MRP7_CAEEL
ID MRP7_CAEEL Reviewed; 1525 AA.
AC Q9U2G5;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Multidrug resistance protein mrp-7 {ECO:0000303|PubMed:24266639};
GN Name=mrp-7 {ECO:0000312|WormBase:Y43F8C.12};
GN ORFNames=Y43F8C.12 {ECO:0000312|WormBase:Y43F8C.12};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY METHYLMERCURY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24266639; DOI=10.1111/jnc.12515;
RA VanDuyn N., Nass R.;
RT "The putative multidrug resistance protein MRP-7 inhibits methylmercury-
RT associated animal toxicity and dopaminergic neurodegeneration in
RT Caenorhabditis elegans.";
RL J. Neurochem. 128:962-974(2014).
CC -!- FUNCTION: Negatively regulates cellular toxicity by mediating the
CC export of environmental toxicants such as methylmercury out of the cell
CC (PubMed:24266639). Plays a role in inhibiting methylmercury-induced
CC dopamine (DA) motor neuron degeneration (PubMed:24266639). Not involved
CC in Mn(2+)- or Al(3+)-associated toxicity (PubMed:24266639).
CC {ECO:0000269|PubMed:24266639}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in head neurons, including the dopamine
CC (DA) motor neuron, and other cells in the body.
CC {ECO:0000269|PubMed:24266639}.
CC -!- INDUCTION: Up-regulated in response to environmental toxicants such as
CC methylmercury. {ECO:0000269|PubMed:24266639}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in increased
CC death in response to the environmental toxicant methylmercury
CC (PubMed:24266639). Furthermore, in response to methylmercury, RNAi-
CC mediated knockdown results in the accumulation of the methylmercury in
CC cells, the subsequent increase of gst-1, hsp-4, hsp-6, and hsp-16.1
CC gene expression, and in dopamine (DA) motor neuron degeneration
CC (PubMed:24266639). {ECO:0000269|PubMed:24266639}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; BX284605; CAA21622.4; -; Genomic_DNA.
DR RefSeq; NP_507812.3; NM_075411.4.
DR AlphaFoldDB; Q9U2G5; -.
DR SMR; Q9U2G5; -.
DR STRING; 6239.Y43F8C.12; -.
DR EPD; Q9U2G5; -.
DR PaxDb; Q9U2G5; -.
DR PeptideAtlas; Q9U2G5; -.
DR EnsemblMetazoa; Y43F8C.12.1; Y43F8C.12.1; WBGene00003413.
DR GeneID; 180289; -.
DR KEGG; cel:CELE_Y43F8C.12; -.
DR UCSC; Y43F8C.12; c. elegans.
DR CTD; 180289; -.
DR WormBase; Y43F8C.12; CE43255; WBGene00003413; mrp-7.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000166156; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q9U2G5; -.
DR OMA; ELHEYST; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q9U2G5; -.
DR Reactome; R-CEL-189483; Heme degradation.
DR Reactome; R-CEL-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-9707564; Cytoprotection by HMOX1.
DR Reactome; R-CEL-9749641; Aspirin ADME.
DR Reactome; R-CEL-9753281; Paracetamol ADME.
DR Reactome; R-CEL-9754706; Atorvastatin ADME.
DR Reactome; R-CEL-9758890; Transport of RCbl within the body.
