MRP9_MOUSE
ID MRP9_MOUSE Reviewed; 1366 AA.
AC Q80WJ6; B2RRF4; Q80WJ2; Q80WJ3; Q8C0P3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=12801629; DOI=10.1016/s0378-1119(03)00504-3;
RA Shimizu H., Taniguchi H., Hippo Y., Hayashizaki Y., Aburatani H.,
RA Ishikawa T.;
RT "Characterization of the mouse Abcc12 gene and its transcript encoding an
RT ATP-binding cassette transporter, an orthologue of human ABCC12.";
RL Gene 310:17-28(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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:0000269|PubMed:17472575}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80WJ6-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q80WJ6-2; Sequence=VSP_021093, VSP_021094;
CC Name=3; Synonyms=A;
CC IsoId=Q80WJ6-3; Sequence=VSP_021097, VSP_021098;
CC Name=4;
CC IsoId=Q80WJ6-4; Sequence=VSP_021095, VSP_021096;
CC -!- TISSUE SPECIFICITY: Widely expressed at low level (PubMed:12801629,
CC PubMed:16141072, PubMed:17472575). Highly expressed in testis by
CC Sertoli cells and Leydig cells (PubMed:12801629, PubMed:16141072).
CC Detected in testicular germ cells and sperm (at protein level)
CC (PubMed:17472575). {ECO:0000269|PubMed:12801629,
CC ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:17472575}.
CC -!- DEVELOPMENTAL STAGE: First detected at 3 weeks of age IN the pachytene
CC spermatocytes. During germ cell differentiation in the adult testis,
CC pachytene spermatocytes in stage VI of the epithelial cycle are the
CC first germ cells to show MRP9 expression.
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; AF502146; AAP30800.1; -; mRNA.
DR EMBL; AF514414; AAP30871.1; -; mRNA.
DR EMBL; AF514415; AAP30872.1; -; mRNA.
DR EMBL; AK030123; BAC26794.1; -; mRNA.
DR EMBL; AK133175; BAE21541.1; -; mRNA.
DR EMBL; BC138380; AAI38381.1; -; mRNA.
DR EMBL; BC138381; AAI38382.1; -; mRNA.
DR EMBL; BC171952; AAI71952.1; -; mRNA.
DR CCDS; CCDS22502.1; -. [Q80WJ6-1]
DR RefSeq; NP_766500.3; NM_172912.4. [Q80WJ6-1]
DR RefSeq; XP_006531047.1; XM_006530984.3. [Q80WJ6-1]
DR AlphaFoldDB; Q80WJ6; -.
DR SMR; Q80WJ6; -.
DR STRING; 10090.ENSMUSP00000122402; -.
DR GlyGen; Q80WJ6; 2 sites.
DR iPTMnet; Q80WJ6; -.
DR PhosphoSitePlus; Q80WJ6; -.
DR MaxQB; Q80WJ6; -.
DR PaxDb; Q80WJ6; -.
DR PRIDE; Q80WJ6; -.
DR ProteomicsDB; 290324; -. [Q80WJ6-1]
DR ProteomicsDB; 290325; -. [Q80WJ6-2]
DR ProteomicsDB; 290326; -. [Q80WJ6-3]
DR ProteomicsDB; 290327; -. [Q80WJ6-4]
DR Antibodypedia; 28132; 214 antibodies from 28 providers.
DR DNASU; 244562; -.
DR Ensembl; ENSMUST00000080115; ENSMUSP00000079014; ENSMUSG00000036872. [Q80WJ6-1]
DR Ensembl; ENSMUST00000129898; ENSMUSP00000122577; ENSMUSG00000036872. [Q80WJ6-4]
DR Ensembl; ENSMUST00000131423; ENSMUSP00000122402; ENSMUSG00000036872. [Q80WJ6-1]
DR Ensembl; ENSMUST00000152438; ENSMUSP00000114582; ENSMUSG00000036872. [Q80WJ6-4]
DR GeneID; 244562; -.
DR KEGG; mmu:244562; -.
DR UCSC; uc009mqk.1; mouse. [Q80WJ6-1]
DR UCSC; uc009mql.1; mouse. [Q80WJ6-4]
DR CTD; 94160; -.
DR MGI; MGI:2441679; Abcc12.
DR VEuPathDB; HostDB:ENSMUSG00000036872; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000159578; -.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; Q80WJ6; -.
DR OMA; IKGFIFT; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q80WJ6; -.
DR TreeFam; TF105202; -.
DR BioGRID-ORCS; 244562; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q80WJ6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q80WJ6; protein.
