PGP1_CAEEL
ID PGP1_CAEEL Reviewed; 1321 AA.
AC P34712; Q21349;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Multidrug resistance protein pgp-1;
DE EC=7.6.2.2;
DE AltName: Full=P-glycoprotein A;
DE AltName: Full=P-glycoprotein-related protein 1;
GN Name=pgp-1; ORFNames=K08E7.9;
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: Energy-dependent efflux pump responsible for decreased drug
CC accumulation in multidrug-resistant cells.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; X65054; CAA46190.1; -; Genomic_DNA.
DR EMBL; Z77666; CAB01232.1; -; Genomic_DNA.
DR PIR; S27337; S27337.
DR PIR; T23476; T23476.
DR RefSeq; NP_502413.1; NM_070012.4.
DR PDB; 4F4C; X-ray; 3.40 A; A=1-1321.
DR PDBsum; 4F4C; -.
DR AlphaFoldDB; P34712; -.
DR SMR; P34712; -.
DR STRING; 6239.K08E7.9; -.
DR TCDB; 3.A.1.201.14; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P34712; -.
DR EPD; P34712; -.
DR PaxDb; P34712; -.
DR PeptideAtlas; P34712; -.
DR PRIDE; P34712; -.
DR EnsemblMetazoa; K08E7.9.1; K08E7.9.1; WBGene00003995.
DR GeneID; 178215; -.
DR KEGG; cel:CELE_K08E7.9; -.
DR UCSC; K08E7.9; c. elegans.
DR CTD; 178215; -.
DR WormBase; K08E7.9; CE11932; WBGene00003995; pgp-1.
DR eggNOG; KOG0055; Eukaryota.
DR GeneTree; ENSGT00970000195996; -.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; P34712; -.
DR OMA; CMALCFW; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; P34712; -.
DR BRENDA; 7.6.2.2; 1045.
DR PRO; PR:P34712; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003995; Expressed in adult organism 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:0093002; P:response to nematicide; IEP: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; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1321
FT /note="Multidrug resistance protein pgp-1"
FT /id="PRO_0000093342"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 371..753
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..774
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 798..818
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 874..894
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1017..1037
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1038..1321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 77..381
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 416..652
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 754..1043
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1077..1315
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 451..458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1112..1119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 850
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 156
FT /note="T -> I (in Ref. 1; CAA46190)"
FT /evidence="ECO:0000305"
FT HELIX 5..16
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 71..88
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 90..113
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 128..179
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 212..234
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 246..283
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 294..345
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 352..392
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 416..423
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 433..441
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 457..464
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 471..477
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 487..493
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 521..530
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 534..539
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 541..544
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 557..569
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 581..584
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 590..601
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 604..609
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 613..618
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 620..626
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 629..634
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 636..640
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 645..663
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 722..728
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 729..732
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 740..746
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 747..750
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 751..763
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 764..766
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 767..781
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 788..792
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 793..838
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 848..850
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 852..860
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 862..867
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 868..870
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 872..894
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 896..916
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 925..927
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 930..943
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 945..950
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 951..953
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 954..986
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 989..1003
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1006..1009
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1014..1025
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 1026..1028
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1033..1036
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1037..1056
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1077..1084
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1094..1102
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1107..1111
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1121..1125
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1132..1138
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 1143..1145
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1148..1152
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1155..1158
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1166..1168
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1169..1173
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1174..1177
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 1179..1181
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1184..1193
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1197..1201
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 1204..1207
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1209..1211
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 1212..1214
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1220..1233
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1237..1243
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1251..1260
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 1261..1263
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1264..1272
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1274..1277
FT /evidence="ECO:0007829|PDB:4F4C"
FT TURN 1278..1281
FT /evidence="ECO:0007829|PDB:4F4C"
FT STRAND 1283..1297
FT /evidence="ECO:0007829|PDB:4F4C"
FT HELIX 1299..1304
FT /evidence="ECO:0007829|PDB:4F4C"
SQ SEQUENCE 1321 AA; 145063 MW; 68094121B30E8746 CRC64;
MLRNGSLRQS LRTLDSFSLA PEDVLKTAIK TVEDYEGDNI DSNGEIKITR DAKEEVVNKV
SIPQLYRYTT TLEKLLLFIG TLVAVITGAG LPLMSILQGK VSQAFINEQI VINNNGSTFL
PTGQNYTKTD FEHDVMNVVW SYAAMTVGMW AAGQITVTCY LYVAEQMNNR LRREFVKSIL
RQEISWFDTN HSGTLATKLF DNLERVKEGT GDKIGMAFQY LSQFITGFIV AFTHSWQLTL
VMLAVTPIQA LCGFAIAKSM STFAIRETLR YAKAGKVVEE TISSIRTVVS LNGLRYELER
YSTAVEEAKK AGVLKGLFLG ISFGAMQASN FISFALAFYI GVGWVHDGSL NFGDMLTTFS
SVMMGSMALG LAGPQLAVLG TAQGAASGIY EVLDRKPVID SSSKAGRKDM KIKGDITVEN
VHFTYPSRPD VPILRGMNLR VNAGQTVALV GSSGCGKSTI ISLLLRYYDV LKGKITIDGV
DVRDINLEFL RKNVAVVSQE PALFNCTIEE NISLGKEGIT REEMVAACKM ANAEKFIKTL
PNGYNTLVGD RGTQLSGGQK QRIAIARALV RNPKILLLDE ATSALDAESE GIVQQALDKA
AKGRTTIIIA HRLSTIRNAD LIISCKNGQV VEVGDHRALM AQQGLYYDLV TAQTFTDAVD
SAAEGKFSRE NSVARQTSEH EGLSRQASEM DDIMNRVRSS TIGSITNGPV IDEKEERIGK
DALSRLKQEL EENNAQKTNL FEILYHARPH ALSLFIGMST ATIGGFIYPT YSVFFTSFMN
VFAGNPADFL SQGHFWALMF LVLAAAQGIC SFLMTFFMGI ASESLTRDLR NKLFRNVLSQ
HIGFFDSPQN ASGKISTRLA TDVPNLRTAI DFRFSTVITT LVSMVAGIGL AFFYGWQMAL
LIIAILPIVA FGQYLRGRRF TGKNVKSASE FADSGKIAIE AIENVRTVQA LAREDTFYEN
FCEKLDIPHK EAIKEAFIQG LSYGCASSVL YLLNTCAYRM GLALIITDPP TMQPMRVLRV
MYAITISTST LGFATSYFPE YAKATFAGGI IFGMLRKISK IDSLSLAGEK KKLYGKVIFK
NVRFAYPERP EIEILKGLSF SVEPGQTLAL VGPSGCGKST VVALLERFYD TLGGEIFIDG
SEIKTLNPEH TRSQIAIVSQ EPTLFDCSIA ENIIYGLDPS SVTMAQVEEA ARLANIHNFI
AELPEGFETR VGDRGTQLSG GQKQRIAIAR ALVRNPKILL LDEATSALDT ESEKVVQEAL
DRAREGRTCI VIAHRLNTVM NADCIAVVSN GTIIEKGTHT QLMSEKGAYY KLTQKQMTEK
K
