ID H2R2Q4_PANTR Unreviewed; 808 AA.
AC H2R2Q4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=ABC-type antigen peptide transporter {ECO:0000256|ARBA:ARBA00034522};
DE EC=7.4.2.14 {ECO:0000256|ARBA:ARBA00034522};
GN Name=TAP1 {ECO:0000313|Ensembl:ENSPTRP00000044308.3,
GN ECO:0000313|VGNC:VGNC:12708};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000044308.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000044308.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000044308.3}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AACZ04022817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001166911.2; XM_001166911.5.
DR AlphaFoldDB; H2R2Q4; -.
DR PaxDb; 9598-ENSPTRP00000044308; -.
DR Ensembl; ENSPTRT00000050192.4; ENSPTRP00000044308.3; ENSPTRG00000018023.5.
DR GeneID; 471978; -.
DR KEGG; ptr:471978; -.
DR CTD; 6890; -.
DR VGNC; VGNC:12708; TAP1.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000159023; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; H2R2Q4; -.
DR OMA; FNQFFVG; -.
DR OrthoDB; 5487044at2759; -.
DR TreeFam; TF105197; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000018023; Expressed in spleen and 21 other cell types or tissues.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0042824; C:MHC class I peptide loading complex; IBA:GO_Central.
DR GO; GO:0042825; C:TAP complex; IEA:Ensembl.
DR GO; GO:0015433; F:ABC-type peptide antigen transporter activity; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; 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:0042288; F:MHC class I protein binding; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0046979; F:TAP2 binding; IEA:Ensembl.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IBA:GO_Central.
DR GO; GO:0046967; P:cytosol to endoplasmic reticulum transport; IEA:Ensembl.
DR GO; GO:0006952; P:defense response; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18589; ABC_6TM_TAP1; 1.
DR CDD; cd03248; ABCC_TAP; 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; IPR039421; Type_1_exporter.
DR NCBIfam; TIGR00958; 3a01208; 1.
DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43394:SF15; TRANSPORTER 1, ATP BINDING CASSETTE SUBFAMILY B MEMBER; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR PIRSF; PIRSF002773; ABC_prm/ATPase_B; 1.
DR PRINTS; PR01896; TAP1PROTEIN.
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:UP000002277};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 249..530
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 563..802
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 22..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 87217 MW; D9994E92DF9B5DF6 CRC64;
MAELLASAAS ACSWDFPRAP PSFPPSAASR GGLGGTQSFR PHRGAESPRP GRDRDGVRVP
MASSRCPAPR GCRCLPGASL AWLGTVLLFL ADWVLLRTAL PRIFSLLVPT ALPLLRVWAV
GLSRWAVLWL GACGVLRATV GSKSENAGAQ GWLAALEPLA AALGLALPVL ALFRELISWG
APGSADSTRL LHWGSHPSAF VVSYAAALPA AALWHKLGSL WVPGGQGGSG DSVRRLLGCL
GSETRRLSLF LVLVVLSSLG EMAIPFFTGR LTDWILQDGS ADTFTRNLTL MSILTIASAV
LEFVGDGIYN NTMGHVHSHL QGEVFGAVLR QETEFFQQNQ TGNITSRVTE DTSTLSDSLS
ENLSLFLWYL VRGLCLLGIM LWGSVSLTMV TLVTLPLLFL LPKKVGKWYQ LLEVQVRESL
AKSSQVAIEA LSAMPTVRSF ANEEGEAQKF REKLQEIKTL NQKEAVAYAV NSWTTSISGM
LLKVGILYIG GQLVTSGAVS SGNLVTFVLY QMQFTQAVEV LLSIYPRVQK AVGSSEKIFE
YLDRTPRCPP SGLLTPLHLE GLVQFQDVSF AYPNRPDVLV LQGLTFTLRP GEVTALVGPN
GSGKSTVAAL LQNLYQPTEG QLLLDGKPLP QYEHRYLHRQ VAAVGQEPQV FGRSLQENIA
YGLTQKPTME EITAAAVKSG AHSFISGLPQ GYDTEVGEAG SQLSGGQRQA VALARALIRK
PCVLILDDAT SALDANSQLQ VEQLLYESPE RYSRSVLLIT QHLSLVEQAD HILFLEGGAI
REGGTHQQLM EKKGCYWAMV QAPADAPE
//
