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ATP-binding cassette sub-family B member 9 (ATP-binding cassette transporter 9) (ABC transporter 9 protein) (hABCB9) (TAP-like protein) (TAPL)

 ABCB9_HUMAN             Reviewed;         766 AA.
Q9NP78; B4E2J0; Q5W9G7; Q769F3; Q769F4; Q96AB1; Q9P208;
02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 168.
RecName: Full=ATP-binding cassette sub-family B member 9;
AltName: Full=ATP-binding cassette transporter 9;
Short=ABC transporter 9 protein;
Short=hABCB9;
AltName: Full=TAP-like protein;
Short=TAPL;
Name=ABCB9; Synonyms=KIAA1520;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
TISSUE=Embryonic kidney;
PubMed=11011155; DOI=10.1093/oxfordjournals.jbchem.a022805;
Kobayashi A., Kasano M., Maeda T., Hori S., Motojima K., Suzuki M.,
Fujiwara T., Takahashi E., Yabe T., Tanaka K., Kasahara M.,
Yamaguchi Y., Maeda M.;
"A half-type ABC transporter TAPL is highly conserved between rodent
and man, and the human gene is not responsive to interferon-gamma in
contrast to TAP1 and TAP2.";
J. Biochem. 128:711-718(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Lymphoblast;
PubMed=10748049; DOI=10.1074/jbc.M001819200;
Zhang F., Zhang W., Liu L., Fisher C.L., Hui D., Childs S.,
Dorovini-Zis K., Ling V.;
"Characterization of ABCB9, an ATP binding cassette protein associated
with lysosomes.";
J. Biol. Chem. 275:23287-23294(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5).
TISSUE=Cervix carcinoma, and Embryonic kidney;
PubMed=13679046; DOI=10.1016/j.bbrc.2003.08.081;
Kobayashi A., Hori S., Suita N., Maeda M.;
"Gene organization of human transporter associated with antigen
processing-like (TAPL, ABCB9): analysis of alternative splicing
variants and promoter activity.";
Biochem. Biophys. Res. Commun. 309:815-822(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028;
Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.;
"Alternative splice variants encoding unstable protein domains exist
in the human brain.";
J. Mol. Biol. 343:1207-1220(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[6]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R.;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[10]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=15577206; DOI=10.1248/bpb.27.1916;
Kobayashi A., Maeda T., Maeda M.;
"Membrane localization of transporter associated with antigen
processing (TAP)-like (ABCB9) visualized in vivo with a fluorescence
protein-fusion technique.";
Biol. Pharm. Bull. 27:1916-1922(2004).
[11]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=15863492; DOI=10.1074/jbc.M503231200;
Wolters J.C., Abele R., Tampe R.;
"Selective and ATP-dependent translocation of peptides by the
homodimeric ATP binding cassette transporter TAP-like (ABCB9).";
J. Biol. Chem. 280:23631-23636(2005).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17977821; DOI=10.1074/jbc.M708139200;
Demirel O., Waibler Z., Kalinke U., Grunebach F., Appel S.,
Brossart P., Hasilik A., Tampe R., Abele R.;
"Identification of a lysosomal peptide transport system induced during
dendritic cell development.";
J. Biol. Chem. 282:37836-37843(2007).
[13]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Placenta;
PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
"Integral and associated lysosomal membrane proteins.";
Traffic 8:1676-1686(2007).
[14]
SUBCELLULAR LOCATION.
PubMed=18952056; DOI=10.1016/j.bbrc.2008.10.078;
Kamakura A., Fujimoto Y., Motohashi Y., Ohashi K.,
Ohashi-Kobayashi A., Maeda M.;
"Functional dissection of transmembrane domains of human TAP-like
(ABCB9).";
Biochem. Biophys. Res. Commun. 377:847-851(2008).
[15]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=18175933; DOI=10.1248/bpb.31.1;
Ohara T., Ohashi-Kobayashi A., Maeda M.;
"Biochemical characterization of transporter associated with antigen
processing (TAP)-like (ABCB9) expressed in insect cells.";
Biol. Pharm. Bull. 31:1-5(2008).
[16]
FUNCTION.
