ID A0A452RF49_URSAM Unreviewed; 703 AA. AC A0A452RF49; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 13-SEP-2023, entry version 23. 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|Ensembl:ENSUAMP00000017400.1}; OS Ursus americanus (American black bear) (Euarctos americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus. OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000017400.1, ECO:0000313|Proteomes:UP000291022}; RN [1] {ECO:0000313|Proteomes:UP000291022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L., RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.; RT "De novo assembly and RNA-Seq shows season-dependent expression and editing RT in black bear kidneys."; RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSUAMP00000017400.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A452RF49; -. DR STRING; 9643.ENSUAMP00000017400; -. DR Ensembl; ENSUAMT00000019470.1; ENSUAMP00000017400.1; ENSUAMG00000013187.1. DR GeneTree; ENSGT00940000160499; -. DR Proteomes; UP000291022; Unassembled WGS sequence. 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; 2. 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; PTHR43394:SF8; ATP BINDING CASSETTE SUBFAMILY B MEMBER 9; 1. DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 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 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:UP000291022}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 52..77 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 98..119 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 149..172 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 184..205 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 153..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 703 AA; 77752 MW; E767AD5D9FA6CBC1 CRC64; MLFPDLRPWA FLLLADSALL WLLQGTLGAL LPPGLPGLWL EGTLRLGGLW WLLKVGGLLG LVGTLLAPLC LGTPLFLSLR ALVPGALSAP PVRVASAPWS WLLLGYAAVW LGWAMWALLS SPGAQETKQG QENNTDLMWR LLKLSWPDLP YLLAAFFFLI VAVLGETVIP YYSGHVIDIL RGDFDPDAFT SAILFMCLFS IGSSLCAGCR GSCFTFTMSR INVRVRQLLF SSLLRQDLSF FQDTKTGELN SRLNSDTKLM SCWLAFNANV LLRSVVKVVG LYSFMLSLSP RLALLSLLKV PLEITAQKLY DVRHQAVLRE IQNAVAKAGQ VVREAVGGLQ TVRSFGAEEH ELGLYKEALE QCRQLWWRRD LERALYVLFQ RMLHLGMQVL MLNCGLQQIL AGDLTQGGLL SFLLYQEDMG HYVQTLVYMC GDMLSNVGAA EKVFQYLDRK PNLPPPGTLA PPTLRGLVEF QDVSFAYPNR PDQPVLKGLT FTLRPGQMTA LVGPNGSGKS TVAALLQNLY QPTGGRLLLD GQPLSQYEHR YLHRQVTSVG QEPVLFSGSV RDNIAYGLKS CSDEQVMAAA QAANADGFIQ DLEHGLYTDV GERGNQLAVG QKQCLAIARA LVRDPRVLIL DEATSALDVQ CEQALQDWKS RGDRTVLVIA HRLQTVQSAD QILVLRQGEL LERAQLMEGQ DLYSRLAQQL LED //