ABCB9_MOUSE
ID ABCB9_MOUSE Reviewed; 762 AA.
AC Q9JJ59; Q8CHA1; Q9D212; Q9JIN1;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=ABC-type oligopeptide transporter ABCB9 {ECO:0000250|UniProtKB:Q9NP78};
DE EC=7.4.2.6 {ECO:0000250|UniProtKB:Q9NP78};
DE AltName: Full=ATP-binding cassette sub-family B member 9;
DE AltName: Full=ATP-binding cassette transporter 9;
DE Short=ABC transporter 9 protein;
DE Short=mABCB9;
DE AltName: Full=TAP-like protein {ECO:0000303|PubMed:11011155};
DE Short=TAPL {ECO:0000303|PubMed:11011155};
GN Name=Abcb9 {ECO:0000312|MGI:MGI:1861729};
GN Synonyms=Kiaa1520 {ECO:0000303|PubMed:12465718};
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] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11011155; DOI=10.1093/oxfordjournals.jbchem.a022805;
RA Kobayashi A., Kasano M., Maeda T., Hori S., Motojima K., Suzuki M.,
RA Fujiwara T., Takahashi E., Yabe T., Tanaka K., Kasahara M., Yamaguchi Y.,
RA Maeda M.;
RT "A half-type ABC transporter TAPL is highly conserved between rodent and
RT man, and the human gene is not responsive to interferon-gamma in contrast
RT to TAP1 and TAP2.";
RL J. Biochem. 128:711-718(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10748049; DOI=10.1074/jbc.m001819200;
RA Zhang F., Zhang W., Liu L., Fisher C.L., Hui D., Childs S.,
RA Dorovini-Zis K., Ling V.;
RT "Characterization of ABCB9, an ATP binding cassette protein associated with
RT lysosomes.";
RL J. Biol. Chem. 275:23287-23294(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 414-762 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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).
CC -!- FUNCTION: ATP-dependent low-affinity peptide transporter which
CC translocates a broad spectrum of peptides from the cytosol to the
CC lysosomal lumen for degradation. Displays a broad peptide length
CC specificity from 6-mer up to at least 59-mer peptides with an optimum
CC of 23-mers. Binds and transports smaller and larger peptides with the
CC same affinity. Favors positively charged, aromatic or hydrophobic
CC residues in the N- and C-terminal positions whereas negatively charged
CC residues as well as asparagine and methionine are not favored.
CC {ECO:0000250|UniProtKB:Q9NP78}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a [oligopeptide](in) + ATP + H2O = a [oligopeptide](out) + ADP
CC + H(+) + phosphate; Xref=Rhea:RHEA:14429, Rhea:RHEA-COMP:10531,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83228, ChEBI:CHEBI:456216; EC=7.4.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q9NP78};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14430;
CC Evidence={ECO:0000250|UniProtKB:Q9NP78};
CC -!- SUBUNIT: Homodimer. Interacts (via TMD0 region) with LAMP1; this
CC interaction strongly stabilizes ABCB9 and protects ABCB9 against
CC lysosomal degradation. Interacts (via TMD0 region) with LAMP2 (isoform
CC LAMP-2B). Interacts (via TMD0) with YIF1B; this interaction allows (but
CC is not essential) the ER-to-Golgi trafficking and strongly depends on a
CC salt bridge within TMD0. {ECO:0000250|UniProtKB:Q9NP78}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9NP78};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NP78,
CC ECO:0000255|PROSITE-ProRule:PRU00441}. Note=May be located in membrane
CC rafts. Takes an intracellular route from the endoplasmic reticulum
CC (ER), via Golgi and early endosomes to late endosomal and lysosomal
CC compartments. {ECO:0000250|UniProtKB:Q9NP78}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JJ59-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JJ59-2; Sequence=VSP_000032, VSP_000033;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, particularly in the
CC Sertoli cells of the seminiferous tubules, and at moderate levels in
CC brain and spinal cord. {ECO:0000269|PubMed:10748049}.
CC -!- DOMAIN: Divided into an N-terminal domain (TMD0) comprising four
CC transmembrane helices and the following core domain (coreABCB9). TMD0
CC is required for lysosomal localization and LAMP1, LAMP2 and YIF1B
CC interaction. The core domain is required for homodimerization and
CC peptide transport activity. {ECO:0000250|UniProtKB:Q9NP78}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC MHC peptide exporter (TC 3.A.1.209) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41480.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB045382; BAA97990.2; -; mRNA.
DR EMBL; AF216495; AAF89994.1; -; mRNA.
DR EMBL; AB093298; BAC41480.1; ALT_INIT; mRNA.
DR EMBL; AK020749; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK044140; BAC31796.1; -; mRNA.
DR EMBL; BC053014; AAH53014.1; -; mRNA.
DR CCDS; CCDS19671.1; -. [Q9JJ59-1]
DR RefSeq; NP_063928.2; NM_019875.2. [Q9JJ59-1]
DR AlphaFoldDB; Q9JJ59; -.
DR SMR; Q9JJ59; -.
DR STRING; 10090.ENSMUSP00000031354; -.
DR iPTMnet; Q9JJ59; -.
DR PhosphoSitePlus; Q9JJ59; -.
DR EPD; Q9JJ59; -.
DR MaxQB; Q9JJ59; -.
DR PaxDb; Q9JJ59; -.
