MDR2_CRIGR
ID MDR2_CRIGR Reviewed; 1276 AA.
AC P21449;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Multidrug resistance protein 2;
DE EC=7.6.2.2;
DE AltName: Full=P-glycoprotein 2;
GN Name=PGY2; Synonyms=PGP2;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1685679; DOI=10.3109/10425179109039677;
RA Endicott J.A., Sarangi F., Ling V.;
RT "Complete cDNA sequences encoding the Chinese hamster P-glycoprotein gene
RT family.";
RL DNA Seq. 2:89-101(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 622-1276.
RX PubMed=2893255; DOI=10.1128/mcb.7.11.4075-4081.1987;
RA Endicott J.A., Juranka P.F., Sarangi F., Gerlach J.H., Deuchars K.L.,
RA Ling V.;
RT "Simultaneous expression of two P-glycoprotein genes in drug-sensitive
RT Chinese hamster ovary cells.";
RL Mol. Cell. Biol. 7:4075-4081(1987).
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 -!- MISCELLANEOUS: PGP isoforms differ in their drug transport
CC capabilities: PGP1 and PGP2 can mediate MDR, while PGP3 apparently
CC cannot.
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; M60041; AAA68884.1; -; mRNA.
DR EMBL; M17896; AAA37007.1; -; mRNA.
DR PIR; B27126; DVHY2C.
DR RefSeq; NP_001230918.1; NM_001243989.1.
DR AlphaFoldDB; P21449; -.
DR SMR; P21449; -.
DR STRING; 10029.NP_001230918.1; -.
DR PRIDE; P21449; -.
DR GeneID; 100682537; -.
DR KEGG; cge:100682537; -.
DR CTD; 18669; -.
DR eggNOG; KOG0055; Eukaryota.
DR OrthoDB; 186078at2759; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
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; Glycoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Repeat; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1276
FT /note="Multidrug resistance protein 2"
FT /id="PRO_0000093340"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 346..708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 852..872
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 935..955
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 993..1276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..356
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 391..627
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 709..998
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1033..1271
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 635..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 426..433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1068..1075
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21440"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1276 AA; 141058 MW; 5096B1385628812D CRC64;
MEFEEDFSAR ADKDFLKMGR KSKKEKKEKE NPNVGIFGMF RYADWLDKLY MVLGTLAAVL
HGTSLPLLML VFGNMTDSFT KAETSIWPNM TNQSEINNTE VISGSLEEDM ATYAYYYTGI
GAGVLIVAYI QVSFWCLAAG RQINKIRQKF FHAIMNQEIG WFDVHDIGEL NTRLTDDVSK
INDGIGDKIG MFFQSIATFL AAFIVGFISG WKLTLVILAV SPLIGLSSAM WAKVLTSFTN
KELQAYAKAG AVAEEVLAAI RTVIAFGGQN KELERYNKNL EEAKNVGIKK AVTANISIGI
AYLLVYASYA LAFWYGTSLV LSNEYSVGQV LTVFFSILFG TFSIGHIAPN IEVFANARGA
AYEIFKIIDN EPSIDSFSTQ GHKPDSVMGN LEFKNVHFSY PSRSGIKILK GLNLKVQSGQ
TVALVGKSGC GKSTTVQLLQ RLYDPTEGVV SIDGQDIRTI NVRYLREIIG VVSQEPVLFA
TTIAENIRYG RENVTMDEIE KAVKEANAYD FIMKLPHKFD TLVGERGAQL SGGQKQRIAI
ARALVRNPKI LLLDEATSAL DTESEAVVQA ALDKAREGRT TIVIAHRLST VRNADVIAGF
DGGVIVEQGN HEELMKEKGI YCRLVMMQTR GNEVELGSEA DGSQSDTIAS ELTSEEFKSP
SVRKSTCRSI CGSQDQERRV SVKEAQDEDV PLVSFWGILK LNITEWPYLV VGVLCAVING
CMQPVFSIVF SGIIGVFTRD DDPKTKQQNC NLFSLFFLVM GMICFVTYFF QGFTFGKAGE
ILTKRLRYMV FKSMLRQDIS WFDDHRNSTG ALTTRLASDA ANVKGAMSSR LAGITQNVAN
LGTGIIISLV YGWQLTLLLV VIAPLIILSG MMEMKVLSGQ ALKDKKELEV SGKIATEAIE
NFRTVVSLTR EQKFENMYAQ SLQIPYRNAL KKAHVFGITF SFTQAMMYFS YAACFRFGAY
LVAHQIMTFE NVMLVFSAVV FGAIAAGNAS SFAPDYAKAK VSASHIIRIM EKIPSIDSYS
TRGLKPNWLE GNVKFNEVVF NYPTRPDIPV LQGLSLEVKK GQTLALVGSS GCGKSTVVQL
LERFYDPMAG TVFLDGKEIK QLNVQWLRAH LGIVSQEPIL FDCSIAENIA YGDNSRVVSQ
DEIERAAKEA NIHQFIESLP DKYNTRVGDK GTQLSGGQKQ RIAIARALVR QPHILLLDEA
TSALDTESEK VVQEALDKAR EGRTCIVIAH RLSTIQNADL IVVIQNGKVK EHGTHQQLLA
QKGIYFSMVQ AGAKRL
