UniProtKB:O88563, ECO:0000269|PubMed:10359813, ECO:0000269|PubMed:11581266, ECO:0000269|PubMed:15083066, ECO:0000269|PubMed:29175180, ECO:0000269|PubMed:30959153, ECO:0000269|PubMed:31704245, ECO:0000269|PubMed:37485728, ECO:0000269|PubMed:39993711, ECO:0000305|PubMed:35307651}.
uniprot
proteins
mass_dalton
169343
uniprot
proteins
mutagenesis
MUTAGEN 32..203; /note="Missing: No effect on the transporter activity toward estradiol-17-(beta-D-glucuronate). Does not alter protein thermal stability."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 318; /note="K->A: Markedly decreases the binding affinity for dehydroepiandrosterone 3-sulfate. Decreases dehydroepiandrosterone 3-sulfate- or estradiol-17-(beta-D-glucuronate)-stimulated ATPase activity by around 50%."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 371; /note="Y->A: Decreases the binding affinity for estradiol-17-(beta-D-glucuronate) and dehydroepiandrosterone 3-sulfate. Decreases estradiol-17-(beta-D-glucuronate)- or dehydroepiandrosterone 3-sulfate-stimulated ATPase activity by around 50%. Decreases the transporter activity toward estradiol-17-(beta-D-glucuronate) by around 75%."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 375; /note="F->A: Decreases the binding affinity for estradiol-17-(beta-D-glucuronate) and dehydroepiandrosterone 3-sulfate. Decreases estradiol-17-(beta-D-glucuronate)-stimulated ATPase activity and transporter activity by around 50%. Decreases dehydroepiandrosterone sulfate-stimulated ATPase activity by around 25%."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 429; /note="L->A: Decreases estradiol-17-(beta-D-glucuronate)- or dehydroepiandrosterone sulfate-stimulated ATPase activity by around 50%. No effect on transporter activity toward estradiol-17-(beta-D-glucuronate)."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 535; /note="T->A: Decreases dehydroepiandrosterone 3-sulfate-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 539; /note="W->A: Decreases the binding affinity for estradiol-17-(beta-D-glucuronate) and dehydroepiandrosterone 3-sulfate. Decreases estradiol-17-(beta-D-glucuronate)- or dehydroepiandrosterone sulfate-stimulated ATPase activity by around 50%. Markedly decreases the transporter activity toward estradiol-17-(beta-D-glucuronate) by around 75%."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1193; /note="R->A: Markedly decreases the binding affinity for estradiol-17-(beta-D-glucuronate) and dehydroepiandrosterone 3-sulfate. Markedly decreases estradiol-17-(beta-D-glucuronate)-stimulated ATPase activity by around 75%. Almost complete loss of transporter activity toward estradiol-17-(beta-D-glucuronate). Decreases dehydroepiandrosterone 3-sulfate-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1193; /note="R->K: Markedly decreases estradiol-17-(beta-D-glucuronate)- and dehydroepiandrosterone sulfate-stimulated ATPase activity by around 75% and 50%, respectively."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1193; /note="R->Q: Markedly decreases estradiol-17-(beta-D-glucuronate)- or dehydroepiandrosterone sulfate-stimulated ATPase activity by around 75% and 50%, respectively."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1238; /note="F->A: Decreases the binding affinity for estradiol-17-(beta-D-glucuronate) and dehydroepiandrosterone 3-sulfate substrates. Decreases estradiol-17-(beta-D-glucuronate)- or dehydroepiandrosterone sulfate-stimulated ATPase activity by around 50%."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1241; /note="N->A: Decreases estradiol-17-(beta-D-glucuronate)-stimulated ATPase activity. No effect on transporter activity toward estradiol-17-(beta-D-glucuronate)."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1242; /note="W->A: Decreases estradiol-17-(beta-D-glucuronate)- or dehydroepiandrosterone 3-sulfate-stimulated ATPase activity. No effect on transporter activity toward estradiol-17-(beta-D-glucuronate)."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1242; /note="W->F: No effect on estradiol-17-(beta-D-glucuronate)-stimulated ATPase activity. Decreases dehydroepiandrosterone 3-sulfate-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1242; /note="W->Y: No effect on estradiol-17-(beta-D-glucuronate)-stimulated ATPase activity. Decreases dehydroepiandrosterone 3-sulfate-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1245; /note="R->A: Markedly decreases the binding affinity for estradiol-17-(beta-D-glucuronate) and dehydroepiandrosterone 3-sulfate. Decreases estradiol-17-(beta-D-glucuronate)-stimulated ATPase activity by around 75%. Decreases dehydroepiandrosterone 3-sulfate-stimulated ATPase activity. Complete loss of the transporter activity toward estradiol-17-(beta-D-glucuronate)."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1245; /note="R->K: Decreases estradiol-17-(beta-D-glucuronate)-stimulated ATPase activity by around by around 50%. Decreases dehydroepiandrosterone 3-sulfate-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1245; /note="R->Q: Decreases estradiol-17-(beta-D-glucuronate)- or dehydroepiandrosterone 3-sulfate-stimulated ATPase activity by around 75% and 50%, respectively."; /evidence="ECO:0000269|PubMed:37485728"; MUTAGEN 1451; /note="E->Q: Loss-of-function. Abolishes substrate-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:37485728
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCC family
uniprot
proteins
protein_family
Conjugate transporter (TC 3.A.1.208) subfamily
uniprot
proteins
pubmed
10094960
uniprot
proteins
pubmed
10359813
uniprot
proteins
pubmed
11581266
uniprot
proteins
pubmed
14759258
uniprot
proteins
pubmed
15083066
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28408210
uniprot
proteins
pubmed
29175180
uniprot
proteins
pubmed
30959153
uniprot
proteins
pubmed
31704245
uniprot
proteins
pubmed
35307651
uniprot
proteins
pubmed
37485728
uniprot
proteins
pubmed
39993711
uniprot
proteins
pubmed
9270026
uniprot
proteins
pubmed
9738950
uniprot
proteins
pubmed
9813153
uniprot
proteins
pubmed
9827529
uniprot
proteins
pubmed
9889399
uniprot
proteins
sequence_length
1527
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:10094960, ECO:0000269|PubMed:10359813, ECO:0000269|PubMed:15083066, ECO:0000269|PubMed:28408210}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to the basolateral membrane of enterocytes (PubMed:28408210). Localized to the basal membrane of Sertoli cells (PubMed:35307651). {ECO:0000269|PubMed:28408210, ECO:0000269|PubMed:35307651}.
uniprot
proteins
transmembrane_region
TRANSMEM 38..54; /note="Helical; Name=1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 73..89; /note="Helical; Name=2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 107..122; /note="Helical; Name=3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 134..148; /note="Helical; Name=4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 172..189; /note="Helical; Name=5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 316..331; /note="Helical; Name=6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 353..367; /note="Helical; Name=7"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 431..444; /note="Helical; Name=8"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 450..465; /note="Helical; Name=9"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 532..549; /note="Helical; Name=10"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 569..584; /note="Helical; Name=11"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 968..988; /note="Helical; Name=12"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 1016..1032; /note="Helical; Name=13"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 1088..1104; /note="Helical; Name=14"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 1111..1123; /note="Helical; Name=15"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 1196..1211; /note="Helical; Name=16"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH"; TRANSMEM 1228..1243; /note="Helical; Name=17"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000305|PubMed:37485728, ECO:0000312|PDB:8HVH
uniprot
proteins