DR Bgee; ENSMUSG00000036872; Expressed in spermatocyte and 30 other tissues.
DR ExpressionAtlas; Q80WJ6; baseline and differential.
DR Genevisible; Q80WJ6; MM.
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:0005739; C:mitochondrion; HDA:MGI.
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 1: Evidence at protein 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_0000253579"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 152..172
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 931..951
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 459..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 470..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Polar residues"
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 978
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 665..686
FT /note="FLESCDEVILLEDGEICEKGTH -> KVALPEQGIEMVGDTDESCSHS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12801629"
FT /id="VSP_021093"
FT VAR_SEQ 687..1366
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12801629"
FT /id="VSP_021094"
FT VAR_SEQ 735..738
FT /note="VLAS -> GTVR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021095"
FT VAR_SEQ 739..1366
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021096"
FT VAR_SEQ 758..774
FT /note="APAHQLIQTESPQEGIV -> VEGTSGSQNVKIWRRKS (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:12801629"
FT /id="VSP_021097"
FT VAR_SEQ 775..1366
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12801629"
FT /id="VSP_021098"
SQ SEQUENCE 1366 AA; 153060 MW; FAE080A60BB4B6C0 CRC64;
MVGEGPYLIS DLDRRGHRRS FAERYDPSLK TMIPVRPRAR LAPNPVDDAG LLSFATFSWL
TPVMIRSYKH TLTVDTLPPL SPYDSSDINA KRFQILWEEE IKRVGPEKAS LGRVVWKFQR
TRVLMDVVAN ILCIVMAALG PTVLIHQILQ HITSISSGHI GIGICLCLAL FTTEFTKVLF
WALAWAINYR TAIRLKVALS TLIFENLLSF KTLTHISAGE VLNILSSDSY SLFEAALFCP
LPATIPILMV VCAVYAFFIL GSTALVGISV YLIFIPIQMF MAKLNSTFRR SAISVTDKRV
QTMNEFLTCI KLIKMYAWEE SFINTIHDIR KREKKLLEKA GYVQSGNSAL APIVSTIAIV
STFTCHIFLK RKLTAPVAFS VIAMFNVMKF SIAILPFSVK AVAEASVSLR RMKKILIAKS
PPSYITQPED PDTILLLANA TLTWEQEINR KSDPPKAQIQ KRHVFKKQRP ELYSEQSRSD
QGVASPEWQS GSPKSVLHNI SFVVRKGKVL GICGNVGSGK SSLISALLGQ MQLQKGVVAV
NGPLAYVSQQ AWIFHGNVRE NILFGEKYNH QRYQHTVHVC GLQKDLNSLP YGDLTEIGER
GVNLSGGQRQ RISLARAVYA NRQLYLLDDP LSAVDAHVGK HVFEECIKKT LKGKTVVLVT
HQLQFLESCD EVILLEDGEI CEKGTHKELM EERGRYAKLI HNLRGLQFKD PEHIYNVAMV
ETLKESPAQR DEDAVLASGD EKDEGKEPET EEFVDTNAPA HQLIQTESPQ EGIVTWKTYH
TYIKASGGYL VSFLVLCLFF LMMGSSAFST WWLGIWLDRG SQVVCASQNN KTACNVDQTL
QDTKHHMYQL VYIASMVSVL MFGIIKGFTF TNTTLMASSS LHNRVFNKIV RSPMSFFDTT
PTGRLMNRFS KDMDELDVRL PFHAENFLQQ FFMVVFILVI MAAVFPVVLV VLAGLAVIFL
ILLRIFHRGV QELKQVENIS RSPWFSHITS SIQGLGVIHA YDKKDDCISK FKTLNDENSS
HLLYFNCALR WFALRMDILM NIVTFVVALL VTLSFSSISA SSKGLSLSYI IQLSGLLQVC
VRTGTETQAK FTSAELLREY ILTCVPEHTH PFKVGTCPKD WPSRGEITFK DYRMRYRDNT
PLVLDGLNLN IQSGQTVGIV GRTGSGKSSL GMALFRLVEP ASGTIIIDEV DICTVGLEDL
RTKLTMIPQD PVLFVGTVRY NLDPLGSHTD EMLWHVLERT FMRDTIMKLP EKLQAEVTEN
GENFSVGERQ LLCMARALLR NSKIILLDEA TASMDSKTDT LVQSTIKEAF KSCTVLTIAH
RLNTVLNCDL VLVMENGKVI EFDKPEVLAE KPDSAFAMLL AAEVGL
