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Multidrug resistance-associated protein 5 (ATP-binding cassette sub-family C member 5) (Multi-specific organic anion transporter C) (MOAT-C) (SMRP)

 MRP5_MOUSE              Reviewed;        1436 AA.
Q9R1X5; O88284; Q5CZY2;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 2.
12-SEP-2018, entry version 148.
RecName: Full=Multidrug resistance-associated protein 5;
AltName: Full=ATP-binding cassette sub-family C member 5;
AltName: Full=Multi-specific organic anion transporter C;
Short=MOAT-C;
AltName: Full=SMRP;
Name=Abcc5; Synonyms=Abcc5a, Mrp5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=10721709; DOI=10.1016/S0378-1119(99)00529-6;
Suzuki T., Sasaki H., Kuh H.J., Agui M., Tatsumi Y., Tanabe S.,
Terada M., Saijo N., Nishio K.;
"Detailed structural analysis on both human MRP5 and mouse mrp5
transcripts.";
Gene 242:167-173(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 261-266, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1302-1436.
Suzuki T., Kuh H., Nishio K.;
"Moleculer cloning of mouse homologue of SMRP/MRP5.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-505; SER-509 AND
THR-513, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Acts as a multispecific organic anion pump which can
transport nucleotide analogs. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB019003; BAA76609.1; -; mRNA.
EMBL; AB012090; BAA32782.1; -; mRNA.
EMBL; CH466521; EDK97565.1; -; Genomic_DNA.
EMBL; BC090629; AAH90629.1; -; mRNA.
CCDS; CCDS28045.1; -.
RefSeq; NP_038818.2; NM_013790.2.
RefSeq; XP_006522271.1; XM_006522208.3.
UniGene; Mm.20845; -.
ProteinModelPortal; Q9R1X5; -.
SMR; Q9R1X5; -.
STRING; 10090.ENSMUSP00000078158; -.
iPTMnet; Q9R1X5; -.
PhosphoSitePlus; Q9R1X5; -.
MaxQB; Q9R1X5; -.
PaxDb; Q9R1X5; -.
PeptideAtlas; Q9R1X5; -.
PRIDE; Q9R1X5; -.
DNASU; 27416; -.
Ensembl; ENSMUST00000079158; ENSMUSP00000078158; ENSMUSG00000022822.
Ensembl; ENSMUST00000115547; ENSMUSP00000111209; ENSMUSG00000022822.
GeneID; 27416; -.
KEGG; mmu:27416; -.
UCSC; uc007ypp.1; mouse.
CTD; 10057; -.
MGI; MGI:1351644; Abcc5.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00880000137856; -.
HOVERGEN; HBG108314; -.
InParanoid; Q9R1X5; -.
KO; K05668; -.
OMA; YPAMMFV; -.
OrthoDB; EOG091G01TC; -.
TreeFam; TF105202; -.
Reactome; R-MMU-2142850; Hyaluronan biosynthesis and export.
Reactome; R-MMU-382556; ABC-family proteins mediated transport.
ChiTaRS; Abcc5; mouse.
PRO; PR:Q9R1X5; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022822; Expressed in 290 organ(s), highest expression level in skeletal muscle tissue.
ExpressionAtlas; Q9R1X5; baseline and differential.
Genevisible; Q9R1X5; MM.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0008514; F:organic anion transmembrane transporter activity; IEA:InterPro.
GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR030238; ABCC5.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24223:SF196; PTHR24223:SF196; 1.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Complete proteome; Direct protein sequencing;
Glycoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1436 Multidrug resistance-associated protein
5.
/FTId=PRO_0000093364.
TRANSMEM 179 199 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 219 239 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 296 316 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 317 337 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 400 420 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 426 446 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 608 628 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 847 867 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 916 936 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 996 1016 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 1017 1037 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 1101 1121 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 1126 1146 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
DOMAIN 179 459 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 562 783 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 858 1154 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1192 1426 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 595 602 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1226 1233 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:O15440}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:O15440}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000250|UniProtKB:O15440}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 509 509 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 513 513 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 494 494 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 636 636 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 684 684 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 889 889 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 896 896 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1043 1043 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1328 1328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1416 1416 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 146 146 S -> C (in Ref. 1; BAA76609).
{ECO:0000305}.
CONFLICT 200 200 V -> M (in Ref. 1; BAA76609).
{ECO:0000305}.
CONFLICT 217 217 Y -> C (in Ref. 1; BAA76609).
