MRP9_RAT
ID MRP9_RAT Reviewed; 1366 AA.
AC Q6Y306; Q6Y305;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=ATP-binding cassette sub-family C member 12;
DE AltName: Full=Multidrug resistance-associated protein 9;
GN Name=Abcc12; Synonyms=Mrp9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RA Shimizu H., Ishikawa T.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=17472575; DOI=10.1042/bj20070292;
RA Ono N., Van der Heijden I., Scheffer G.L., Van de Wetering K.,
RA Van Deemter E., De Haas M., Boerke A., Gadella B.M., De Rooij D.G.,
RA Neefjes J.J., Groothuis T.A., Oomen L., Brocks L., Ishikawa T., Borst P.;
RT "Multidrug resistance-associated protein 9 (ABCC12) is present in mouse and
RT boar sperm.";
RL Biochem. J. 406:31-40(2007).
CC -!- FUNCTION: Probable transporter, its substrate specificity is unknown.
CC {ECO:0000250|UniProtKB:Q96J65}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96J65}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to the midpiece of the sperm tail.
CC {ECO:0000250|UniProtKB:Q80WJ6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6Y306-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q6Y306-2; Sequence=VSP_021099;
CC -!- TISSUE SPECIFICITY: High expressed in testis.
CC {ECO:0000269|PubMed:17472575}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- CAUTION: Does not transport any of the organic anions transported by
CC the other multidrug resistance-associated proteins (MRPs) in vesicular
CC transport assays, nor does it confer resistance to cytotoxic agents in
CC intact cell assays. {ECO:0000250|UniProtKB:Q96J65}.
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DR EMBL; AY188179; AAO74586.1; -; mRNA.
DR EMBL; AY188180; AAO74587.1; -; mRNA.
DR RefSeq; NP_955409.1; NM_199377.1. [Q6Y306-1]
DR AlphaFoldDB; Q6Y306; -.
DR SMR; Q6Y306; -.
DR STRING; 10116.ENSRNOP00000021095; -.
DR GlyGen; Q6Y306; 3 sites.
DR iPTMnet; Q6Y306; -.
DR PhosphoSitePlus; Q6Y306; -.
DR PaxDb; Q6Y306; -.
DR PRIDE; Q6Y306; -.
DR GeneID; 291923; -.
DR KEGG; rno:291923; -.
DR CTD; 94160; -.
DR RGD; 735100; Abcc12.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; Q6Y306; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q6Y306; -.
DR PRO; PR:Q6Y306; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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: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; IPR030250; ABCC12.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF10; PTHR24223:SF10; 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 Alternative splicing; ATP-binding; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1366
FT /note="ATP-binding cassette sub-family C member 12"
FT /id="PRO_0000253580"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 788..808
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 850..870
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 943..963
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 123..404
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 478..702
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 792..1089
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1127..1361
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 472..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514..521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1161..1168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 978
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 142..220
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021099"
SQ SEQUENCE 1366 AA; 152965 MW; 632672C4565C5C15 CRC64;
MVGEDPYLIS DLDRRGRRRS FAERYDPSLK TMIPMRPYAR LAPNPVDDAG LLSFATFSWL
TPVMIRSYKH TLTVDTLPPL SPYDSSDVNA KRLQILWDEE IERVGPERAS LGRVVWKFQR
TRVLMDVVAN ILCIIMAALG PTVLIHQILQ HVTNISSGHI GISICLCLAL FATEFTKVLF
RALAWAINYR TAIRLKVALS TLIFKNLLSF KTLTHISAGE VLNVLSSDSY SLFEAALFCP
LPATIPILMV VCAVYAFFIL GSTALVGICV YLIFIPIQMF MAKLNSAFRR SAISVTDKRV
QTMNEFLTCI KLIKMYAWEK SFMNTIHDIR KREKKLLEKA GYVQSGNSAL APIVSTIAIV
STFTCHIFLK RTLTAPVAFS VIAMFNVMKF SIAILPFSVK AVAEASVSLR RMKKILVAKS
PPSYITQPED PDTILLLANA TLTWEQEINR KRGPSKTQDQ RRHVFKKQRA ELYSEQSLSD
QGVASPERQS GSPKSVLHNI SFVVRKGKVL GICGNVGSGK SSLISALLGQ MQLQKGVVAA
SGPLAYVSQQ AWIFHGNVRE NILFGEKYNH QRYQHTVHVC GLQKDLNSLP YGDLTEIGER
GVNLSGGQRQ RISLARAVYA NRQLYLLDDP LSAVDAHVGK HVFEECIKKT LKGKTVVLVT
HQLQFLESCD EVILLEDGEI CEKGTHKELM EERGRYAKLI HNLRGLQFKD PEHIYNVAMV
ETLKESQAQR DEDAVLASGD ERDEGKEPET EEFVDIKAPV HQLIQIESPQ EGIVTWKTYH
TYIKASGGYL VSFLVLCLFF LMMGSSAFST WWLGLWLDSG SQVICAPQSN ETACNVNQTL
QDTKHHMYQL VYIASMMSVL TFGIIKGFTF TNTTLMASSS LHNRVFNKIV SSPMSFFDTT
PTGRLMNRFS KDMDELDVRL PFHAENFLQQ FSMVVFILVI MAASFPVVLV VLAGLAILFF
ILLRIFHRGV QELKQVENIS RSPWFSHITS SMQGLGVIHA YDKKDDCISK FKALNDENSS
HLLYFNCALR WFALRMDILM NIVTFVVALL VTLSFSSISA SSKGLSLSYI IQLSGLLQVC
VRTGTETQAK FTSAELMREY ISTCVPEHTQ SFKVGTCPKD WPSRGEITFK DYRMRYRDNT
PLVLDGLNLN IQSGQTVGIV GRTGSGKSSL GMALFRLVEP ASGTIFIDEV DICTVGLEEL
RTKLTMIPQD PVLFVGTVRY NLDPLGSHTD EMLWHVLERT FMRDTIMKLP EKLQAEVTEN
GENFSVGERQ LLCMARALLR NSKIILLDEA TASMDSKTDT LVQSTIKEAF KSCTVLTIAH
RLNTVLNCDL VLVMENGKVI EFDKPEVLAE KPDSAFAMLL AAEVGL
