ABCB9_RAT
ID ABCB9_RAT Reviewed; 762 AA.
AC Q9QYJ4; Q764Q5; Q764Q6;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
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 AltName: Full=TAP-like protein {ECO:0000303|PubMed:10471785};
DE Short=TAPL {ECO:0000303|PubMed:10471785};
GN Name=Abcb9 {ECO:0000312|RGD:620254};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Intestine, and Kidney;
RX PubMed=10471785; DOI=10.1016/s0014-5793(99)01042-x;
RA Yamaguchi Y., Kasano M., Terada T., Sato R., Maeda M.;
RT "An ABC transporter homologous to TAP proteins.";
RL FEBS Lett. 457:231-236(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=14709908; DOI=10.1248/bpb.27.100;
RA Yamaguchi Y., Iseoka H., Kobayashi A., Maeda M.;
RT "The carboxyl terminal sequence of rat transporter associated with antigen
RT processing (TAP)-like (ABCB9) is heterogeneous due to splicing of its
RT mRNA.";
RL Biol. Pharm. Bull. 27:100-104(2004).
RN [3]
RP SUBUNIT.
RX PubMed=18175933; DOI=10.1248/bpb.31.1;
RA Ohara T., Ohashi-Kobayashi A., Maeda M.;
RT "Biochemical characterization of transporter associated with antigen
RT processing (TAP)-like (ABCB9) expressed in insect cells.";
RL Biol. Pharm. Bull. 31:1-5(2008).
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 (PubMed:18175933). Interacts (via TMD0 region) with
CC LAMP1; this interaction strongly stabilizes ABCB9 and protects ABCB9
CC against lysosomal degradation. Interacts (via TMD0 region) with LAMP2
CC (isoform LAMP-2B). Interacts (via TMD0) with YIF1B; this interaction
CC allows (but is not essential) the ER-to-Golgi trafficking and strongly
CC depends on a salt bridge within TMD0 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NP78, ECO:0000269|PubMed:18175933}.
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=4;
CC Name=1; Synonyms=TAPLa, C-I;
CC IsoId=Q9QYJ4-1; Sequence=Displayed;
CC Name=2; Synonyms=TAPLb, C-II;
CC IsoId=Q9QYJ4-2; Sequence=VSP_000034;
CC Name=3; Synonyms=C-III;
CC IsoId=Q9QYJ4-3; Sequence=VSP_041888;
CC Name=4; Synonyms=C-IV;
CC IsoId=Q9QYJ4-4; Sequence=VSP_041887;
CC -!- TISSUE SPECIFICITY: Found in testis, particularly in the Sertoli cells
CC of the seminiferous tubules. Also expressed in kidney, brain, heart,
CC lung, spleen, thymus, intestine and testis. Higher expression detected
CC in brain and testis than in thymus and intestine.
CC {ECO:0000269|PubMed:10471785, ECO:0000269|PubMed:14709908}.
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}.
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DR EMBL; AB027520; BAA85306.1; -; mRNA.
DR EMBL; AB116264; BAD10852.1; -; mRNA.
DR EMBL; AB116265; BAD10853.1; -; mRNA.
DR RefSeq; NP_071574.1; NM_022238.1. [Q9QYJ4-1]
DR AlphaFoldDB; Q9QYJ4; -.
DR SMR; Q9QYJ4; -.
DR STRING; 10116.ENSRNOP00000051058; -.
DR PhosphoSitePlus; Q9QYJ4; -.
DR PaxDb; Q9QYJ4; -.
DR PRIDE; Q9QYJ4; -.
DR Ensembl; ENSRNOT00000045223; ENSRNOP00000051058; ENSRNOG00000001082. [Q9QYJ4-3]
DR Ensembl; ENSRNOT00000098844; ENSRNOP00000096168; ENSRNOG00000001082. [Q9QYJ4-1]
DR Ensembl; ENSRNOT00000114288; ENSRNOP00000083417; ENSRNOG00000001082. [Q9QYJ4-4]
DR GeneID; 63886; -.
DR KEGG; rno:63886; -.
DR UCSC; RGD:620254; rat. [Q9QYJ4-1]
DR CTD; 23457; -.
DR RGD; 620254; Abcb9.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000155431; -.
DR InParanoid; Q9QYJ4; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; Q9QYJ4; -.
DR TreeFam; TF105197; -.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR PRO; PR:Q9QYJ4; -.
DR Proteomes; UP000002494; Chromosome 12.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; TAS:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
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:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0046978; F:TAP1 binding; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; ISO:RGD.
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 1: Evidence at protein 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_0000000254"
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 677..762
FT /note="IQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGG
FT LYAKLVQRQMLGLEHPLDYTAGHKEPPSNTEHKA -> VALADLKYREIHPSPQD (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14709908"
FT /id="VSP_041888"
FT VAR_SEQ 677..762
FT /note="IQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGG
FT LYAKLVQRQMLGLEHPLDYTAGHKEPPSNTEHKA -> SEAQTPGLEHTPHPATTAWLE
FT ATLSPKPGCQG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14709908"
FT /id="VSP_041887"
FT VAR_SEQ 721..762
FT /note="QQLLAQGGLYAKLVQRQMLGLEHPLDYTAGHKEPPSNTEHKA -> LPLLST
FT PATLQRNLVCKMYSQIGGGDRGNAQGLALSWFKILGELGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10471785"
FT /id="VSP_000034"
SQ SEQUENCE 762 AA; 84033 MW; E39D3B42CFBD88EF CRC64;
MRLWKAVVVT LAFVSMDVGV 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
RQPTMVHDGR LAPDHLEGRV DFENVTFTYR TRPHTQVLQN VSFSLSPGKV TALVGPSGSG
KSSCVNILEN FYPLQGGRVL LDGEPIGAYD HKYLHRVISL VSQEPVLFAR SITDNISYGL
PTVPFEMVVE AAQKANAHGF IMELQDGYST ETGEKGAQLS GGQKQRVAMA RALVRNPPVL
ILDEATSALD AESEYLIQQA IHGNLQRHTV LIIAHRLSTV ERAHLIVVLD KGRVVQQGTH
QQLLAQGGLY AKLVQRQMLG LEHPLDYTAG HKEPPSNTEH KA