DR PeptideAtlas; Q9JJ59; -.
DR PRIDE; Q9JJ59; -.
DR ProteomicsDB; 285902; -. [Q9JJ59-1]
DR ProteomicsDB; 285903; -. [Q9JJ59-2]
DR Antibodypedia; 31719; 249 antibodies from 30 providers.
DR DNASU; 56325; -.
DR Ensembl; ENSMUST00000031354; ENSMUSP00000031354; ENSMUSG00000029408. [Q9JJ59-1]
DR GeneID; 56325; -.
DR KEGG; mmu:56325; -.
DR UCSC; uc008zou.1; mouse. [Q9JJ59-1]
DR CTD; 23457; -.
DR MGI; MGI:1861729; Abcb9.
DR VEuPathDB; HostDB:ENSMUSG00000029408; -.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000155431; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; Q9JJ59; -.
DR OMA; RVMHDLR; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; Q9JJ59; -.
DR TreeFam; TF105197; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 56325; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Abcb9; mouse.
DR PRO; PR:Q9JJ59; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JJ59; protein.
DR Bgee; ENSMUSG00000029408; Expressed in choroid plexus of fourth ventricle and 163 other tissues.
DR ExpressionAtlas; Q9JJ59; baseline and differential.
DR Genevisible; Q9JJ59; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0042824; C:MHC class I peptide loading complex; IBA:GO_Central.
DR GO; GO:0015421; F:ABC-type oligopeptide transporter activity; ISS:UniProtKB.
DR GO; GO:0015433; F:ABC-type peptide antigen transporter activity; IBA:GO_Central.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0046978; F:TAP1 binding; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; ISO:MGI.
DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IBA:GO_Central.
DR GO; GO:0006518; P:peptide metabolic process; ISS:UniProtKB.
DR GO; GO:0015833; P:peptide transport; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR030254; ABCB9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR PANTHER; PTHR24221:SF242; PTHR24221:SF242; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Lysosome; Membrane; Nucleotide-binding;
KW Peptide transport; Protein transport; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..762
FT /note="ABC-type oligopeptide transporter ABCB9"
FT /id="PRO_0000000253"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 184..467
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 500..736
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 535..542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT SITE 17
FT /note="Intramolecular salt bridge with Arg-57. Essential
FT for the release from the ER"
FT /evidence="ECO:0000250|UniProtKB:Q9NP78"
FT SITE 45
FT /note="Important for the second trafficking step from the
FT Golgi to the endosomal and lysosomal compartments"
FT /evidence="ECO:0000250|UniProtKB:Q9NP78"
FT SITE 49
FT /note="Important for the second trafficking step from the
FT Golgi to the endosomal and lysosomal compartments"
FT /evidence="ECO:0000250|UniProtKB:Q9NP78"
FT SITE 57
FT /note="Intramolecular salt bridge with Asp-17. Essential
FT for the release from the ER"
FT /evidence="ECO:0000250|UniProtKB:Q9NP78"
FT VAR_SEQ 631..636
FT /note="ETGEKG -> GTRRRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_000032"
FT VAR_SEQ 637..762
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_000033"
FT CONFLICT 67
FT /note="G -> R (in Ref. 2; AAF89994)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="P -> A (in Ref. 4; AK020749)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="S -> N (in Ref. 4; AK020749)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="N -> S (in Ref. 2; AAF89994)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="F -> L (in Ref. 4; AK020749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 762 AA; 83963 MW; A03C41760974DC9F CRC64;
MRLWKAVVVT LAFVSTDVGV TTAIYAFSHL DRSLLEDIRH FNIFDSVLDL WAACLYRSCL
LLGATIGVAK NSALGPRRLR ASWLVITLVC LFVGIYAMAK LLLFSEVRRP IRDPWFWALF
VWTYISLAAS FLLWGLLATV RPDAEALEPG NEGFHGEGGA PAEQASGATL QKLLSYTKPD
VAFLVAASFF LIVAALGETF LPYYTGRAID SIVIQKSMDQ FTTAVVVVCL LAIGSSLAAG
IRGGIFTLVF ARLNIRLRNC LFRSLVSQET SFFDENRTGD LISRLTSDTT MVSDLVSQNI
NIFLRNTVKV TGVVVFMFSL SWQLSLVTFM GFPIIMMVSN IYGKYYKRLS KEVQSALARA
STTAEETISA MKTVRSFANE EEEAEVFLRK LQQVYKLNRK EAAAYMSYVW GSGLTLLVVQ
VSILYYGGHL VISGQMSSGN LIAFIIYEFV LGDCMESVGS VYSGLMQGVG AAEKVFEFID
RQPTMVHDGS LAPDHLEGRV DFENVTFTYR TRPHTQVLQN VSFSLSPGKV TALVGPSGSG
KSSCVNILEN FYPLQGGRVL LDGKPIGAYD HKYLHRVISL VSQEPVLFAR SITDNISYGL
PTVPFEMVVE AAQKANAHGF IMELQDGYST ETGEKGAQLS GGQKQRVAMA RALVRNPPVL
ILDEATSALD AESEYLIQQA IHGNLQRHTV LIIAHRLSTV ERAHLIVVLD KGRVVQQGTH
QQLLAQGGLY AKLVQRQMLG LEHPLDYTAS HKEPPSNTEH KA
