ID A0A1U8D0V2_MESAU Unreviewed; 704 AA.
AC A0A1U8D0V2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ABC-type antigen peptide transporter {ECO:0000256|ARBA:ARBA00034522};
DE EC=7.4.2.14 {ECO:0000256|ARBA:ARBA00034522};
GN Name=Tap2 {ECO:0000313|RefSeq:XP_012981234.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012981234.1};
RN [1] {ECO:0000313|RefSeq:XP_012981234.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a peptide antigen(in) + ATP + H2O = a peptide antigen(out) +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:65972, Rhea:RHEA-COMP:16941,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:166823, ChEBI:CHEBI:456216;
CC EC=7.4.2.14; Evidence={ECO:0000256|ARBA:ARBA00034404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65973;
CC Evidence={ECO:0000256|ARBA:ARBA00034404};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC MHC peptide exporter (TC 3.A.1.209) subfamily.
CC {ECO:0000256|ARBA:ARBA00006493}.
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DR RefSeq; XP_012981234.1; XM_013125780.2.
DR AlphaFoldDB; A0A1U8D0V2; -.
DR STRING; 10036.ENSMAUP00000015703; -.
DR GeneID; 101835124; -.
DR CTD; 6891; -.
DR eggNOG; KOG0058; Eukaryota.
DR OrthoDB; 5487044at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0042825; C:TAP complex; IEA:Ensembl.
DR GO; GO:0015433; F:ABC-type peptide antigen transporter activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0023029; F:MHC class Ib protein binding; IEA:Ensembl.
DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl.
DR GO; GO:0046978; F:TAP1 binding; IEA:Ensembl.
DR GO; GO:0002485; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent; IEA:Ensembl.
DR GO; GO:0002489; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent; IEA:Ensembl.
DR GO; GO:0002481; P:antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent; IEA:Ensembl.
DR GO; GO:0046967; P:cytosol to endoplasmic reticulum transport; IEA:Ensembl.
DR GO; GO:0046968; P:peptide antigen transport; IEA:Ensembl.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEA:Ensembl.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl.
DR CDD; cd18590; ABC_6TM_TAP2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR013305; ABC_Tap-like.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005293; Tap2/ABCB3.
DR InterPro; IPR039421; Type_1_exporter.
DR NCBIfam; TIGR00958; 3a01208; 1.
DR PANTHER; PTHR24221:SF237; ANTIGEN PEPTIDE TRANSPORTER 2; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR PIRSF; PIRSF002773; ABC_prm/ATPase_B; 1.
DR PRINTS; PR01897; TAP2PROTEIN.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunity {ECO:0000256|ARBA:ARBA00023130};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..704
FT /note="ABC-type antigen peptide transporter"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010586856"
FT TRANSMEM 49..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 154..435
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 468..702
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 704 AA; 77744 MW; 9FAF94BCE247247F CRC64;
MALAHLRPWA SLLLVDMALL ALLQGSPGNL LPLGLPGLWL EGTLRLGGLW GLLAVGGLLG
RVGTFPPLLC LATPLFFSLR ALVGGTMSSP AVRVASASWV WLLADYKAAA LGWAVWAVLS
PPGAREKEAG QEKNKSLMWQ LLRLSRPDLP FLMVAFFFLA WAVLGETLIP HYSGRVIDIL
GSDFDPDAFA SAIFFMCLFS VGSSLSAGCR GGSFLFTMSR INLRIRERLF SSLLRQDLGF
FQENKTGELN SRLSSDTSKM SRWLPYNANI LLRSLVKVIG LYCFMLQVSP RLTFLSLLDL
PLTIAAEKVY NPRHQAVLTE IQDATAKAGQ VVREAVGGLQ TVRSFGAEEQ EVSRYKEALE
RCRQLWWRRD LERALYLAIR RVMALGMQVL ILNCGVQQIL AGEVTRGGLL SFLLYQEEVG
DYVRNLVYMY GDMLSNVGAA EKVFCYIDRK PNLPQPGTLA PSRLEGRVEF QDVTFSYPSR
PEKPVLKGLT FTLHPGKVTA LVGPNGSGKS TVAALLQNLY QPTGGQLLLD GQPLVQYDHH
YLHRQVVLVG QEPVLFSGSV KDNIAYGLKD CEDAQVMAAV RAACADDFIG EMPDGIHTEI
GEKGSQLAVG QKQRLAIARA LVRNPRVLIL DEATSALDSQ CEQALQAWRS KGDRTVLVIA
HRLHTVQNVD QVLVLKQGQL VEHSQLREDQ DVYAHLVQQQ RLEE
//