PubMed=18434309; DOI=10.1074/jbc.M801794200;
Zhao C., Haase W., Tampe R., Abele R.;
"Peptide specificity and lipid activation of the lysosomal transport
complex ABCB9 (TAPL).";
J. Biol. Chem. 283:17083-17091(2008).
[17]
SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 136-LYS-LYS-137.
PubMed=20377823; DOI=10.1111/j.1600-0854.2009.01021.x;
Demirel O., Bangert I., Tampe R., Abele R.;
"Tuning the cellular trafficking of the lysosomal peptide transporter
TAPL by its N-terminal domain.";
Traffic 11:383-393(2010).
[18]
SUBCELLULAR LOCATION.
PubMed=21212514; DOI=10.1248/bpb.34.36;
Fujimoto Y., Kamakura A., Motohashi Y., Ohashi-Kobayashi A., Maeda M.;
"Transporter associated with antigen processing-like (ABCB9) stably
expressed in Chinese hamster ovary-K1 cells is sorted to the
microdomains of lysosomal membranes.";
Biol. Pharm. Bull. 34:36-40(2011).
[19]
VARIANT MET-121.
PubMed=11829140; DOI=10.1007/s10038-002-8653-6;
Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S.,
Higuchi S., Nakamura Y.;
"Three hundred twenty-six genetic variations in genes encoding nine
members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the
Japanese population.";
J. Hum. Genet. 47:38-50(2002).
-!- FUNCTION: ATP-dependent low-affinity peptide transporter which
translocates a broad spectrum of peptides from the cytosol to the
lysosomal lumen. Displays a broad peptide length specificity from
6-mer up to at least 59-mer peptides with an optimum of 23-mers.
Favors positively charged, aromatic or hydrophobic residues in the
N- and C-terminal positions whereas negatively charged residues as
well as asparagine and methionine are not favored.
{ECO:0000269|PubMed:15863492, ECO:0000269|PubMed:17977821,
ECO:0000269|PubMed:18434309}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.8 uM for peptide RRYQNSTCL {ECO:0000269|PubMed:15863492};
pH dependence:
Optimum pH is 7.0. {ECO:0000269|PubMed:15863492};
Temperature dependence:
Optimum temperature is 37 degrees Celsius.
{ECO:0000269|PubMed:15863492};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15863492}.
-!- SUBCELLULAR LOCATION: Lysosome membrane
{ECO:0000269|PubMed:10748049, ECO:0000269|PubMed:15577206,
ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:17977821,
ECO:0000269|PubMed:18175933, ECO:0000269|PubMed:18952056,
ECO:0000269|PubMed:20377823, ECO:0000269|PubMed:21212514}; Multi-
pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
ECO:0000269|PubMed:10748049, ECO:0000269|PubMed:15577206,
ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:17977821,
ECO:0000269|PubMed:18175933, ECO:0000269|PubMed:18952056,
ECO:0000269|PubMed:20377823, ECO:0000269|PubMed:21212514}.
Note=May be located in membrane rafts.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=12A, c1-l;
IsoId=Q9NP78-1; Sequence=Displayed;
Name=2; Synonyms=c1-s;
IsoId=Q9NP78-2; Sequence=VSP_000027;
Name=3;
IsoId=Q9NP78-3; Sequence=VSP_000029, VSP_000030;
Note=No experimental confirmation available.;
Name=4; Synonyms=12B;
IsoId=Q9NP78-5; Sequence=VSP_041884, VSP_041886;
Name=5; Synonyms=12C;
IsoId=Q9NP78-6; Sequence=VSP_041885;
Name=6;
IsoId=Q9NP78-7; Sequence=VSP_044884;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in testis, and at moderate
levels in brain, spinal cord, and thyroid. Not expressed in
monocytes but strongly expressed during differentiation of
monocytes to dendritic cells and macrophages.
{ECO:0000269|PubMed:10748049, ECO:0000269|PubMed:17977821}.
-!- INDUCTION: Not induced by interferon-gamma.
{ECO:0000269|PubMed:11011155}.
-!- DOMAIN: The N-terminal region comprising the first four
transmembrane domains is required for lysosomal localization but
not for homodimerization or peptide transport.
{ECO:0000269|PubMed:15577206, ECO:0000269|PubMed:18175933,
ECO:0000269|PubMed:20377823}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. MHC peptide exporter (TC 3.A.1.209) subfamily.