DR PRO; PR:Q9U2G5; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003413; Expressed in adult organism and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0051597; P:response to methylmercury; IMP:WormBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 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; IPR005292; Multidrug-R_assoc.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1525
FT /note="Multidrug resistance protein mrp-7"
FT /id="PRO_0000453174"
FT TOPO_DOM 1..24
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..94
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..139
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..165
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 166..186
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 347..367
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 368..434
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 435..455
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 456..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 536..556
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 557..561
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 562..582
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 583..953
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 954..974
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 975..1005
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1006..1026
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 1027..1068
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1069..1089
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 1090
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1091..1111
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 1112..1184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1185..1205
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 1206..1525
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 305..587
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 622..849
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 959..1245
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1282..1516
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 900..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 659..666
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1316..1323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1525 AA; 171048 MW; 7A2CA935E9249CFD CRC64;
MLSSFCGDGH PFSTGLPNVS ICAQHTVLVW VPAAFFLLTL PFLSAQCHLT AQRFARLPFS
AHFIIKLLLV AFLAANSLAT WCYVLFSKNS YAAAYYVYPG LWVLVWTGTF LVHLIRLRCG
LVSSGIQHVT SLIFLLCGAP EFYQWIRMEN SNSFPNDLTT TDSAQFLSIA YLSWYSALIL
YTFSLCFADP RGAKTDDEKA SSKSAASPEL QSSFLNRLTL WWFNSIPWTG ARRDLEIDDI
FELNERSGTE FLSELWESFW EPKRLKYIHD TSIWAKKDPS EQEKDPVVIP SVVSSLFMMF
RWEFLLASTL KFVSDTMQFA SPFLLHELLN FISAKNAPFW KGMALSILMF SVSELRSLIL
NGYFYIMFRM GTKIQTSLTA AVYKKTLLIS NSARRDRTVG EIVNLMAIDV ERFQMITPQI
QQFWSCPYQI TFALVYLFIT LGYSALPGVV IMVIFVPMNI ISSMIVRKWQ IEQMKLKDER
TKMVNEVLNG IKVVKLYAWE VPMEAYIDEI RTKELALIKK SAMVRNILDS FNTASPFLVA
LFSFGTFVLS NPSHLLTPQI AFVSLALFNQ LRSPMTMIAL LINQAVQAVV SNKRLKEFLV
AEELDEKCVD RSVNIERSHN AVRVENLTAS WDPEEAAGEK TLQDVDLTAP RNSLIAVVGK
VGSGKSSLLQ ALLGEMGKLR GRIGVNGRVA YVPQQPWIQN MTLRDNITFG RPFDRKRYDQ
VLYACALKAD IKILPAGDQT EIGEKGINLS GGQKARVSLA RAVYQNLDVY LLDDPLSAVD
AHVGRHIFEK VIGPNGLLRE KTRILVTHGL TYTKMADEIL VMLEGKIEES GTFEHLIKRR
GLFFDFMEEY KSGSDNSSEA GGSQDDDFEA IGGEIQDYMN PEDVVLTVTN DLDETIRTPE
LTTQISTMSS PEKPPTGTSP AAATESQNKL IKKEGIAQGK VEIATYQLYV KAAGYLLSIA
FIGFFIVYMT LQILRSFWLS AWSDEYDPDS PSAHPMAKGW RLGVYGALGF SETACFFVAL
LALVFVGQRA SKNLHGPLIH NLMRSPMSFY DTTPLGRILN RCAKDIETID MMLPMNFRYL
VMCVLQVAFT LIVIIISTPL FAVVILPLAL IYLIFLRYYV PTSRQLKRLE SVHRSPIYSH
FGETIQGAAS IRAFGKVDEF RQDSGRILDT FIRCRYSSLV SNRWLAVRLE FVGNCIIFFA
ALFAVLSKEF GWITSPGVIG VSVSYALNIT EVLNFAVRQV SEIEANIVSV ERVNEYTNTP
NEAPWRIEGR EPAPGWPSRG VVKFDGYSTR YREGLDLVLH DISADVAAGE KIGIVGRTGA
GKSSFALALF RMIEAAGGRI VIDDVEVSQI GLHDLRSNIT IIPQDPVLFS GTLRFNLDPF
FTYSDDQIWR ALELAHLKHF AAGLPDGLLY KISEAGENLS VGQRQLVALA RALLRHTRVL
VLDEATAAVD VATDALIQET IREEFKECTV FTIAHRLNTI MDYDRIMVLD KGSILEFDTP
DALMADKNSA FAKMVADAAE QDKHE
