TAP1_GORGO
ID TAP1_GORGO Reviewed; 748 AA.
AC Q28433; Q28432; Q28434;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Antigen peptide transporter 1;
DE Short=APT1;
DE EC=7.4.2.- {ECO:0000250|UniProtKB:Q03518};
DE AltName: Full=ATP-binding cassette sub-family B member 2;
DE AltName: Full=Peptide transporter TAP1;
GN Name=TAP1;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-233; MET-273; SER-619 AND
RP ARG-629.
RC STRAIN=Isolate Machi, and Isolate Oko;
RX PubMed=8891732; DOI=10.1016/0198-8859(96)00137-1;
RA Laud P.R., Loflin P.T., Jeevan A., Lawlor D.A.;
RT "Transporter associated with antigen-processing-1 (TAP1) alleles in Gorilla
RT gorilla: diversification of the locus postspeciation.";
RL Hum. Immunol. 50:91-102(1996).
CC -!- FUNCTION: ABC transporter associated with antigen processing. In
CC complex with TAP2 mediates unidirectional translocation of peptide
CC antigens from cytosol to endoplasmic reticulum (ER) for loading onto
CC MHC class I (MHCI) molecules. Uses the chemical energy of ATP to export
CC peptides against the concentration gradient. During the transport cycle
CC alternates between 'inward-facing' state with peptide binding site
CC facing the cytosol to 'outward-facing' state with peptide binding site
CC facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2
CC induces a switch to hydrolysis-competent 'outward-facing' conformation
CC ready for peptide loading onto nascent MHCI molecules. Subsequently ATP
CC hydrolysis resets the transporter to the 'inward facing' state for a
CC new cycle. As a component of the peptide loading complex (PLC), acts as
CC a molecular scaffold essential for peptide-MHCI assembly and antigen
CC presentation. {ECO:0000250|UniProtKB:Q03518}.
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 Evidence={ECO:0000250|UniProtKB:Q03518};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65973;
CC Evidence={ECO:0000250|UniProtKB:Q03518};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q03518};
CC -!- SUBUNIT: Heterodimer of TAP1 and TAP2 (TAP1-TAP2). A component of the
CC peptide loading complex (PLC), interacts via TAPBP with MHCI
CC heterodimer; this interaction mediates peptide-MHCI assembly. Interacts
CC with PSMB5 and PSMB8. {ECO:0000250|UniProtKB:Q03518}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q03518}; Multi-pass membrane protein
CC {ECO:0000255}. Note=The transmembrane segments seem to form a pore in
CC the membrane.
CC -!- DOMAIN: The peptide-binding site is shared between the cytoplasmic
CC loops of TAP1 and TAP2. {ECO:0000250|UniProtKB:Q03518}.
CC -!- DOMAIN: The nucleotide-binding domain (NBD) mediates ATP hydrolysis
CC coupled to peptide translocation. Two ATP molecules are accommodated at
CC distinct nucleotide binding sites (NBS) at TAP1-TAP2 dimer interface.
CC Each NBS is formed by Walker A (GxxGxGKST) and Q-loop motifs from NBD
CC of one subunit, while the NBD from the second subunit completes the
CC active site by contributing the C loop motif (LSGGQ). Each ATP molecule
CC is coordinated via the beta- and gamma-phosphates to a Mg2+ ion, which
CC is necessary for ATP hydrolysis. {ECO:0000250|UniProtKB:P36370}.
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; L76468; AAA91199.1; -; mRNA.
DR EMBL; L76469; AAA91200.1; -; mRNA.
DR EMBL; L76470; AAA91198.1; -; mRNA.
DR AlphaFoldDB; Q28433; -.
DR SMR; Q28433; -.
DR STRING; 9593.ENSGGOP00000010681; -.
DR eggNOG; KOG0058; Eukaryota.
DR InParanoid; Q28433; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0042824; C:MHC class I peptide loading complex; IBA:GO_Central.
DR GO; GO:0042825; C:TAP complex; IEA:InterPro.
DR GO; GO:0015433; F:ABC-type peptide antigen transporter activity; IBA:GO_Central.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042287; F:MHC protein binding; IEA:InterPro.
DR GO; GO:0046978; F:TAP1 binding; IBA:GO_Central.
DR GO; GO:0046979; F:TAP2 binding; IEA:InterPro.
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:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; IEA:InterPro.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
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; 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; IPR013306; Tap1/ABCB2.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR PANTHER; PTHR24221:SF249; PTHR24221:SF249; 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 TIGRFAMs; TIGR00958; 3a01208; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; ATP-binding; Endoplasmic reticulum; Immunity; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Peptide transport;
KW Protein transport; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..748
FT /note="Antigen peptide transporter 1"
FT /id="PRO_0000093325"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 37..53
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..76
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 77..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 114..133
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 155..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 208..227
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 249..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 320..328
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 350..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 440..443
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 465..748
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 187..470
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 503..742
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 375..420
FT /note="Part of the peptide-binding site"
FT /evidence="ECO:0000250|UniProtKB:Q03518"
FT REGION 453..487
FT /note="Part of the peptide-binding site"
FT /evidence="ECO:0000250|UniProtKB:Q03518"
FT BINDING 538..546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P36370,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 545
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q03518"
FT BINDING 641..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P36370"
FT BINDING 701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P36370"
FT SITE 32
FT /note="Inter-subunit salt bridge with TAPBP"
FT /evidence="ECO:0000250|UniProtKB:Q03518"
FT VARIANT 233
FT /note="I -> V (in allele Gogo-TAP1b)"
FT /evidence="ECO:0000269|PubMed:8891732"
FT /id="VAR_019127"
FT VARIANT 273
FT /note="T -> M (in allele Gogo-TAP1b)"
FT /evidence="ECO:0000269|PubMed:8891732"
FT /id="VAR_019128"
FT VARIANT 619
FT /note="C -> S (in allele Gogo-TAP1b)"
FT /evidence="ECO:0000269|PubMed:8891732"
FT /id="VAR_019129"
FT VARIANT 629
FT /note="P -> R (in allele Gogo-TAP1c)"
FT /evidence="ECO:0000269|PubMed:8891732"
FT /id="VAR_019130"
SQ SEQUENCE 748 AA; 80880 MW; D834F6DA0AD6217B CRC64;
MASSRCPAPR GCRCLPGASL AWLGTVLLFL ADWVLLRTAL PRIFSLLVPT ALPLLRVWAV
GLSRWAVLWL GACGVLRATV GSKSENAGAQ GWLAALEPLA AALGLALPGL ALFRELISWG
APGSADSTRL LHWGSHPSAF VVSYAAALPA AALWHKLGSL WVPGGQGGSG NPVRRLLGCL
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 LQGLTFTLHP GEVTALVGPN
GSGKSTVAAL LQNLYQPTGG QLLLDGKPLP QYEHRYLHRQ VAAVGQEPQV FGRSLQENIA
YGLTQKPTME EITAAAVKCG AHSFISGLPQ GYDTEVGEAG SQLSGGQRQA VALARALIRK
PCVLILDDAT SALDANSQLQ VEQLLYESPE RYSRSVLLIT QHLSLVEQAD HILFLEGGAI
REGGTHQQLM EKKGCYWAMV QAPADAPE
