ID   PGP3_CAEEL              Reviewed;        1268 AA.
AC   P34713; Q20335;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Multidrug resistance protein pgp-3;
DE            EC=7.6.2.2;
DE   AltName: Full=P-glycoprotein C;
DE   AltName: Full=P-glycoprotein-related protein 3;
GN   Name=pgp-3; ORFNames=ZK455.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=1360540; DOI=10.1016/0022-2836(92)90855-e;
RA   Lincke C.R., The I., van Groenigen M., Borst P.;
RT   "The P-glycoprotein gene family of Caenorhabditis elegans. Cloning and
RT   characterization of genomic and complementary DNA sequences.";
RL   J. Mol. Biol. 228:701-711(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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   [3]
RP   TISSUE SPECIFICITY.
RC   STRAIN=Bristol N2;
RX   PubMed=8096815; DOI=10.1002/j.1460-2075.1993.tb05806.x;
RA   Lincke C.R., Broeks A., The I., Plasterk H.A., Borst P.;
RT   "The expression of two P-glycoprotein (pgp) genes in transgenic
RT   Caenorhabditis elegans is confined to intestinal cells.";
RL   EMBO J. 12:1615-1620(1993).
CC   -!- FUNCTION: Mediates ATP-dependent export of organic anions and
CC       xenobiotics from the cytoplasm. Hydrolyzes ATP with low efficiency (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- TISSUE SPECIFICITY: Intestinal cells. {ECO:0000269|PubMed:8096815}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR   EMBL; X65055; CAA46191.1; -; Genomic_DNA.
DR   EMBL; Z66567; CAA91495.1; -; Genomic_DNA.
DR   EMBL; Z66562; CAA91495.1; JOINED; Genomic_DNA.
DR   PIR; S27338; S27338.
DR   PIR; T22094; T22094.
DR   RefSeq; NP_509901.1; NM_077500.4.
DR   AlphaFoldDB; P34713; -.
DR   SMR; P34713; -.
DR   STRING; 6239.ZK455.7.2; -.
DR   iPTMnet; P34713; -.
DR   EPD; P34713; -.
DR   PaxDb; P34713; -.
DR   PeptideAtlas; P34713; -.
DR   PRIDE; P34713; -.
DR   EnsemblMetazoa; ZK455.7.1; ZK455.7.1; WBGene00003997.
DR   GeneID; 181326; -.
DR   KEGG; cel:CELE_ZK455.7; -.
DR   UCSC; ZK455.7; c. elegans.
DR   CTD; 181326; -.
DR   WormBase; ZK455.7; CE03818; WBGene00003997; pgp-3.
DR   eggNOG; KOG0055; Eukaryota.
DR   HOGENOM; CLU_000604_17_2_1; -.
DR   InParanoid; P34713; -.
DR   OMA; ANYILWL; -.
DR   OrthoDB; 186078at2759; -.
DR   PhylomeDB; P34713; -.
DR   PRO; PR:P34713; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00003997; Expressed in material anatomical entity and 3 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
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:0015562; F:efflux transmembrane transporter activity; ISS:WormBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:WormBase.
DR   GO; GO:0045087; P:innate immune response; IGI:WormBase.
DR   GO; GO:0010038; P:response to metal ion; IGI:WormBase.
DR   GO; GO:1990170; P:stress response to cadmium ion; IEP:WormBase.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1560.10; -; 3.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
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   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1268
FT                   /note="Multidrug resistance protein pgp-3"
FT                   /id="PRO_0000093343"
FT   TOPO_DOM        1..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        40..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        63..100
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        122..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        171..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        193..199
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        221..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        279..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        301..314
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        315..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        337..708
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        709..729
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        730..751
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        752..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        773..827
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        828..848
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        849
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        850..869
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        870..931
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        932..952
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        953..968
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        969..990
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        991..1268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          46..341
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          376..612
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          708..995
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1029..1265
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         411..418
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1064..1071
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        962
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        581..594
FT                   /note="Missing (in Ref. 1; CAA46191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        860
FT                   /note="A -> E (in Ref. 1; CAA46191)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1268 AA;  140291 MW;  A26E2DED84CA8163 CRC64;
     MKKTKVNPED DITLGKFTPK PSPQDSYQGN FFDVFRDADY KDYILFSGGL ILSAVNGALV
     PFNSLIFEGI ANALMEGESQ YQNGTINMPW FSSEIKMFCL RYFYLGVALF LCSYFANSCL
     YTLCERRLHC IRKKYLKSVL RQDAKWFDET TIGGLTQKMS SGIEKIKDGI GDKVGVLVGG
     VATFISGVSI GFYMCWQLTL VMMITVPLQL GSMYLSAKHL NRATKNEMSA YSNAGGMANE
     VIAGIRTVMA FNAQPFEINR YAHQLNEARR MGIRKAIILA ICTAFPLMLM FTCMAVAFWY
     GATLAAAGAV SSGAVFAVFW AVLIGTRRLG EAAPHLGAIT GARLAIHDIF KVIDHEPEIK
     CTSSEGKIPE KIQGKLTFDG IEFTYPTRPE LKILKGVSFE VNPGETVALV GHSGCGKSTS
     IGLLMRFYNQ CAGMIKLDGI PIQEYNIRWL RSTIGIVQQE PIIFVATVAE NIRMGDVLIT
     DQDIEEACKM ANAHEFICKL SDRYDTVIGA GAVQLSGGQK QRVAIARAIV RKPQILLLDE
     ATSALDTESE RMVQTALDKA SEGRTTLCIA HRLSTIRNAS KILVFDQGLI AERGTHDELI
     SKDDGIYASM VKAQEIERAK EDTTLDDEED EKTHRSFHRD SVTSDEEREL QQSLARDSTR
     LRQSMISTTT QVPEWEIENA REEMIEEGAM EASLFDIFKY ASPEMRNIII SLVFTLIRGF
     TWPAFSIVYG QLFKILSAGG DDVSIKALLN SLWFILLAFT GGISTLISGS LLGKAGETMS
     GRLRMDVFRN IMQQDASYFD DSRHNVGSLT SRLATDAPNV QAAIDQRLAE VLTGIVSLFC
     GVGVAFYYGW NMAPIGLATA LLLVVVQSSV AQYLKFRGQR DMDSAIEASR LVTESISNWK
     TVQALTKQEY MYDAFTAASK SPHRRAIVRG LWQSLSFALA GSFVMWNFAI AYMFGLWLIS
     NNWSTPYTVF QVIEALNMAS MSVMLAASYF PEYVRARISA GIMFTMIRQK SVIDNRGLTG
     DTPTIKGNIN MRGVYFAYPN RRRQLVLDGF NMSANFGQTV ALVGPSGCGK STTIQLIERY
     YDALCGSVKI DDSDIRDLSV KHLRDNIALV GQEPTLFNLT IRENITYGLE NITQDQVEKA
     ATLANIHTFV MGLPDGYDTS VGASGGRLSG GQKQRVAIAR AIVRDPKILL LDEATSALDT
     ESEKIVQEAL DKARLGRTCV VIAHRLSTIQ NADKIIVCRN GKAIEEGTHQ TLLARRGLYY
     RLVEKQSS