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 01-MAY-2013, entry version 110.
DE RecName: 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;
DE Short=TAPL;
GN Name=Abcb9; Synonyms=Kiaa1520;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11011155;
RA Kobayashi A., Kasano M., Maeda T., Hori S., Motojima K., Suzuki M.,
RA Fujiwara T., Takahashi E., Yabe T., Tanaka K., Kasahara M.,
RA Yamaguchi Y., Maeda M.;
RT "A half-type ABC transporter TAPL is highly conserved between rodent
RT and man, and the human gene is not responsive to interferon-gamma in
RT contrast 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
RT with 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.,
RA Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT cDNAs identified by screening of terminal sequences of cDNA clones
RT randomly sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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/6; 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
RT project: 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. Displays a broad peptide length specificity from
CC 6-mer up to at least 59-mer peptides with an optimum of 23-mers.
CC Favors positively charged, aromatic or hydrophobic residues in the
CC N- and C-terminal positions whereas negatively charged residues as
CC well as asparagine and methionine are not favored (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane
CC protein (By similarity). Note=May be located in membrane rafts (By
CC similarity).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, particularly in
CC the Sertoli cells of the seminiferous tubules, and at moderate
CC levels in brain and spinal cord.
CC -!- DOMAIN: The N-terminal region comprising the first four
CC transmembrane domains is required for lysosomal localization but
CC not for homodimerization or peptide transport (By similarity).
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
CC family. MHC peptide exporter (TC 3.A.1.209) subfamily.
CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain.
CC -!- SIMILARITY: Contains 1 ABC transporter domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41480.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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 IPI; IPI00162932; -.
DR IPI; IPI00380188; -.
DR RefSeq; NP_063928.2; NM_019875.2.
DR UniGene; Mm.254839; -.
DR ProteinModelPortal; Q9JJ59; -.
DR SMR; Q9JJ59; 171-737.
DR PhosphoSite; Q9JJ59; -.
DR PaxDb; Q9JJ59; -.
DR PRIDE; Q9JJ59; -.
DR Ensembl; ENSMUST00000031354; ENSMUSP00000031354; ENSMUSG00000029408.
DR GeneID; 56325; -.
DR KEGG; mmu:56325; -.
DR UCSC; uc008zou.1; mouse.
DR CTD; 23457; -.
DR MGI; MGI:1861729; Abcb9.
DR eggNOG; COG1132; -.
DR GeneTree; ENSGT00550000074497; -.
DR HOVERGEN; HBG008358; -.
DR InParanoid; Q9JJ59; -.
DR KO; K05656; -.
DR OMA; ANGSHKA; -.
DR OrthoDB; EOG4VT5X2; -.
DR NextBio; 312302; -.
DR ArrayExpress; Q9JJ59; -.
DR Bgee; Q9JJ59; -.
DR Genevestigator; Q9JJ59; -.
DR GermOnline; ENSMUSG00000029408; Mus musculus.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:RefGenome.
DR GO; GO:0042825; C:TAP complex; IBA:RefGenome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; IBA:RefGenome.
DR GO; GO:0015421; F:oligopeptide-transporting ATPase activity; IBA:RefGenome.
DR GO; GO:0042605; F:peptide antigen binding; IBA:RefGenome.
DR GO; GO:0046978; F:TAP1 binding; IBA:RefGenome.
DR GO; GO:0046979; F:TAP2 binding; IBA:RefGenome.
DR GO; GO:0046980; F:tapasin binding; IBA:RefGenome.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:RefGenome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013305; ABC_B2.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR017871; ABC_transporter_CS.
DR InterPro; IPR017940; ABC_transporter_type1.
DR InterPro; IPR001140; ABC_transptr_TM_dom.
DR InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR PRINTS; PR01896; TAP1PROTEIN.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC_TM_1; 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; Complete proteome; Lysosome;
KW Membrane; Nucleotide-binding; Peptide transport; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 762 ATP-binding cassette sub-family B member
FT 9.
FT /FTId=PRO_0000000253.
FT TRANSMEM 7 27 Helical; (Potential).
FT TRANSMEM 47 67 Helical; (Potential).
FT TRANSMEM 84 104 Helical; (Potential).
FT TRANSMEM 116 136 Helical; (Potential).
FT TRANSMEM 181 201 Helical; (Potential).
FT TRANSMEM 221 241 Helical; (Potential).
FT TRANSMEM 315 335 Helical; (Potential).
FT TRANSMEM 412 432 Helical; (Potential).
FT DOMAIN 184 467 ABC transmembrane type-1.
FT DOMAIN 500 736 ABC transporter.
FT NP_BIND 535 542 ATP (Potential).
FT COMPBIAS 380 385 Poly-Glu.
FT VAR_SEQ 631 636 ETGEKG -> GTRRRL (in isoform 2).
FT /FTId=VSP_000032.
FT VAR_SEQ 637 762 Missing (in isoform 2).
FT /FTId=VSP_000033.
FT CONFLICT 67 67 G -> R (in Ref. 2; AAF89994).
FT CONFLICT 513 513 P -> A (in Ref. 4; AK020749).
FT CONFLICT 524 524 S -> N (in Ref. 4; AK020749).
FT CONFLICT 550 550 N -> S (in Ref. 2; AAF89994).
FT CONFLICT 605 605 F -> L (in Ref. 4; AK020749).
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
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