{ECO:0000305}.
CONFLICT 230 230 V -> I (in Ref. 1; BAA76609).
{ECO:0000305}.
CONFLICT 347 347 C -> R (in Ref. 1; BAA76609).
{ECO:0000305}.
CONFLICT 1098 1098 A -> P (in Ref. 1; BAA76609).
{ECO:0000305}.
CONFLICT 1103 1103 L -> I (in Ref. 1; BAA76609).
{ECO:0000305}.
CONFLICT 1111 1111 T -> S (in Ref. 1; BAA76609).
{ECO:0000305}.
CONFLICT 1118 1124 LMHGQIP -> SGMARSL (in Ref. 1; BAA76609).
{ECO:0000305}.
CONFLICT 1139 1139 T -> I (in Ref. 1; BAA76609).
{ECO:0000305}.
SEQUENCE 1436 AA; 161125 MW; 6B40BA516D8BE87D CRC64;
MKDIDMGKEY IIPSPGYRSD RDRSAVPGQH RDPEEPRFRR TRSLECQDAL ETAARVEGLS
LDISVHSHLQ ILDEEHSKGK YHHGLSVLKP FRTTTKHQHP VDNAGLFSYM TFSWLSPLAR
VVHKKGELLM EDVWPLSKYE SSDVNSRRLE RLWQEELNEV GPDAASLRRV VWIFCRTRLI
LSIVCLMITQ LAGFSGPAFV VKHLLEYTQA TESNLQYSLL LVLGLLLTEV VRSWSLALTW
ALNYRTGVRL RGAILTMAFK KILKLKNIKE KSLGELINIC SNDGQRMFEA AAVGSLLAGG
PVVAILGMIY NVIILGPTGF LGSAVFILFY PAMMFVSRLT AYFRRKCVAA TDDRVQKMNE
VLTYIKFIKM YAWVKAFSQC VQKIREEERR ILEKAGYFQS ITVGVAPIVV VIASVVTFSV
HMTLGFHLTA AQAFTVVTVF NSMTFALKVT PFSVKSLSEA SVAVDRFKSL FLMEEVHMIK
NKPASPHIKI EMKNATLAWD SSHSSIQNSP KLTPKMKKDK RATRGKKEKS RQLQHTEHQA
VLAEQKGHLL LDSDERPSPE EEEGKQIHTG SLRLQRTLYN IDLEIEEGKL VGICGSVGSG
KTSLVSAILG QMTLLEGSIA VSGTFAYVAQ QAWILNATLR DNILFGKEFD EERYNSVLNS
CCLRPDLAIL PNSDLTEIGE RGANLSGGQR QRISLARALY SDRSIYILDD PLSALDAHVG
NHIFNSAIRK RLKSKTVLFV THQLQYLVDC DEVIFMKEGC ITERGTHEEL MNLNGDYATI
FNNLLLGETP PVEINSKKEA TGSQKSQDKG PKPGSVKKEK AVKSEEGQLV QVEEKGQGSV
PWSVYWVYIQ AAGGPLAFLV IMVLFMLNVG STAFSTWWLS YWIKQGSGNS TVYQGNRSFV
SDSMKDNPFM QYYASIYALS MAVMLILKAI RGVVFVKGTL RASSRLHDEL FRRILRSPMK
FFDTTPTGRI LNRFSKDMDE VDVRLPFQAE MFIQNVILVF FCVGMIAGVF PWFLVAVGPL
LILFSLLHIV SRVLIRELKR LDNITQSPFL SHITSSIQGL ATIHAYNKRQ EFLHRYQELL
DDNQAPFFLF TCAMRWLAVR LDLISIALIT TTGLMIVLMH GQIPSAYAGL AISYAVQLTG
LFQFTVRLAS ETEARFTSVE RINHYIKTLS LEAPARIKNK APPHDWPQEG EVTFENAEMR
YRENLPLVLK KVSFTIKPKE KIGIVGRTGS GKSSLGMALF RLVELSGGCI KIDGIRISDI
GLADLRSKLA IIPQEPVLFS GTVRSNLDPF NQYTEDQIWD ALERTHMKEC IAQLPLKLES
EVMENGDNFS VGERQLLCIA RALLRHCKIL ILDEATAAMD TETDLLIQET IREAFADCTM
LTIAHRLHTV LGSDRIMVLA QGQVVEFDTP SVLLSNDSSR FYAMFAAAEN KVAVKG


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