{ECO:0000305}.
-!- CAUTION: Has also been detected in the endoplasmic reticulum but
appears to be a lysosomal protein in vivo.
{ECO:0000305|PubMed:11011155}.
-!- SEQUENCE CAUTION:
Sequence=BAA96044.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAD66830.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q9NP78";
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EMBL; AB045381; BAA97989.2; -; mRNA.
EMBL; AF216494; AAF89993.1; -; mRNA.
EMBL; AB112582; BAC98409.1; -; mRNA.
EMBL; AB112583; BAC98410.1; -; mRNA.
EMBL; AB177852; BAD66830.1; ALT_INIT; mRNA.
EMBL; AB040953; BAA96044.2; ALT_INIT; mRNA.
EMBL; AK304295; BAG65152.1; -; mRNA.
EMBL; AC026362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC027290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017348; AAH17348.1; -; mRNA.
CCDS; CCDS58286.1; -. [Q9NP78-7]
CCDS; CCDS58287.1; -. [Q9NP78-6]
CCDS; CCDS58288.1; -. [Q9NP78-5]
CCDS; CCDS9241.1; -. [Q9NP78-1]
RefSeq; NP_001229942.1; NM_001243013.1. [Q9NP78-7]
RefSeq; NP_001229943.1; NM_001243014.1. [Q9NP78-6]
RefSeq; NP_062570.1; NM_019624.3. [Q9NP78-2]
RefSeq; NP_062571.1; NM_019625.3. [Q9NP78-1]
RefSeq; NP_982269.2; NM_203444.3. [Q9NP78-5]
RefSeq; XP_011536397.1; XM_011538095.2. [Q9NP78-1]
RefSeq; XP_011536398.1; XM_011538096.2. [Q9NP78-1]
RefSeq; XP_016874592.1; XM_017019103.1. [Q9NP78-1]
UniGene; Hs.511951; -.
ProteinModelPortal; Q9NP78; -.
SMR; Q9NP78; -.
BioGrid; 117021; 14.
STRING; 9606.ENSP00000280560; -.
ChEMBL; CHEMBL1293189; -.
TCDB; 3.A.1.209.2; the atp-binding cassette (abc) superfamily.
iPTMnet; Q9NP78; -.
PhosphoSitePlus; Q9NP78; -.
BioMuta; ABCB9; -.
DMDM; 22095458; -.
PaxDb; Q9NP78; -.
PeptideAtlas; Q9NP78; -.
PRIDE; Q9NP78; -.
Ensembl; ENST00000280560; ENSP00000280560; ENSG00000150967. [Q9NP78-1]
Ensembl; ENST00000344275; ENSP00000456813; ENSG00000150967. [Q9NP78-6]
Ensembl; ENST00000346530; ENSP00000280559; ENSG00000150967. [Q9NP78-2]
Ensembl; ENST00000392439; ENSP00000376234; ENSG00000150967. [Q9NP78-1]
Ensembl; ENST00000442833; ENSP00000456375; ENSG00000150967. [Q9NP78-5]
Ensembl; ENST00000540285; ENSP00000441734; ENSG00000150967. [Q9NP78-7]
Ensembl; ENST00000542678; ENSP00000440288; ENSG00000150967. [Q9NP78-1]
GeneID; 23457; -.
KEGG; hsa:23457; -.
UCSC; uc001udm.5; human. [Q9NP78-1]
CTD; 23457; -.
DisGeNET; 23457; -.
EuPathDB; HostDB:ENSG00000150967.17; -.
GeneCards; ABCB9; -.
HGNC; HGNC:50; ABCB9.
HPA; CAB033052; -.
HPA; HPA035113; -.
HPA; HPA035114; -.
MIM; 605453; gene.
neXtProt; NX_Q9NP78; -.
OpenTargets; ENSG00000150967; -.
PharmGKB; PA24391; -.
eggNOG; KOG0058; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00550000074497; -.
HOVERGEN; HBG008358; -.
InParanoid; Q9NP78; -.
KO; K05656; -.
PhylomeDB; Q9NP78; -.
TreeFam; TF105197; -.
BRENDA; 3.6.3.43; 2681.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
SABIO-RK; Q9NP78; -.
GeneWiki; ABCB9; -.
GenomeRNAi; 23457; -.
PRO; PR:Q9NP78; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000150967; -.
CleanEx; HS_ABCB9; -.
ExpressionAtlas; Q9NP78; baseline and differential.
Genevisible; Q9NP78; HS.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0015421; F:oligopeptide-transporting ATPase activity; TAS:Reactome.
GO; GO:0015440; F:peptide-transporting ATPase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015833; P:peptide transport; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
Gene3D; 1.20.1560.10; -; 1.
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; IPR030254; ABCB9.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24221:SF242; PTHR24221:SF242; 1.
Pfam; PF00664; ABC_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF90123; SSF90123; 1.
PROSITE; PS50929; ABC_TM1F; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Lysosome;
Membrane; Nucleotide-binding; Peptide transport; Polymorphism;
Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 766 ATP-binding cassette sub-family B member
9.
/FTId=PRO_0000000252.
TRANSMEM 7 27 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 47 67 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 84 104 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 116 136 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 185 205 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 225 245 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 319 339 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 416 436 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
DOMAIN 188 471 ABC transmembrane type-1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 504 740 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 539 546 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
COMPBIAS 384 389 Poly-Glu.
VAR_SEQ 418 460 Missing (in isoform 2).
{ECO:0000303|PubMed:10748049}.
/FTId=VSP_000027.
VAR_SEQ 461 523 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_044884.
VAR_SEQ 582 596 ISLVSQEPVLFARSI -> VCARAWATLLRPFCI (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_000029.
VAR_SEQ 597 766 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_000030.
VAR_SEQ 681 683 IQQ -> CAG (in isoform 4).
{ECO:0000303|PubMed:13679046}.
/FTId=VSP_041884.
VAR_SEQ 682 766 Missing (in isoform 5).
{ECO:0000303|PubMed:13679046}.
/FTId=VSP_041885.
VAR_SEQ 684 766 Missing (in isoform 4).
{ECO:0000303|PubMed:13679046}.
/FTId=VSP_041886.
VARIANT 121 121 V -> M (in dbSNP:rs3803002).
{ECO:0000269|PubMed:11829140}.
/FTId=VAR_013701.
MUTAGEN 136 137 LL->AA: No effect on lysosomal
localization.
{ECO:0000269|PubMed:20377823}.
SEQUENCE 766 AA; 84475 MW; C83FA62C929EC792 CRC64;
MRLWKAVVVT LAFMSVDICV TTAIYVFSHL DRSLLEDIRH FNIFDSVLDL WAACLYRSCL
LLGATIGVAK NSALGPRRLR ASWLVITLVC LFVGIYAMVK LLLFSEVRRP IRDPWFWALF
VWTYISLGAS FLLWWLLSTV RPGTQALEPG AATEAEGFPG SGRPPPEQAS GATLQKLLSY
TKPDVAFLVA ASFFLIVAAL GETFLPYYTG RAIDGIVIQK SMDQFSTAVV IVCLLAIGSS
FAAGIRGGIF TLIFARLNIR LRNCLFRSLV SQETSFFDEN RTGDLISRLT SDTTMVSDLV
SQNINVFLRN TVKVTGVVVF MFSLSWQLSL VTFMGFPIIM MVSNIYGKYY KRLSKEVQNA
LARASNTAEE TISAMKTVRS FANEEEEAEV YLRKLQQVYK LNRKEAAAYM YYVWGSGLTL
LVVQVSILYY GGHLVISGQM TSGNLIAFII YEFVLGDCME SVGSVYSGLM QGVGAAEKVF
EFIDRQPTMV HDGSLAPDHL EGRVDFENVT FTYRTRPHTQ VLQNVSFSLS PGKVTALVGP
SGSGKSSCVN ILENFYPLEG GRVLLDGKPI SAYDHKYLHR VISLVSQEPV LFARSITDNI
SYGLPTVPFE MVVEAAQKAN AHGFIMELQD GYSTETGEKG AQLSGGQKQR VAMARALVRN
PPVLILDEAT SALDAESEYL IQQAIHGNLQ KHTVLIIAHR LSTVEHAHLI VVLDKGRVVQ
QGTHQQLLAQ GGLYAKLVQR QMLGLQPAAD FTAGHNEPVA NGSHKA


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